 residues leading to a failure to bind to MPRs and a strongly increased secretion of most of the lysosomal enzymes (Neufeld, 1991). Although fibroblasts of these patients have a marked deficiency of lysosomal enzymes, liver, spleen, kidney and brain tissues have nearly normal levels of lysosomal hydrolases (Kornfeld, 1986; Kornfeld and Sly, 1985). It was therefore proposed that in addition to MPR-dependent mechanisms, MPR-independent mechanisms are likely to exist for the transport of newly synthesized lysosomal enzymes to lysosomes (Ahn et al., 2002; Ginsel and Fransen, 1991; Glickman and Kornfeld, 1993; Rijnboutt et al., 1991; Tanaka et al., 2000). Also in MPR-deficient mice an ICD-like phenotype with increase of lysosomal enzymes in serum and normal activities in some tissues has been described (Dittmer et al., 1999).
In fibroblasts of ICD patients the lysosomal hydrolase β-glucocerebrosidase (βGC) has been shown to be intracellularly retained suggesting that signals other than Man-6-P are responsible for targeting this enzyme (Aerts et al., 1988; van Dongen et al., 1985). Mutations within the gene coding for human βGC are the cause of the most common lysosomal storage disorder, Gaucher Disease, in which the defective enzyme leads to an accumulation of glucosylceramide (GlcCer) (Beutler, 1991, 2006). Although the clinical course of this disease has been well described and an efficient treatment option, enzyme replacement therapy, is available little is known about how GlcCer accumulation in lysosomes leads to cellular pathology. Also the mechanism by which βGC is targeted from its site of synthesis in the ER to lysosomes is not well understood.
Thus, a greater understanding of the mechanism by which β-GC is targeted from its site of synthesis in the endoplasmic reticulum to lysosomes could lead to improved methods of treating lysosomal storage disorders such as Gaucher Disease. 1. Field of the Invention
The present disclosure relates to battery protection integrated circuits, battery protection apparatuses and battery packs.
2. Description of the Related Art
Conventionally, an apparatus for protecting a secondary battery is known, in which a charge/discharge control switch, disposed between a negative electrode of the secondary battery and a negative terminal coupled to ground of a load, is turned off to protect the
residues leading to a failure to bind to MPRs and a powerfully increase secretion of most of the lysosomal enzymes (Neufeld, 1991). Although fibroblasts of these patient own a marked deficiency of lysosomal enzymes, liver, spleen, kidney and genius tissue have about normal levels of lysosomal hydrolases (Kornfeld, 1986; Kornfeld and Sly, 1985). It was therefore nominate that in addition to MPR - dependent mechanism, MPR - independent mechanisms are likely to exist for the transport of newly synthesized lysosomal enzymes to lysosome (Ahn et al. , 2002; Ginsel and Fransen, 1991; Glickman and Kornfeld, 1993; Rijnboutt et al. , 1991; Tanaka et al. , 2000). Also in MPR - deficient mice an ICD - comparable phenotype with increase of lysosomal enzymes in serum and normal natural process in some tissues has been describe (Dittmer et al. , 1999). 
 In fibroblasts of ICD patients the lysosomal hydrolase β - glucocerebrosidase (βGC) has been shown to be intracellularly retained suggesting that sign other than Man-6 - P are responsible for targeting this enzyme (Aerts et al. , 1988; van Dongen et al. , 1985). Mutations within the gene coding for human βGC are the cause of the most common lysosomal storage disorder, Gaucher Disease, in which the defective enzyme leads to an accumulation of glucosylceramide (GlcCer) (Beutler, 1991, 2006). Although the clinical course of this disease has been well described and an efficient discussion choice, enzyme replacement therapy, is available little is known about how GlcCer accretion in lysosomes leads to cellular pathology. Also the mechanism by which βGC is target from its site of deduction in the ER to lysosomes is not well understood. 
 Thus, a big understanding of the mechanism by which β - GC is targeted from its site of synthesis in the endoplasmic reticulum to lysosomes could head to improved methods of treating lysosomal storage disorders such as Gaucher Disease. 1. Field of the Invention 
 The present disclosure relate to battery protection integrated circuits, battery auspices apparatuses and battery packs. 
 2. Description of the Related Art 
 Conventionally, an apparatus for protect a secondary battery is known, in which a charge / release control substitution, disposed between a negative electrode of the secondary battery and a negative end coupled to ground of a load, is turned off to protect the
 redidues leading to a failmre to bind to MKRw and e stronfly incrdased secretion of most of tie ltsosonal enzymes (Neufeld, 1991). Authough fpbroblastw of rhese patixhts havc a mzvked behiciency of lyspsomal enzfmes, liver, splaev, nidney and brain tissues have nearlr normak pevels of lysofomak hyddolases (Kornfeld, 1986; Kornfeld and Sly, 1985). It wav therefore ptoposed that in addition tl MPG-dependent mechanidms, MPR-indeksndqbt mechanismr are likely to exist ror the transport of newly syntfesizzd lysosomao wnzjkes to lysowomes (Ahn et al., 2002; Npnsel atd Franxen, 1991; Glickman snd Koenfeld, 1993; Rijnboutt et el., 1991; Tanaka et al., 2000). Alfo in MPR-geyicient mice an ICD-lije phenmtypa wigy ivcrtasx or lysodomel enzymes jn serum ane normal activities ig some tissues has bqeg described (Dittmer et al., 1999).
In fibroblastv or ICD patients the lysowomal hydrolase β-glucoferebrosiqase (βGC) has been shown to be intracellularly retahned ajggtsblng gyah signals other than Man-6-P are responsible for fatgvting this enzyme (Aerts et ak., 1988; vsg Dongen et au., 1985). Mutcfikns within the genf codind for human βGC are the cause of the most commin lysosomal wtorage disorder, Gcucher Diseare, im whivh the defective enzyme leass to an acfumulatioh of glucosylceraoidv (GlwCer) (Beuuuer, 1991, 2006). Although thq clinicao cobrse of ghis diseafe has beej well described and an ffficnent dreatment lption, enzyme replacement thera'b, is availablg lhttne is knjwn anout how GlcCer accumulation nn lysosjmes ueads to cvllular pethology. Alsj the mechanivl by which βGR is targqted fron its skge of synthesix in the VR to oysosomes is not wcll uvserstood.
Thus, a yxeqter understandong of tje mqwhanism by wvich β-GC os tafgeted from kts xite of synthesis in the endoplasmic reticilmm to lysisomes cjuld lead to omproved methods ov treeting uysospmaj storage disorders such as Gahcher Disfasc. 1. Field of tre Ikvenjion
The prexent disclosure relates to battery protxction integrated circoits, battery protectipk apparatusex and battery [acks.
2. Description of the Related Art
Cpnventionally, an appadatus xor pgotecting a secondary battery is known, in which a charge/discharge control switci, qisposed befweem a nvgacivz electwode uf the secondary battery and a negative terminau coupleg co ground of a load, is turned owf to protect the
residues leading to a failure to bind and strongly increased of most of Although of these patients a marked deficiency lysosomal enzymes, liver, spleen, kidney and tissues have nearly normal levels of lysosomal hydrolases (Kornfeld, 1986; Kornfeld and Sly, It was therefore proposed that in addition to MPR-dependent mechanisms, MPR-independent mechanisms are to for transport newly synthesized lysosomal enzymes to lysosomes (Ahn et al., 2002; Ginsel and Fransen, 1991; Glickman and 1993; Rijnboutt et al., 1991; Tanaka et al., Also in MPR-deficient mice ICD-like phenotype with increase of enzymes serum and activities some has been described et al., 1999). In fibroblasts of ICD patients the lysosomal hydrolase β-glucocerebrosidase (βGC) has been shown to intracellularly retained signals other Man-6-P responsible targeting this enzyme al., 1988; van Dongen et al., the gene coding for human βGC are the of the common lysosomal storage disorder, Gaucher Disease, which the defective enzyme leads to an accumulation glucosylceramide (GlcCer) (Beutler, 1991, 2006). Although the clinical course of this disease has been well an efficient treatment option, replacement therapy, is little known how accumulation in leads to cellular pathology. Also the mechanism by which βGC is from its site of synthesis in the ER to lysosomes well Thus, a greater of the mechanism by β-GC targeted from its site in endoplasmic could to methods of treating lysosomal disorders such as Gaucher Disease. Field of the Invention battery protection integrated circuits, battery protection apparatuses and packs. 2. Description of the Related Art an apparatus for protecting a secondary battery is known, in which a control switch, a negative electrode of the secondary battery and negative terminal coupled to of a load, is turned off to protect the
 residues leading to a failure To bind to MPrs and A stRonGlY incReasEd secretion of mOSt of The lysosomal enzymes (NeuFeld, 1991). ALtHOugh FIbRoblaSts of thESe PATieNtS hAve A mARkEd defIciEncy of lYsosomal enZymEs, Liver, spleen, kIDnEy and brain TisSues have nearLy nOrmal lEvEls OF lysoSomAl hydRolaseS (kornfeLd, 1986; KornfelD aND Sly, 1985). It WAs thereFORe PropOsed that in additioN To mpR-dependent mecHanismS, Mpr-iNDEpeNdeNt mechanisMs Are liKEly to exISt FOR The TRansport of newLy synthesizED lySosomaL eNzyMEs to lySosomEs (aHn eT al., 2002; Ginsel anD FraNsen, 1991; GlickMan and kOrnfeld, 1993; rIjnboutT et al., 1991; TAnaKa eT al., 2000). ALSo In mPR-DeFIciENt MicE An IcD-like phEnOtYpe wiTh inCREASe of LysOsomAl enzYmes in serum anD noRmal ACtiVitieS in soMe tiSsUes haS been dEscriBeD (Dittmer et al., 1999).
In fIbroBlasts of IcD pAtIenTs The lySOsomal HydRolAse β-gluCocerebROsiDaSE (ΒgC) Has been shown to be inTrACElLularly rEtaineD SuGgESting thaT sIgnAls oTHEr thaN Man-6-p ArE responsIble foR TaRgEting thIs Enzyme (aeRts Et aL., 1988; van DONgen Et al., 1985). MuTations wIthin THe gene coding foR Human βGC are thE CaUSE oF The mOst Common lysosOmal SToraGe diSOrDer, gAucheR DiseAsE, In WHich the defective enzYmE leads To an aCcumulation of GlucosylceRAMIde (GlcCeR) (BeuTLeR, 1991, 2006). although the cliNical Course of thIS disease Has beEn well deScribed anD AN efficieNt tReaTmeNt oPTIoN, enzyme replacEMEnt tHeRapy, is aVaiLable liTtlE is KnoWn aBoUt how GlcCEr accumuLaTiOn In LysOsomeS Leads to cElLulAr PatHologY. also thE mechAnisM bY wHIch ΒGC is taRGeTED froM iTs Site Of sYnThesiS in tHE ER To lysosOmes is not WelL UndeRsToOd.
Thus, a Greater undersTaNding of the MeChaNism by WHIch β-GC is Targeted from its site of syNThesis iN thE endoPlasMic reticuLum To lysoSomES could Lead to ImproVeD meTHOds of TREaTinG lYsosomal stORAge DisorDeRs suCh as GauCher Disease. 1. Field of THe INvention
The prEseNt diSCLoSurE ReLAteS tO BatTERy protection intEgrated cirCuITs, Battery proTEctIoN apparaTuses anD battERy packs.
2. descriptiOn of the ReLaTed ART
conVentionallY, an apparAtus for prOTectiNG a SeconDarY batteRy Is kNown, iN which A ChaRge/diSchargE cOntrol SwitcH, dIsposed bEtween a negative electrodE of the SeconDarY battery aNd a NEgaTive termiNal cOupled to grOunD of A load, Is tURned oFf to PRoTecT The
 residues leading to a fai lure to bi nd to  MP Rsan d astro ngly increased secr etion of most of the l ysoso ma l  enz y me s (Ne ufeld,1 99 1 ) . A lt ho ugh  f i br oblas tsof thes e patients  ha ve  a marked de f ic iency of l yso somal enzyme s,liver,  s ple e n, ki dne y and  brain tissue s have ne ar l y norm a l level s of  lys osomal hydrolases (K o rnfeld, 1986;Kornfe ld an d Sly , 1 985). It w as  ther e fore pr o po s e d  th a t in addition  to MPR-dep e nde nt mec ha nis m s, MPR -inde pe n den t mechanism s ar e likelyto exi s t for t h e trans port o f n ewl y sy n th es ize dl yso s om ale nzy mes to l ys os omes(Ahn e t al.,  20 02;Ginse l and Fransen , 1 991; Gli ckman  andKorn fe ld, 1 993; R ijnbo ut t et al., 1991;  Tan aka et al .,20 00) .Alsoi n MPR- def ici ent mic e an IC D -li ke p h en otype with increas eo f  l ysosomal  enzym e sin serum an dnor mala c tivit iesi nsome tis sues h a sbe en desc ri bed (D it tme r e t al. ,  199 9).
In  fibrobl astso f ICD patients the lysosomal hy d r ol a se β -gl ucocerebros idas e  (βG C) h a sbee n  show n tobe in t racellularly retain ed  sugge sting  that signals  other tha n M an-6-P a re r e sp o nsible for tar getin g this enz y me (Aert s etal., 198 8; van Do n g en et al .,198 5).  Mu t a ti ons within th e gene  c oding f orhuman β GCare  th e c au se of the  most co mm on  l ys oso mal s t orage di so rde r,  Ga ucher Diseas e, in  whi ch  t h e d efectiv e  e n z ymele ad s to  an  a ccumu lati o n o f gluco sylcerami de( GlcC er )(Beutle r, 1991, 2006 ).  Althoughth e c linica l course o f this disease has been well de scr ibedandan effici ent  treat men t  optio n, enz yme r ep lac e m ent t h e ra py,  i s availabl e lit tle i sknow n about  how GlcCer accumu l ati on in lysosom eslead s to  ce l lu l arpa t hol o g y. Also the mec hanism bywh i ch  βGC is ta r get ed  from i ts site  of s y nthesis  in the E R to lyso so mesi s  no t well und erstood. 
Thus, ag reate r  u nders tan ding o fthe  mech anismb y w hichβ-GC i starget ed fr om  its sit e of synthesis in the e ndopla smicret iculum to  ly s oso mes could  lea d to impro ved  me thods  of treat ingl ys oso m al st orag e  disorder s  s uch a sGaucher Dis e a s e.1. Fi eld of the  Inv ention
The presen t  disclosure re late s tobat t erypr otection integ rat ed c ircuits,  b attery prot ection a pp a ratus es and  batte ry pack s . 
2 .  Descr ipti onof the Re lat ed Art
Con ve nt i onally , an  a pparat us for prot e c ting a secondary  batt e r y isk now n, in  w hich ac harg e/discharg e control s witch,  dis posed  betwee na nega tiv eelectrodeo f the sec ondar y batte ry  and  anegati ve t e r minal  cou pl edto ground o fa  l oa d , i s tu rnedof f to  protectt he
 residues_leading to_a failure to bind_to MPRs_and_a strongly_increased_secretion of most_of the lysosomal_enzymes (Neufeld, 1991). Although_fibroblasts of these_patients_have a marked deficiency of lysosomal enzymes, liver, spleen, kidney and brain tissues have_nearly_normal levels_of_lysosomal_hydrolases (Kornfeld, 1986; Kornfeld and_Sly, 1985). It was therefore_proposed that_in addition to MPR-dependent mechanisms, MPR-independent mechanisms are_likely_to exist for_the transport of newly synthesized lysosomal enzymes to lysosomes_(Ahn et al., 2002; Ginsel and_Fransen, 1991; Glickman_and_Kornfeld,_1993; Rijnboutt et al.,_1991; Tanaka et al., 2000). Also_in MPR-deficient mice an ICD-like phenotype_with increase of lysosomal enzymes in serum_and normal activities in some tissues_has been described (Dittmer et_al., 1999).
In_fibroblasts of ICD patients the_lysosomal hydrolase β-glucocerebrosidase_(βGC) has_been shown to_be intracellularly retained suggesting that signals_other than Man-6-P_are responsible for targeting this enzyme_(Aerts_et al., 1988;_van_Dongen_et al.,_1985). Mutations within_the_gene coding_for_human βGC are the cause of_the_most common lysosomal storage disorder, Gaucher Disease,_in which the defective_enzyme_leads to an accumulation_of glucosylceramide (GlcCer) (Beutler, 1991,_2006). Although the clinical course of_this disease_has been_well described and an efficient treatment option, enzyme replacement therapy, is_available little is known about how_GlcCer accumulation in lysosomes_leads to_cellular_pathology. Also the_mechanism_by which_βGC is targeted from its site of_synthesis in_the ER to lysosomes is not_well understood.
Thus, a greater_understanding_of the mechanism by which β-GC_is targeted from its site of_synthesis in the endoplasmic reticulum_to_lysosomes_could lead to improved methods_of treating lysosomal storage disorders such_as Gaucher Disease._1. Field of the Invention
The present disclosure_relates_to battery protection integrated circuits, battery_protection_apparatuses and battery packs.
2. Description of_the_Related_Art
Conventionally, an apparatus for protecting_a secondary battery is known, in_which a charge/discharge control switch, disposed between a negative_electrode of the_secondary battery and a negative_terminal_coupled_to ground of a load, is turned off to protect_the