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Patent US20080045444 - Compositions and methods for treating cardiovascular disease and myocardial ... - Google PatentsSearch Images Maps Play YouTube News Gmail Drive More »Sign inAdvanced Patent SearchPatentsThe present invention describes compositions and methods for treating cardiovascular disease and myocardial infarction using dipeptidyl peptidase inhibitors. Also provided are methods for increasing natriuretic peptide function by administering one or more analogues of B type natriuretic peptide that...http://www.google.com/patents/US20080045444?utm_source=gb-gplus-sharePatent US20080045444 - Compositions and methods for treating cardiovascular disease and myocardial infarction with dipeptidyl peptidase inhibitors or b type natriuretic peptide analogues resistant to prolyl-specific dipeptidyl degradationAdvanced Patent SearchPublication numberUS20080045444 A1Publication typeApplicationApplication numberUS 11/560,425Publication dateFeb 21, 2008Filing dateNov 16, 2006Priority dateAug 20, 2003Also published asCA2579802A1, DE602005019175D1, EP1786931A2, EP1786931A4, EP1786931B1, US7524635, US20050148024, US20090275512, WO2006029369A2, WO2006029369A3Publication number11560425, 560425, US 2008/0045444 A1, US 2008/045444 A1, US 20080045444 A1, US 20080045444A1, US 2008045444 A1, US 2008045444A1, US-A1-20080045444, US-A1-2008045444, US2008/0045444A1, US2008/045444A1, US20080045444 A1, US20080045444A1, US2008045444 A1, US2008045444A1InventorsMichael WhittakerOriginal AssigneeBiosite IncorporatedExport CitationBiBTeX, EndNote, RefManReferenced by (22), Classifications (23), Legal Events (3) External Links: USPTO, USPTO Assignment, EspacenetCompositions and methods for treating cardiovascular disease and myocardial infarction with dipeptidyl peptidase inhibitors or b type natriuretic peptide analogues resistant to prolyl-specific dipeptidyl degradation
This application is a continuation of Ser. No. 10/938,760 filed Sep. 9, 2004, which is a continuation-in-part of U.S. patent application Ser. No. 10/645,874 filed Aug. 20, 2003, which claims priority to U.S. Provisional Patent Application No. 60/642,086 filed Feb. 4, 2004, from each of which priority is claimed, and each of which is hereby incorporated by reference in its entirety, including all tables, figures, and claims.
FIELD OF THE INVENTION The present invention relates to medical diagnostics and therapeutics. BACKGROUND OF THE INVENTION The following discussion of the background of the invention is merely provided to aid the reader in understanding the invention and is not admitted to describe or constitute prior art to the present invention. Natriuretic peptides are a group of naturally occurring substances that act in the body to oppose the activity of the renin-angiotensin system. There are three major natriuretic peptides: atrial natriuretic peptide (ANP), which is synthesized in the atria; brain-type natriuretic peptide (BNP), which is synthesized in the ventricles; and C-type natriuretic peptide (CNP), which is synthesized in the brain. Mature human A-type natriuretic peptide (ANP) (also referred to as atrial natriuretic peptide) is a biologically active 28 amino acid peptide that is synthesized, stored, and released by atrial myocytes in response to atrial distension, angiotensin II stimulation, endothelin, and sympathetic stimulation (beta-adrenoceptor mediated). Mature ANP is generated by proteolytic cleavage of a 128 amino acid precursor molecule (pro-ANP), yielding the biologically active 28 amino acid peptide representing amino acids 99-126 of the pro-ANP molecule (ANP99-126). Linear peptide fragments from the N-terminal prohormone segment have also been reported to have biological activity. Mature human B-type natriuretic peptide (BNP) (also called brain-type natriuretic peptide) is a 32 amino acid, 4 kDa biologically active peptide that is involved in the natriuresis system to regulate blood pressure and fluid balance (Bonow, R. O., Circulation 93:1946-1950, 1996). The mature BNP hormone is generated by proteolytic cleavage of a 108-amino acid precursor molecule, referred to herein as “pro-BNP.” Cleavage generates t a 76-amino acid N-terminal peptide (amino acids 1-76), referred to as “NT pro BNP,” and the 32-amino acid mature hormone, referred to as BNP or BNP 32 (amino acids 77-108). It has been suggested that each of these species—NT pro-BNP, BNP-32, and the pre-pro-BNP—can circulate in human plasma (Tateyama et al., Biochem. Biophys. Res. Commun. 185:760-7, 1992; Hunt et al., Biochem. Biophys. Res. Commun. 214:1175-83, 1995). Mature human C-type natriuretic peptide (CNP) a 22-amino acid peptide that is the primary active natriuretic peptide in the human brain; CNP is also considered to be an endothelium-derived relaxant factor, which acts in the same way as nitric oxide (NO) (Davidson et al, Circulation 93:1155-9, 1996). CNP is structurally related to A-type natriuretic peptide (ANP) and B-type natriuretic peptide (BNP); however, while ANP and BNP are synthesized predominantly in the myocardium, CNP is synthesized in the vascular endothelium as a precursor (pro-CNP) (Prickett et al., Biochem. Biophys. Res. Commun. 286:513-7, 2001). CNP is thought to possess vasodilator effects on both arteries and veins and has been reported to act mainly on the vein by increasing the intracellular cGMP concentration in vascular smooth muscle cells. ANP and BNP are released in response to atrial and ventricular stretch, respectively, and will cause vasorelaxation, inhibition of aldosterone secretion in the adrenal cortex, and inhibition of renin secretion in the kidney. Both ANP and BNP will cause natriuresis and a reduction in intravascular volume, effects amplified by the antagonism of antidiuretic hormone (ADH). The physiologic effects of CNP differ from those of ANP and BNP; CNP has a hypotensive effect, but no significant diuretic or natriuretic actions. Increased blood levels of natriuretic peptides have been found in certain disease states, suggesting a role in the pathophysiology of those diseases, including stroke, congestive heart failure (CHF), cardiac ischemia, systemic hypertension, and acute myocardial infarction. See, e.g., WO 02/089657; WO 02/083913; and WO 03/016910, each of which is hereby incorporated in its entirety, including all tables, figures, and claims. Numerous non-human homologs of the natriuretic peptides are known to those of skill in the art. The natriuretic peptides, alone, collectively, and/or together with additional proteins, can serve as disease markers and indicators of prognosis in various cardiovascular conditions. For example, BNP, which is synthesized in the cardiac ventricles and correlates with left ventricular pressure, amount of dyspnea, and the state of neurohormonal modulation, makes this peptide the first potential marker for heart failure. Measurement of plasma BNP concentration is evolving as a very efficient and cost effective mass screening technique for identifying patients with various cardiac abnormalities regardless of etiology and degree of LV systolic dysfunction that can potentially develop into obvious heart failure and carry a high risk of a cardiovascular event. Finding a simple blood test that would aid in the diagnosis and management of patients with CHF clearly would have a favorable impact on the staggering costs associated with the disease. Removal of the natriuretic peptides from the circulation is affected mainly by binding to clearance receptors and enzymatic degradation in the circulation. See, e.g., Cho et al., Heart Dis. 1: 305-28, 1999; Smith et al., J. Endocrinol. 167: 239-46, 2000. Additionally, human pro-BNP is reported to be processed in serum such that circulating pre-pro-BNP is unlikely to be the intact 108 amino acid form. Hunt et al., Peptides 18: 1475-81, 1997. Degradation of the natriuretic peptides is believed mediated by neutral endopeptidase. For example, Norman et al. (Biochem. Biophys. Res. Commun. 28: 175: 22-30, 1991) report that neutral endopeptidase can cleave human BNP between residues 2 and 3, between residues 4 and 5, and between residues 17 and 18. Similarly, Lindberg and Andersson (Regul. Pept. 47: 53-63, 1993) report that human ANP is cleaved between residues 3 and 4 and residues 14 and 15. The biological activity of this hydrolyzed product was about 500-fold less than intact ANP. Additionally, Knecht et al. (Life Sci. 71: 2701-12, 2002) report that renal neutral endopeptidase is upregulated in heart failure, a condition where natriuretic peptide levels are increased. For this reason, neutral endopeptidase has been targeted for inhibition in treatment of cardiovascular disease. See, e.g., Corti et al., Circulation 104: 1856-62, 2001. Confusion over the stability of the natriuretic peptides, particularly in blood-derived samples (e.g., serum, plasma, whole blood) has been reported. ANP is reported to be a better substrate for neutral endopeptidase than is BNP. Similarly, Shimizu et al. (Clin, Chem. Acta 305: 181-6, 2001), Gobinet-Georges et al. (Clin. Chem. Lab. Med. 38: 519-23, 2000) and Murdoch et al. (Heart 78: 594-7, 1997) report that BNP is stable in certain blood-derived samples or when blood is collected under certain conditions. A more recent report by Shimizu et al. (Clin. Chem. Acta 316: 129-35, 2002) indicates that 94% of BNP in whole blood was a digested form in which 2 amino terminal residues had been removed; and that BNP in plasma was degraded to a number of unidentified forms. BRIEF SUMMARY OF THE INVENTION The present invention relates in part to compositions and methods designed to determine the presence or amount of biologically active natriuretic peptides, or their fragments, in a sample. The degradation of natriuretic peptides is an ongoing process that may be a function of, inter alia, the elapsed time between onset of an event triggering natriuretic peptide release into the tissues and the time the sample is obtained or analyzed; the quantity of proteolytic enzymes present; etc. This degradation can produce circulating amounts of natriuretic peptides having reduced or lost biological function (referred to herein for convenience as “inactive fragments” of a natriuretic peptide). Failure to consider this degradation when designing an assay for one or more natriuretic peptides may result in an assay that detects both biologically active forms of a natriuretic peptide(s) of interest, as well as inactive fragments of the natriuretic peptide(s). This may lead to the conclusion that an assay shows particularly good stability (i.e., the analyte of interest is not lost to the assay during sample storage), when in fact the natriuretic peptide of interest is actually being degraded to an inactive fragment and the assay result is confounded by the inability to distinguish the intended analyte from the pool of inactive fragments originally present in the sample. Because the biologically active forms may be more relevant to the physiologic state of the subject, and because upregulated proteolytic enzymes in diseased subjects may lead to particularly large pools of inactive fragments in the subjects of potentially the greatest interest, the compositions and methods described herein may provide improved diagnostic and prognostic information to the artisan in comparison to assays that are not specific for the biologically active forms. The methods and compositions described herein can meet the need in the art for rapid, sensitive and specific diagnostic assay to be used in the diagnosis and differentiation of various cardiovascular diseases, including stroke, congestive heart failure (CHF), cardiac ischemia, systemic hypertension, and/or acute myocardial infarction. Moreover, the methods and compositions of the present invention can also be used to facilitate the treatment of patients and the development of additional diagnostic and/or prognostic indicators and indicator panels. In a first aspect then, the present invention relates to methods for detecting the presence or amount of a natriuretic peptide in a sample, comprising performing an assay that detects a biologically active natriuretic peptide, but that exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, one or more biologically inactive fragments of the natriuretic peptide. Biologically inactive fragments may include those in which residues from either or both of the N-terminus or C-terminus of the biologically active natriuretic peptide have been removed, and/or in which the loop formed by intramolecular disulfide bonding of the natriuretic peptide has been cleaved. Such biologically inactive fragments may be formed, for example, by cleaving one or more peptide bonds in the biologically active natriuretic peptide. In related aspects, the present invention relates to methods for detecting the presence or amount of a natriuretic peptide in a sample, comprising performing an assay that detects an intact natriuretic peptide, but that exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, an equimolar amount of a peptide that is generated when a portion, and preferably at least an N-terminal portion, of the intact natriuretic peptide is removed. In various embodiments, the present invention relates to methods for detecting the presence or amount of BNP in a sample, comprising performing an assay that detects BNP77-108, but that exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, an equimolar amount of BNP94-108; the assay detects BNP77-108, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, BNP90-108; the assay detects BNP77-108, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, BNP81-108; the assay detects BNP77-108, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, BNP79-108; the assay detects BNP77-108, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, BNP77-106; and/or the assay detects BNP77-108, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, BNP79-106. In various additional embodiments, the present invention relates to methods for detecting the presence or amount of BNP in a sample, comprising performing an assay that detects BNP1-76, but that exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, an equimolar amount of BNP38-76; the assay detects BNP1-76, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, BNP24-76; the assay detects BNP1-76, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, BNP12-76; the assay detects BNP1-76, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, BNP3-76; the assay detects BNP1-76, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, BNP1-73; and/or the assay detects BNP1-76, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, BNP3-73. In still other additional embodiments, the present invention relates to methods for 6detecting the presence or amount of ANP in a sample, comprising performing an assay that detects ANP99-126, but that exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, an equimolar amount of ANP113-126; the assay detects ANP99-126, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, ANP105-126; the assay detects ANP99-126, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, ANP102-126; the assay detects ANP99-126, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, ANP99-124; and/or the assay detects ANP99-126, but exhibits at least a 5-fold reduction in signal from, and preferably does not appreciably detect, ANP102-124. As described hereinafter, such assays may be designed in a variety of ways known to those of skill in the art. Preferred assays are immunoassays, although other methods are well known to those skilled in the art (for example, the use of biosensors, or the use of natural receptors for natriuretic peptides that are known in the art). Any suitable immunoassay may be utilized, for example, assays which directly detect analyte binding (e.g., by ellipsometric detection), enzyme-linked immunoassays (ELISA), radioimmunoassays (RIAs), competitive binding assays, sandwich immunoassays, and the like. Specific immunological binding of the antibody to the one or more natriuretic peptide fragments can be detected directly or indirectly. Direct labels include fluorescent or luminescent tags, metals, dyes, radionuclides, and the like, attached to the antibody. Indirect labels include various enzymes well known in the art, such as alkaline phosphatase, horseradish peroxidase and the like. Antibodies attached to a second molecule, such as a detectable label, are referred to herein as “antibody conjugates.” The skilled artisan will also understand that natural receptors for the natriuretic peptides exist, and that these receptors may also be used in a manner akin to antibodies in providing binding assays. Immunoassays may be formulated using one or more antibodies selected to bind to an epitope that is partially or completely lost from biologically inactive fragments of the natriuretic peptide as compared to the intact natriuretic peptide. For example, in a sandwich assay, if an antibody bound to a solid phase is selected to bind preferentially to the N-terminal portion of the molecule, and a labeled antibody is selected to bind to the C-terminal portion of the molecule, only those molecules that contain both the N- and C-terminal portions of the molecule will be detected in the assay. Alternatively, both the solid phase and labeled antibodies may be selected to bind to the N-terminal portion of the molecule. The skilled artisan will understand that cleavage of the natriuretic peptide may remove all of the epitope to which an antibody binds (e.g., the antibody binds to the N-terminal region alone). Alternatively, an epitope may be formed from portions of the natriuretic peptide that are not contiguous in the linear sequence of the molecule, but that are associated in 3-dimensional space in solution, so that epitope comprises more than the described amino acid residues, but removal of the region described amino acid residues results in reduced binding of the antibody, and hence a loss of signal in the assay. In certain embodiments, antibodies are selected, based not upon a particular affinity for one or more natriuretic peptide(s), but instead based upon a signal that is obtainable in a binding assay such as an immunoassay. The skilled artisan will recognize that various binding assay formats are known in the art, and that it is often the use of antibodies to formulate an appropriate assay that is more important than a particular affinity of an antibody for one or more target molecules. For example, competitive binding assays may comprise a receptor (e.g., an antibody) bound to a solid surface. An analyte of interest in a test sample competes for binding with a labeled molecule that also binds to the receptor. The amount of labeled molecule bound to the receptor (and hence assay signal) is inversely proportional to the amount of analyte of interest in the test sample. In this case, a single antibody attached to the solid phase is used. Alternatively, in a sandwich immunoassay, a first antibody, typically bound to a solid surface, and a second antibody, typically conjugated to a detectable label, each bind to an analyte of interest in a test sample. The amount of labeled molecule bound to the receptor (and hence assay signal) is directly proportional to the amount of analyte of interest in the test sample. The immunoassays of the present invention are preferably designed to distinguish a biologically active natriuretic peptide from a biologically inactive natriuretic peptide and/or an intact natriuretic peptide from a natriuretic peptide fragment. For example, a preferred immunoassay would distinguish a natriuretic peptide comprising an intact N-terminal region from a fragment of the natriuretic peptide from which the N-terminal region has been lost. An immunoassay is said to “distinguish” between a first group of polypeptides and a second group of polypeptides if the immunoassay provides a signal related to binding of the first group of polypeptides that is at least a factor of 5 greater than a signal obtained from an equal number of molecules of the second group of polypeptides under the same assay conditions, when the assay is performed at no more than twice the amount of the first group of polypeptides necessary to obtain a maximum signal. More preferably, the signal is at least a factor of 10 greater, even more preferably at least a factor of 20 greater, and most preferably at least a factor of 50 greater, at least a factor of 100 greater, or more under such assay conditions. An assay does not “appreciably detect” the second group of polypeptides if a signal related to binding of the first group of polypeptides may be obtained, but no signal above background is obtained from an equal number of molecules of the second group of polypeptides under such assay conditions. In another aspect, the present invention relates to methods for detecting the presence or amount of a natriuretic peptide in a sample, comprising performing an assay in which the signal depends upon an antibody that specifically binds to a biologically active natriuretic peptide, but that does not specifically bind to biologically inactive fragments of the natriuretic peptide. As discussed above, biologically inactive fragments may include those in which residues from either or both of the N-terminus or C-terminus of the intact natriuretic peptide have been removed, and/or in which the loop formed by intramolecular disulfide bonding of the natriuretic peptide has been cleaved. In preferred embodiments, the assay is performed under conditions in which the signal depends upon an antibody that specifically binds to the intact natriuretic peptide, but that does not specifically bind to a peptide that is generated from the natriuretic peptide when an N-terminal portion of the natriuretic peptide is removed. In related aspects, the present invention relates to methods for detecting the presence or amount of a natriuretic peptide in a sample, comprising performing an assay in which the signal depends upon an antibody that specifically binds to the intact natriuretic peptide, but that does not specifically bind to fragments of the natriuretic peptide generated when a portion, and preferably at least an N-terminal portion, of the natriuretic peptide is removed. In various embodiments, the present invention relates to methods for detecting the presence or amount of BNP in a sample, comprising performing an assay in which the signal depends upon an antibody that specifically binds to BNP77-108, but that does not specifically bind to BNP94-108; the assay depends upon an antibody that specifically binds to BNP77-108, but does not specifically bind to BNP90-108; the assay depends upon an antibody that specifically binds to BNP77-108, but does not specifically bind to BNP81-108; the assay depends upon an antibody that specifically binds to BNP77-108, but does not specifically bind to BNP79-108; the assay depends upon an antibody that specifically binds to BNP77-108, but does not specifically bind to BNP77-106; and/or the assay depends upon an antibody that specifically binds to BNP77-108, but does not specifically bind to BNP79-106. In various additional embodiments, the present invention relates to methods for detecting the presence or amount of BNP in a sample, comprising performing an assay in which the signal depends upon an antibody that specifically binds to BNP1-76, but that does not specifically bind to BNP38-76; the assay depends upon an antibody that specifically binds to BNP1-76, but does not specifically bind to BNP24-76; the assay depends upon an antibody that specifically binds to BNP1-76, but does not specifically bind to BNP12-76; the assay depends upon an antibody that specifically binds to BNP1-76, but does not specifically bind to BNP3-76; the assay depends upon an antibody that specifically binds to BNP1-76, but does not specifically bind to BNP1-73; and/or the assay depends upon an antibody that specifically binds to BNP1-76, but does not specifically bind to BNP3-73. In other additional embodiments, the present invention relates to methods for detecting the presence or amount of ANP in a sample, comprising performing an assay in which the signal depends upon an antibody that specifically binds to ANP99-126, but that does not specifically bind to ANP113-126; the assay depends upon an antibody that specifically binds to ANP99-126, but that does not specifically bind to ANP105-126; the assay depends upon an antibody that specifically binds to ANP99-126, but that does not specifically bind to ANP102-126; the assay depends upon an antibody that specifically binds to ANP99-126, but that does not specifically bind to ANP99-124; and/or the assay depends upon an antibody that specifically binds to ANP99-126, but that does not specifically bind to ANP102-124. A signal from an immunoassay is said to “depend upon binding to an antibody” if the antibody participates in formation of a complex necessary to generate the signal. For example, in a sandwich immunoassay formulated using a solid phase antibody and a second antibody conjugate, each of which must bind to an analyte to form the sandwich, each of the solid phase antibody and second antibody participate in formation of the complex necessary to generate the signal. In a competitive immunoassay where a single antibody is used, and an analyte competes with an analyte conjugate for binding, the single antibody participates in formation of the complex necessary to generate the signal. The skilled artisan will understand that numerous additional immunoassay formulations may be provided. The assay methods described herein may also comprise a step of storing a sample for a period of time prior to assay for one or more natriuretic peptides. Because degradation of natriuretic peptides may be an ongoing process during storage, the storage considerations should be selected to reduce loss of the N-terminal portion of the molecule. Thus, the storage conditions may comprise addition of one or more inhibitors of natriuretic peptide degradation. As discussed hereinafter, the storage conditions may comprise one or more inhibitors of neutral endopeptidase and/or one or more inhibitors of prolyl-specific dipeptidyl peptidase. Such inhibitors are well known in the art. See, e.g., Corti et al., Circulation 104: 1856-62, 2001; Senten et al., J. Comb. Chem. 5: 336-44, 2003; Senten et al., Bioorg. Med. Chem. Lett. 12: 2825-8, 2002. In an alternative or in conjunction with such inhibitors, storage conditions may comprise storage at a reduced temperature, preferably below the freezing point of the sample. In another aspect, the present invention relates to an assay device configured and arranged to perform the described assays. Devices for performing the assays described herein preferably contain a plurality of discrete, independently addressable locations, or “diagnostic zones,” each of which is related to a particular analyte or set of analytes of interest, one or more of which is a natriuretic peptide. For example, each of a plurality of discrete zones may comprise a receptor (e.g., an antibody) for binding a different analyte. Following reaction of a sample with the devices, a signal is generated from the diagnostic zone(s), which may then be correlated to the presence or amount of the peptide of interest. In yet another aspect, the presence or amount of one or more natriuretic peptide(s) of interest measured by the methods described herein may be related to the presence or absence of a disease, or a disease prognosis (e.g., the likelihood of a future adverse outcome related to a disease). Preferred diseases include various cardiovascular and cerebrovascular diseases, including stroke, congestive heart failure (CHF), cardiac ischemia, systemic hypertension, and/or acute myocardial infarction. These methods preferably comprise determining the presence or amount of one or more natriuretic peptide(s) by the methods described herein, and relating that presence or amount to the disease or prognosis of interest. In certain embodiments, the signal obtained from an assay need not be related to the presence or amount of one or more natriuretic peptide(s); rather, the signal may be directly related to the presence or absence of a disease, or the likelihood of a future adverse outcome related to a disease. For example, a level of signal x may indicate that y pg/mL of a natriuretic peptide is present in the sample. A table may then indicate that y pg/mL of that natriuretic peptide indicates congestive heart failure. It may be equally valid to simply relate a level of signal x directly to congestive heart failure, without determining how much of the natriuretic peptide is present. Such a signal is preferably obtained from an immunoassay using the antibodies of the present invention, although other methods are well known to those skilled in the art. In still another aspect, the present invention relates to methods for selecting one or more antibodies for use in an assay for natriuretic peptide(s). These methods comprise selecting antibodies that, when used in an assay, detect a biologically active natriuretic peptide of interest, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, biologically inactive fragments of the natriuretic peptide. As above, biologically inactive fragments may include those in which residues from either or both of the N-terminus or C-terminus of the intact natriuretic peptide have been removed, and/or in which the loop formed by intramolecular disulfide bonding of the natriuretic peptide has been cleaved. In related aspects, the present invention relates to methods for for selecting one or more antibodies for use in an assay, comprising selecting antibodies that, when used in an assay, detect an intact natriuretic peptide of interest, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, an equimolar amount of a peptide that is generated from the natriuretic peptide when a portion, and preferably an N-terminal portion, of the natriuretic peptide is removed. In various embodiments, the methods comprise selecting one or more antibodies that detect BNP77-108 when used in an assay, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, an equimolar amount of BNP94-108; selecting one or more antibodies that detect BNP77-108, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, BNP90-108; selecting one or more antibodies that detect BNP77-108, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, BNP81-108; selecting one or more antibodies that detect BNP77-108, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, BNP79-108; selecting one or more antibodies that detect BNP77-108, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, BNP77-106; and/or selecting one or more antibodies that detect BNP77-108, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, BNP79-106. In various additional embodiments, the methods comprise selecting one or more antibodies that detect BNP1-76, when used in an assay, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, an equimolar amount of BNP38-76; selecting one or more antibodies that detect BNP1-76, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, BNP24-76; selecting one or more antibodies that detect BNP1-76, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, BNP12-76; selecting one or more antibodies that detect BNP1-76, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, BNP3-76; selecting one or more antibodies that detect BNP1-76, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, BNP1-73; and/or selecting one or more antibodies that detect BNP1-76, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, BNP3-73. In other additional embodiments, the methods comprise selecting one or more antibodies that detect ANP99-126 when used in an assay, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, an equimolar amount of ANP113-126; selecting one or more antibodies that detect ANP99-126 when used in an assay, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, an equimolar amount of ANP105-126; selecting one or more antibodies that detect ANP99-126 when used in an assay, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, an equimolar amount of ANP101-126; selecting one or more antibodies that detect ANP99-126 when used in an assay, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, an equimolar amount of ANP99-124; and/or selecting one or more antibodies that detect ANP99-126 when used in an assay, but that exhibit at least a 5-fold reduction in signal from, and preferably do not appreciably detect, an equimolar amount of ANP101-124. In other related aspects, the present invention relates to a method of selecting one or more antibodies for use in an assay for natriuretic peptide(s). The methods comprise selecting one or more antibodies that specifically bind to a biologically active natriuretic peptide, but that do not specifically bind to biologically inactive fragments of the natriuretic peptide. As discussed above, biologically inactive fragments may include those in which residues from either or both of the N-terminus or C-terminus of the intact natriuretic peptide have been removed, and/or in which the loop formed by intramolecular disulfide bonding of the natriuretic peptide has been cleaved. In preferred embodiments, the assay is performed under conditions in which the signal depends upon an antibody that specifically binds to the intact natriuretic peptide, but that does not specifically bind to a peptide that is generated from the natriuretic peptide when an N-terminal portion of the natriuretic peptide is removed In still other related aspects, the present invention relates to methods for for selecting one or more antibodies for use in an assay, comprising selecting antibodies that specifically bind to the intact natriuretic peptide, but that do not specifically bind to biologically inactive fragments of the natriuretic peptide generated when an N-terminal portion of the natriuretic peptide is removed. In various embodiments, the methods comprise selecting one or more antibodies that specifically bind to BNP77-108, but that do not specifically bind to BNP94-108; selecting one or more antibodies that specifically bind to BNP77-108, but that do not specifically bind to BNP90-108; selecting one or more antibodies that specifically bind to BNP77-108, but that do not specifically bind to BNP81-108; selecting one or more antibodies that specifically bind to BNP77-108, but that do not specifically bind to BNP79-108; selecting one or more antibodies that specifically bind to BNP77-108, but that do not specifically bind to BNP77-106; and/or selecting one or more antibodies that specifically bind to BNP77-108, but that do not specifically bind to BNP79-106. In various additional embodiments, the methods comprise selecting one or more antibodies that specifically bind to BNP1-76, but that do not specifically bind to BNP38-76; selecting one or more antibodies that specifically bind to BNP1-76, but that do not specifically bind to BNP24-76; selecting one or more antibodies that specifically bind to BNP1-76, but that do not specifically bind to BNP12-76; selecting one or more antibodies that specifically bind to BNP1-76, but that do not specifically bind to BNP3-76; selecting one or more antibodies that specifically bind to BNP1-76, but that do not specifically bind to BNP1-73; and/or selecting one or more antibodies that specifically bind to BNP1-76, but that do not specifically bind to BNP3-73. In other additional embodiments, th


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Patent US6104530 - Transparent laminates and optical filters for displays using same - Google PatentsSearch Images Maps Play YouTube News Gmail Drive More »Sign inAdvanced Patent SearchPatentsTransparent laminates which have high transparency and, moreover, excellent electromagnetic shielding characteristics and near-infrared cutting-off characteristics, and optical filters for displays using these transparent laminates. These transparent laminates are formed by laminating a transparent electrically...http://www.google.com/patents/US6104530?utm_source=gb-gplus-sharePatent US6104530 - Transparent laminates and optical filters for displays using sameAdvanced Patent SearchPublication numberUS6104530 APublication typeGrantApplication numberUS 08/863,562Publication dateAug 15, 2000Filing dateMay 27, 1997Priority dateMay 28, 1996Fee statusPaidAlso published asDE69738228D1, DE69738228T2, EP0810452A2, EP0810452A3, EP0810452B1, EP1901095A1Publication number08863562, 863562, US 6104530 A, US 6104530A, US-A-6104530, US6104530 A, US6104530AInventorsTomoyuki Okamura, Fumiharu Yamazaki, Shin Fukuda, Ryu Oi, Masaaki Yoshikai, Masato KoyamaOriginal AssigneeMitsui Chemicals, Inc.Export CitationBiBTeX, EndNote, RefManPatent Citations (10), Non-Patent Citations (2), Referenced by (85), Classifications (13), Legal Events (6) External Links: USPTO, USPTO Assignment, EspacenetTransparent laminates and optical filters for displays using same
US 6104530 AAbstract
Transparent laminates which have high transparency and, moreover, excellent electromagnetic shielding characteristics and near-infrared cutting-off characteristics, and optical filters for displays using these transparent laminates. These transparent laminates are formed by laminating a transparent electrically conductive layer composed of high-refractive-index transparent film layers (B) and metal film layers (C) consisting of silver or a silver-containing alloy on one major surface of a transparent substrate (A) in such a way that a repeating unit comprising a combination of one high-refractive-index transparent film layer (B) and one metal film layer (C) is laminated three times or more, and further laminating one high-refractive-index transparent film layer (B) thereon. The transparent laminate has a sheet resistance of not greater than 3 Ω/sq., a visible light transmittance of not less than 50%, and a light transmittance of not greater than 20% in a wavelength region longer than 820 nm. Optical filters for displays which serve to block leakage electromagnetic waves and near-infrared light from plasma displays can be acquired by using such a transparent laminate.
1. An optical filter for plasma displays which blocks electromagnetic waves and near-infrared radiation emerging from the plasma display, said optical filter comprising:a transparent laminate formed by laminating high-refractive-index transparent film layers and metal film layers consisting of silver or a silver-containing alloy on one surface of a transparent substrate in such a way that a repeating unit comprising a combination of one high-refractive-index transparent film layer and one metal film layer in this order is repeatedly laminated from three times to six times, and further laminating at least a high-refractive-index transparent film layer thereon; wherein a sheet resistance of an electrically conductive surface of a topmost surface of the transparent laminate is not greater than 3 ohm/sq., and said transparent laminate has a visible light transmittance of not less than 50%, and a light transmittance of not great than 20% at any wavelength between 820 nm and 1000 nm; a metal containing electrode electrically connected to the electrically conductive surface; and the transparent laminate contains a dye which is near-infrared absorbing dye and/or a toning dye which has an absorption band in the visible region. 2. An optical filter for plasma displays as claimed in claim 1, wherein said optical filter has a transparent protective layer which is directly formed on the electrically conductive surface or formed on the electrically conductive surface via one of a transparent tacky material layer and a transparent adhesive layer, said optical filter has optical design of the transparent laminate such that the resulting increase in visible light reflectance of the electrically conductive surface is not greater than 2% when the transparent protective layer is directly formed on the electrically conductive surface or formed on the electrically conductive surface via one of a transparent tacky material layer and a transparent adhesive layer.
It is an object of the present invention to provide a transparent laminate having high transparency and, moreover, excellent electromagnetic shielding characteristics and near-infrared blocking characteristics.
FIG. 1 is a plan view of an optical filter for displays in accordance with a preferred embodiment of the present invention as viewed from the display side;
The transparent laminate of the present invention is formed by laminating high-refractive-index transparent film layers and film layers consisting of silver or a silver-containing alloy (hereinafter referred to as metal film layers) successively on one major surface of a transparent substrate in such a way that a repeating unit comprising a combination of one high-refractive-index transparent film layer and one metal film layer is repeatedly laminated three times or more, and further laminating at least a high-refractive-index transparent film layer (B) thereon, and having a sheet resistance of not greater than 3 Ω/sq., a visible light transmittance of not less than 50%, and a light transmittance of not greater than 20% in a wavelength region longer than 820 nm.
The present invention is further illustrated by the following examples. However, these examples are not to be construed to limit the scope of the invention. The film thicknesses given in the following examples and comparative examples are values obtained from the relationship between the film thickness and the film-forming time as determined previously under the same film-forming conditions, and are not values obtained by actually measuring the thicknesses of the films formed in these examples and comparative examples.
According to a magnetron DC sputtering process, an ITO film (40 nm thick), a silver film (10 nm thick), an ITO film (80 nm thick), a silver film (15 nm thick), an ITO film (80 nm thick), a silver film (10 nm thick) and an ITO film (40 nm thick) were laminated, in that order, on one major surface of a biaxially stretched polyethylene terephthalate film (50 μm thick). Thus, a transparent laminate in accordance with the present invention, having three metal film layers and four high-refractive-index transparent film layers, was formed. The ITO films constituted the high-refractive-index transparent film layers, and the silver films constituted the metal film layers. The ITO films were formed by using an indium oxide/tin oxide sintered body [composed of In2 O3 and SnO2 in a ratio of 90:10 (wt. %)] as the target and an argon-oxygen gaseous mixture (with a total pressure of 266 mPa and a partial pressure of oxygen of 5 mPa) as the sputtering gas. The silver films were formed by using silver as the target and argon gas (with a total pressure of 266 mPa) as the sputtering gas.
In the same manner as in Example 1, an ITO film (40 nm thick), a silver film (12 nm thick), an ITO film (80 nm thick), a silver film (12 nm thick), an ITO film (70 nm thick), a silver film (12 nm thick) and an ITO film (40 nm thick) were laminated, in that order, on one major surface of a biaxially stretched polyethylene terephthalate film (50 μm thick). Thus, a transparent laminate in accordance with the present invention was formed. This transparent laminate was different from the transparent laminate of Example 1 in the thicknesses of the ITO films and the silver films.
In the same manner as in Example 1, an ITO film (40 nm thick), a silver film (9 nm thick), an ITO film (80 nm thick), a silver film (12 nm thick), an ITO film (80 nm thick), a silver film (9 nm thick) and an ITO film (40 nm thick) were laminated, in that order, on one major surface of a biaxially stretched polyethylene terephthalate film (50 μm thick). Thus, a transparent laminate in accordance with the present invention was formed. This transparent laminate was different from the transparent laminates of Examples 1 and 2 in the thicknesses of the ITO films and the silver films.
In the same manner as in Example 1, an ITO film (40 nm thick), a silver film (11 nm thick), an ITO film (80 nm thick), a silver film (11 nm thick), an ITO film (80 nm thick), a silver film (13 nm thick), an ITO film (80 nm thick), a silver film (13 nm thick) and an ITO film (40 nm thick) were laminated, in that order, on one major surface of a biaxially stretched polyethylene terephthalate film (50 μm thick). Thus, a transparent laminate in accordance with the present invention, having four metal film layers and five high-refractive-index transparent film layers, was formed.
According to a magnetron DC sputtering process, an indium oxide film (40 nm thick), a silver film (10 nm thick), an indium oxide film (70 nm thick), a silver film (10 nm thick), an indium oxide film (70 nm thick), a silver film (10 nm thick), an indium oxide film (60 nm thick), a silver film (6 nm thick), an indium oxide film (40 nm thick), a silver film (6 nm thick) and an indium oxide film (20 nm thick) were laminated, in that order, on one major surface of a biaxially stretched polyethylene terephthalate film (50 μm thick). Thus, a transparent laminate in accordance with the present invention, having five metal film layers and six high-refractive-index transparent film layers, was formed. The indium oxide films constituting the high-refractive-index transparent film layers were formed by using indium as the target and an argon-oxygen gaseous mixture (with a total pressure of 266 mPa and a partial pressure of oxygen of 80 mpa) as the sputtering gas. The silver films constituting the metal film layers were formed by using silver as the target and argon gas (with a total pressure of 266 mPa) as the sputtering gas.
In the same manner as in Example 1, an ITO film (40 nm thick), a silver film (9 nm thick), an ITO film (70 nm thick), a silver film (9 nm thick) and an ITO film (40 nm thick) were laminated, in that order, on one major surface of a biaxially stretched polyethylene terephthalate film (50 μm thick). The transparent laminate so formed had two silver films and three ITO films on the polyethylene terephthalate film constituting a transparent substrate.
According to a magnetron DC sputtering process, an indium oxide film (40 nm thick), a silver film (10 nm thick), an indium oxide film (70 nm thick), a silver film (10 rm thick), an indium oxide film (70 nm thick), a silver film (10 nm thick), an indium oxide film (60 nm thick), a silver-gold alloy film (6 nm thick), an indium oxide film (40 nm thick), a silver-gold alloy film (6 nm thick) and an indium oxide film (20 nm thick) were laminated, in that order, on one major surface of a biaxially stretched polyethylene terephthalate film (50 μm thick). Thus, a transparent laminate in accordance with the present invention, having five metal film layers and six high-refractive-index transparent film layers, was formed. The indium oxide films constituted the high-refractive-index transparent film layers, and the silver films and the silver-gold alloy films constituted the metal film layers. The indium oxide films were formed by using indium as the target and an argon-oxygen gaseous mixture (with a total pressure of 266 mPa and a partial pressure of oxygen of 80 mPa) as the sputtering gas. The silver films were formed by using silver as the target and argon gas (with a total pressure of 266 mPa) as the sputtering gas. The silver-gold alloy films were formed by using a silver-gold alloy [composed of silver and gold in a ratio of 85:15 (wt. %)] as the target and argon gas (with a total pressure of 266 mPa) as the sputtering gas.
The major surface of the transparent laminate of Example 1 opposite to the transparent multilayer film was bonded to one major surface of a 2 mm thick PMMA plate [Acrylite (trade name); manufactured by Mitsubishi Rayon Co., Ltd.; 470 mm�350 mm) through the medium of a transparent tacky material. Moreover, as shown in FIG. 1, a silver paste (MSP-600F; manufactured by Mitsui Toatsu Chemicals, Inc.) was screen-printed on the transparent multilayer film-bearing surface (i.e., the electrically conductive surface) of the transparent laminate, and then dried to form a metal-containing electrode (with a resistivity of 5�10-5 Ω�cm) having a thickness of 20 μm and a width of 10 mm. Thus, an optical filter for displays in accordance with the present invention was made.
As shown in FIG. 1, a silver paste (manufactured by Mitsui Toatsu Chemicals, Inc.) was screen-printed on the transparent multilayer film-bearing surface (i.e., the electrically conductive surface) of the transparent laminate (472 mm�350 mm) of Example 5, and then dried to form a metal-containing electrode having a thickness of 20 μm and a width of 10 mm. Thus, an optical filter for displays in accordance with the present invention was made.
Using an extruder, polyethylene terephthalate pellets 1203 (manufactured by Unitika, Ltd.) were mixed with 0.1% by weight of a dithiol complex of the following formula (3), melted at 260-280� C. and extruded to form a film having a thickness of 100 μm. Thereafter, this film was biaxially stretched to a thickness of 50 μm. On one major surface of this film, a 90 nm thick silicon oxide film was formed by electron beam vapor deposition to obtain an antireflection film. The visible light reflectance at the antireflection film-bearing surface was 1.4%. The visible light reflectance was measured by the method later discussed after the surface on which no antireflection film was formed was roughened with sand paper and painted in black. When the moisture permeability of this antireflection film was measured according to ASTM (American Society for Testing Materials)-E96, it was found to be 1.4 g/m2 �day, indicating that this antireflection film had excellent gas barrier properties. The major surface of the antireflection film opposite to the silicon oxide film was bonded to the film-bearing surface of the transparent laminate of Example 1 through the medium of an acrylic tacky material. Thus, an optical filter for displays in accordance with the present invention was made. The acrylic tacky material used for this purpose had a refractive index of 1.64 and an extinction coefficient of 0 in the wavelength region of 500 to 600 nm. In this optical filter for displays, the aforesaid antireflection film containing a near-infrared absorbing dye and having gas barrier properties functions as a transparent protective layer having antireflection properties. ##STR3##
An optical filter for displays in accordance with the present invention was made in the same manner as in Example 9, except that the transparent laminate of Example 2 was used in place of the transparent laminate of Example 1.
An optical filter for displays in accordance with the present invention was made in the same manner as in Example 9, except that the transparent laminate of Example 3 was used in place of the transparent laminate of Example 1.
An optical filter for displays was made in the same manner as in Example 9, except that the transparent laminate of Comparative Example 1 was used in place of the transparent laminate of Example 1.
In the same manner as in Example 9, the film-bearing surface of the transparent laminate of Example 1 was bonded to one major surface of a polycarbonate film (100 μm thick) through the medium of an acrylic tacky material (having a refractive index of 1.64 and an extinction coefficient of 0 in the wavelength region of 500 to 600 nm). Thus, an optical filter for displays was made.
In the same manner as in Example 5, an indium oxide film (40 nm thick), a silver film (10 nm thick), an indium oxide film (70 nm thick), a silver film (10 nm thick), an indium oxide film (70 nm thick), a silver film (10 nm thick) and an indium oxide film (40 nm thick) were laminated, in that order, on one major surface of a biaxially stretched polyethylene terephthalate film (50 μm thick). Thus, a transparent laminate in accordance with the present invention was formed.
In the same manner as in Example 5, an indium oxide film (40 nm thick), a silver film (10 nm thick), an indium oxide film (80 nm thick), a silver film (15 nm thick), an indium oxide film (80 nm thick), a silver film (10 nm thick) and an indium oxide film (40 nm thick) were laminated, in that order, on one major surface of a biaxially stretched polyethylene terephthalate film (50 μm thick). Thus, a transparent laminate (470 mm�350 mm) in accordance with the present invention was formed.
The major surface of the transparent laminate of Example 1 opposite to the transparent multilayer film was bonded to one major surface of a 2 mm thick PMMA plate [Acrylite (trade name); manufactured by Mitsubishi Rayon Co., Ltd.; 470 mm�350 mm]. Moreover, a metal-containing electrode (with a resistivity of 5�10-5 Ω�cm) was formed in the same manner as in Example 7.
The transparent laminate of Example 1 was bonded to a 2 mm thick PMMA plate (Acryfilter MR-NG; manufactured by Mitsubishi Rayon Co., Ltd.; 470 mm�350 mm) having an antiglare layer on one surface and no antiglare layer on the other surface. In this case, the surface of the transparent laminate opposite to the transparent multilayer film was bonded to the other surface of the PMMA plate. When the haze of the antiglare layer on the PMMA plate was measured with a haze meter, it was found to be 2%. Moreover, a metal-containing electrode (with a resistivity of 5�10-5 Ω�cm) was formed in the same manner as in Example 7.
The major surface of the transparent laminate of Example 1 opposite to the transparent multilayer film was bonded to one major surface of a 2 mm thick PMMA plate [Acrylite; manufactured by Mitsubishi Rayon Co., Ltd.; 470 mm�350 mm]. On the other hand, a solution of 3 g of a heat-curable varnish (SF-C-335; manufactured by Dainippon Ink & Chemicals, Inc.) in 100 g of a toluene/methyl ketone (10:1, in weight ratio) solvent mixture was applied to one major surface of a biaxally stretched polyethylene terephthalate film (100 μm thick), dried in air, and then cured at 150� C. for 20 seconds to form a 1 μm thick anti-Newton ring layer. Thus, there was obtained a first anti-Newton ring film. When the haze of the anti-Newton ring layer in this first anti-Newton ring film was measured with a haze meter, it was found to be 2%. When the moisture permeability of this first anti-Newton ring film was measured according to ASTM-E96, it was found to be 1.2 g/m2 �day, indicating that this first anti-Newton ring film had both antiglare properties and gas barrier properties.
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I. du Pont de Nemours and CompanyIntrusion resistant safety glazings and solar cell modulesWO2014055513A1 *Oct 1, 2013Apr 10, 2014High Performance Optics, Inc.Selective blue light filtered optic* Cited by examinerClassifications U.S. Classification359/359, 359/585, 359/350, 359/588, 359/589, 359/360, 428/336International ClassificationG02B5/20, B32B27/06Cooperative ClassificationG02B5/208, B32B27/06European ClassificationB32B27/06, G02B5/20VLegal EventsDateCodeEventDescriptionSep 22, 2011FPAYFee paymentYear of fee payment: 12Mar 29, 2010ASAssignmentOwner name: ASAHI GLASS COMPANY, LIMITED,JAPANEffective date: 20100317Free format text: ASSIGNMENT OF ASSIGNORS INTEREST;ASSIGNOR:MITSUI CHEMICALS, INC.;REEL/FRAME:024151/0082Jan 17, 2008FPAYFee paymentYear of fee payment: 8Jan 14, 2004FPAYFee paymentYear of fee payment: 4Apr 3, 1998ASAssignmentOwner name: MITSUI CHEMICALS, INC., JAPANFree format text: MERGER;ASSIGNOR:MITSUI TOATSU CHEMICALS, INC.;REEL/FRAME:009604/0076Effective date: 19971219Oct 30, 1997ASAssignmentOwner name: MITSUI CHEMICALS, INC., JAPANFree format text: ASSIGNMENT OF ASSIGNORS INTEREST;ASSIGNORS:OKAMURA, TOMOYUKI;YAMAZAKI, FUMIHARU;FUKUDA, SHIN;AND OTHERS;REEL/FRAME:009088/0921Effective date: 19971024RotateOriginal ImageGoogle Home - Sitemap - USPTO Bulk Downloads - Privacy Policy - Terms of Service - About Google Patents - Send FeedbackData provided by IFI CLAIMS Patent Services

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Global Armoured Vehicles Upgrade and Retrofit Market Report 2019: Industry Trends, Share, Size, Growth, Opportunity and Forecasts, 2011-2018 & 2019-2024
May 17, 2019, 15:45 ET
DUBLIN, May 17, 2019 /PRNewswire/ -- The "Armoured Vehicles Upgrade and Retrofit Market: Global Industry Trends, Share, Size, Growth, Opportunity and Forecast 2019-2024" report has been added to ResearchAndMarkets.com's offering.
The global armored vehicles upgrade and retrofit market reached a value of US$ 5.5 Billion in 2018
Armored vehicles refer to transportation and land combat vehicles used for various offensive and defensive operations. They are commonly employed for the transportation of military personnel and cargo as well as operating in active combats. These vehicles are often armed with weapons and protected by an armor against shell fragments, bullets and other projectiles.
Several programs are being conducted to upgrade the equipment and systems in old armored vehicles across the globe. Led by the availability of modern and evolved warfare technologies, these programs are driving the growth of the upgrade and retrofit market. Additionally, many countries are expanding their military budgets on account of increasing terrorism and hostile activities. These activities have also resulted in the requirement of frequent repairing and installation of new parts in armored vehicles.
Besides, there has been a rise in the demand for low-cost per mile military vehicles. As the processes of upgrade and retrofit are comparatively less expensive than manufacturing a fully equipped vehicle, it has positively influenced the market growth. Moreover, there has been a rise in investments for the advancement of military troop equipment for increased mobility and improved protection of land troops across both developed and emerging economies.
Looking forward, the market value to reach US$ 6.9 Billion by 2024, registering a CAGR of 3.7% during 2019-2024.
For more information about this report visit https://www.researchandmarkets.com/r/bouz4e

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BooksAdvanced SearchBrowse GenresBest SellersNew & Future ReleasesPaperbacksTop OffersTextbooksAudiobooksSell Your Books The First World War: A Complete History
3 New from £65.06
This item: The First World War by Sir Martin Gilbert Paperback £18.99
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Paperback£18.99 Amazon Prime 1914-1918: The History of the First World War
Paperback£9.09 Amazon Prime The Holocaust
Paperback£14.24 Amazon Prime The First World War: An Illustrated History
Paperback£9.98 Amazon Prime The Pity of War
Trade in The First World War for an Amazon Gift Card of up to £3.31, which you can then spend on millions of items across the site. Trade-in values may vary (terms apply). Learn more Product details
Amazon Bestsellers Rank: 365,892 in Books (See Top 100 in Books)
28 of 29 people found the following review helpfulAll-encompassing beginners guide
5 of 6 people found the following review helpfulAn ambivalent account
5 of 6 people found the following review helpfulBrilliant narrative history
TOP 1000 REVIEWERVINE VOICE on 27 Nov. 2007Format: Paperback
33 of 41 people found the following review helpfulA one-sided account of the war
12 of 15 people found the following review helpfulA FIRST-CLASS HISTORY
The history of WWI using almost just anecdotes
Far too long. Badly edite. I. E ...
Published 1 month ago by R. Bristow
Published 1 month ago by Jeff Russell
Fairly happy with this book.
Published 14 months ago by Purplemoose
Definitive, comprehensive and thoroughly human
i loved martin gilberts world war 2 but this version has been shrunk down the letters are so small makes hard reading .AVOID or get a bigger copy
Published on 21 Oct. 2007 by D. street
This is a great history boook, one of the definitive histories of the great war. Very detailed and very accessible.

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text:
Patent US7174893 - Mask with anti-asphyxia valve - Google PatentsSearch Images Maps Play YouTube News Gmail Drive More »Sign inAdvanced Patent SearchPatentsAn anti-asphyxia valve includes at least one flap having a first portion adapted for mounting to the housing and a second portion adapted to flex between a first open position allowing gas to pass from the patient side to the housing interior through the at least one port, and from the blower side through...http://www.google.com/patents/US7174893?utm_source=gb-gplus-sharePatent US7174893 - Mask with anti-asphyxia valveAdvanced Patent SearchPublication numberUS7174893 B2Publication typeGrantApplication numberUS 11/285,077Publication dateFeb 13, 2007Filing dateNov 23, 2005Priority dateFeb 9, 1999Fee statusPaidAlso published asCA2298129A1, CA2298129C, CA2733839A1, CA2733839C, DE60020756D1, DE60020756T2, EP1027905A2, EP1027905A3, EP1027905B1, EP1525895A2, EP1525895A3, US6491034, US7089939, US7185652, US7207334, US7861714, US8113197, US20020023649, US20020023650, US20020153012, US20020174867, US20060076017, US20060107960, US20090188505, US20120180794Publication number11285077, 285077, US 7174893 B2, US 7174893B2, US-B2-7174893, US7174893 B2, US7174893B2InventorsAdrienne Mary Claire Walker, Geoffrey Crumblin, Gregory Scott Smart, Michael Kassipillai Gunaratnam, Philip Rodney Kwok, Perry D. LithgowOriginal AssigneeResmed LimitedExport CitationBiBTeX, EndNote, RefManPatent Citations (61), Referenced by (8), Classifications (20), Legal Events (3) External Links: USPTO, USPTO Assignment, EspacenetMask with anti-asphyxia valve
US 7174893 B2Abstract
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KgDevice for releasing breathing gasUS20130213400 *Sep 30, 2011Aug 22, 2013Resmed LimitedPatient interface systems* Cited by examinerClassifications U.S. Classification128/206.21, 128/207.12, 128/205.24International ClassificationA61M16/06, A61M16/20, A61M16/08, A62B18/02, A62B18/10, A62B9/02Cooperative ClassificationY10T137/7771, Y10S128/912, A61M16/208, A61M16/08, A61M16/0683, A61M16/06, A61M16/0616European ClassificationA61M16/08, A61M16/06S, A61M16/20B, A61M16/06Legal EventsDateCodeEventDescriptionJul 16, 2014FPAYFee paymentYear of fee payment: 8Jul 14, 2010FPAYFee paymentYear of fee payment: 4Jan 3, 2007ASAssignmentOwner name: RESMED LIMITED, AUSTRALIAFree format text: CHANGE OF ASSIGNEE S ADDRESS;ASSIGNOR:RESMED LIMITED;REEL/FRAME:018750/0211Effective date: 20061211RotateOriginal ImageGoogle Home - Sitemap - USPTO Bulk Downloads - Privacy Policy - Terms of Service - About Google Patents - Send FeedbackData provided by IFI CLAIMS Patent Services