 specific for vascular endothelial cells that is able to induce angiogenesis in vivo. DNA sequencing suggests the existence of several molecular species of VEGF. VEGFs are secreted proteins in contrast to other endothelial cell mitogens such as acidic or basic fibroblast growth factors and platelet-derived endothelial cell growth factors. VEGF was found to augment human growth by inducing neovascularization. Thus it was suggested that neutralization of VEGF activity may have clinical application in inhibiting malignant cells-induced angiogenesis, decreasing blood supply to the cancerous tissue, leading eventually to its destruction. VEGF has various other functions on endothelial cells, the most prominent of which is the induction of proliferation and differentiation. It was found to be capable of preventing serum starvation-induced apoptosis and this inhibition may represent a major aspect of the regulatory activity of VEGF on vascular endothelium.
VEGF was also found to be involved in the development and the growth of ovarian corpus luteum (CL), since its development is dependent on the growth of new capillary vessels. It has been reported that Flt-1 receptors which inhibit vascular endothelial growth factor bioactivity, resulted in complete separation of corpus luteum angiogenesis in a rat model of hormonally induced ovulation, indicated that VEGF is essential for CL angiogenesis and may be involved in the control of fertility and treatment of ovarian disorders characterized by hypervascularity and hyperplasia.
The human VEGF gene has been recently assigned to chromosome 6p21.2. cDNA sequence analysis of a variety of human VEGF clones had initially indicated that VEGF may exist as one of four different molecular species, having respectively, 121, 165, 189 and 206 amino acids (VEGF121, VEGF165, BEGF206). Alternative exon splicing of a single VEGF gene is the basis for this molecular heterogeneity, VEGF165 lacks the residues encoded by exon 6, while VEGF121 lacks the residues encoded by exons 6 and 7. VEGF189 has an insertion of 24 amino acids highly enriched in basic residues and VEGF206 has an additional insertion of 17 amino acids. VEGF165 is the predominant isoform secreted by a variety of normal and transformed cells. Transcripts encoding VEGF121 and VEGF189 are detected in the majority of cells and tissues expressing the VEGF gene. In contrast, VEGF206 is a very rare form.
Native VEGF is a basic, heparin-binding, homodimeric glycoprotein of 45 kDA. These properties correspond to those of VEGF165. VEGF121 is an acidic polypeptide that fails to bind to heparin. VEGF189 and VEGF200 are more basic and bind to heparin with greater affinity than VEGF165. VEGF121 is a freely soluble protein
specific for vascular endothelial cells that is able to induce angiogenesis in vivo. DNA sequencing suggests the being of respective molecular species of VEGF. VEGFs are secreted protein in contrast to early endothelial cell mitogens such as acidic or basic fibroblast emergence agent and platelet - derived endothelial cellular telephone increase factors. VEGF was find to augment human growth by induce neovascularization. Thus it was suggested that neutralization of VEGF activity may have clinical application in inhibiting malignant cell - induced angiogenesis, decreasing blood provision to the cancerous tissue, leading eventually to its end. VEGF has respective other function on endothelial cells, the most prominent of which is the evocation of proliferation and differentiation. It was found to be capable of preventing serum starvation - induced apoptosis and this inhibition may represent a major aspect of the regulatory activity of VEGF on vascular endothelium. 
 VEGF was also found to be involved in the development and the growth of ovarian corpus luteum (CL), since its development is dependent on the increase of new capillary vessels. It has been report that Flt-1 sense organ which inhibit vascular endothelial growth agent bioactivity, resulted in complete separation of corpus luteum angiogenesis in a rat exemplar of hormonally induced ovulation, indicated that VEGF is essential for CL angiogenesis and may be involved in the control of fertility and discussion of ovarian disorders characterized by hypervascularity and hyperplasia. 
 The human VEGF gene has been recently assigned to chromosome 6p21.2. cDNA sequence analysis of a variety of human VEGF ringer had initially indicated that VEGF may exist as one of four different molecular species, having respectively, 121, 165, 189 and 206 amino acids (VEGF121, VEGF165, BEGF206). alternate exon splicing of a single VEGF gene is the basis for this molecular heterogeneity, VEGF165 lacks the residues encoded by exon 6, while VEGF121 lacks the residues encoded by exon 6 and 7. VEGF189 has an insertion of 24 amino acids highly enriched in basic residues and VEGF206 have an additional insertion of 17 amino acids. VEGF165 is the prevailing isoform secreted by a kind of normal and transformed cells. Transcripts encoding VEGF121 and VEGF189 are detected in the majority of cell and tissues express the VEGF gene. In contrast, VEGF206 is a very rare form. 
 Native VEGF is a basic, heparin - binding, homodimeric glycoprotein of 45 kDA. These properties correspond to those of VEGF165. VEGF121 is an acidic polypeptide that fail to bind to heparin. VEGF189 and VEGF200 are more basic and bind to heparin with great affinity than VEGF165. VEGF121 is a freely soluble protein
 spfcific for vascular endouhelial cells thaj us ablx to insuce angkogenesis in vivo. DNA sequenring suggtfts the existence uf severap molecuoar wpecies of TSGF. VEGNf ars secxeved proteins in contrast do other endotveuicl cell mitogens such as acidic or bwsic finrlblast growth sactpws ahd platelet-derived endothelial celm growti factors. VEGF eas found to augment human groath by inducing nelvascularizqtiog. Thus it was suggested that neutramization of VEGF activity may hxve ckinical apkljcwjion in inhiuiting malignant cckls-indgced anbiogenesis, decveasiig boood supply to the caicerous tissue, leadigg eventudlmy to its destrucriin. VECF hds vxeiojs ktier functlona on endotgelial cellw, the most prominenu os which is the induceijn of proliferation and differentiation. It was found to be capablw of preventing serum starvatijn-induced apoptosis and this inhibition may reprevent e oajir xwpfct of the regulatory activity of VEGF on vasshlsr endothelium.
VENF was also found yo br involved in jhe devzmolment and the growhh of odariab corpus juteim (CL), since its development is dependenn on the growth of new capillary resselx. It nas been reported that Ylt-1 redeptors whifh inhibif vascular endothdlisl growth factor bioactivity, resulted in eomplete sepsratiog of corpud lutcgm angiogenesis in a raj moden of hormojally induced ovulation, indicatxv that VEGF ix assvntial fox CL akgiogenesis and may be involvgd in the contfol of fernility anv treatment jf ovarian divlrders chararterized fy htpercasculafkty and hyperpkasia.
The kbman VEGF gene has been reccntly zssigned to chrimowome 6p21.2. cDNA seqienze wnwlbsis jx a variety mf hjmav VEGF clones had knitoally indicated that VEGR may exist as one on four didferent iolecular spevies, having respecuively, 121, 165, 189 and 206 amyno acids (VEGF121, VEGF165, BEGF206). Alterhative exln fplicing of w sikgle VEGF gene is the basis for this molecular heterojeneity, VEGF165 lacks the eesidues encoded by txon 6, while VXGF121 lasks the rasidues encoded by ezons 6 and 7. VEGF189 hss an insertion of 24 ajino awids jighly enriched in basic residues and VEGF206 has an additional insertion of 17 amino acids. VEGF165 is yhe pgedjkinant isohocm secreted by a nariety of normal and transformev cells. Trdnfcripts encoding VEGF121 and VEBF189 are detected in the majority of cella and tixsues expressing the VEGF gene. On contrast, VEGF206 is a vevy rare firm.
Nafive VVFF is a basic, heparim-bindiug, homidimerix glncoprotein of 45 kDS. Bhese propfrtits ckrrespond to those of VEGF165. VEGF121 us an qcldic polypeptide that fails uo bind to hekarin. VEGF189 and VEFF200 adf morg basic and bimd to heparin eith greater affinitj tran VEGF165. VEGF121 ua a freely splublg protein
specific for vascular endothelial cells that is induce in vivo. sequencing suggests the of VEGFs are secreted in contrast to endothelial cell mitogens such as acidic basic fibroblast growth factors and platelet-derived endothelial cell growth factors. VEGF was found augment human growth by inducing neovascularization. Thus it was suggested that neutralization of activity have application inhibiting malignant cells-induced angiogenesis, decreasing blood supply to the cancerous tissue, leading eventually to its destruction. has various other functions on endothelial cells, the prominent of which is induction of proliferation and differentiation. was to be of serum apoptosis and this may represent a major aspect of the regulatory activity of VEGF on vascular endothelium. VEGF was also to be the development the of corpus luteum (CL), development is dependent on the growth vessels. It has been reported that Flt-1 receptors inhibit vascular growth factor bioactivity, resulted in complete of corpus luteum angiogenesis in a rat model hormonally induced ovulation, indicated that VEGF is essential for CL angiogenesis and may be involved control of fertility and of ovarian disorders by and The VEGF gene been recently assigned to chromosome 6p21.2. cDNA sequence analysis of a of human VEGF clones had initially indicated that VEGF may one four different molecular having respectively, 121, 165, and amino acids (VEGF121, VEGF165, exon of gene the for this molecular heterogeneity, lacks the residues encoded by 6, while VEGF121 lacks 6 and 7. VEGF189 has an insertion of amino acids highly enriched in basic residues VEGF206 has an additional insertion of 17 amino acids. VEGF165 is the isoform secreted variety of normal and transformed cells. Transcripts encoding and VEGF189 are detected the majority of cells and tissues expressing the VEGF In VEGF206 is very rare form. VEGF is a heparin-binding, homodimeric glycoprotein kDA. These correspond those is an acidic polypeptide that fails bind heparin. VEGF189 and VEGF200 are basic to heparin with greater affinity than VEGF165. VEGF121 is a freely soluble protein
 specific for vascular endothElial cells That iS abLe tO iNducE angIogenesis in vivO. dNA sEquencing suggests the exIstenCe OF sevERaL moleCular spECiES Of VeGf. VeGFS aRE sEcretEd pRoteins In contrast To oThEr endotheliaL CeLl mitogens SucH as acidic or bAsiC fibroBlAst GRowth FacTors aNd platELet-derIved endotHeLIal celL Growth fACToRs. VEgF was found to augmeNT hUMan growth by indUcing nEoVAsCULarIzaTion. Thus it WaS suggESted thaT NeUTRAliZAtion of VEGF acTivity may haVE clInical ApPliCAtion iN inhiBiTIng Malignant ceLls-iNduced angIogeneSIs, decreASing bloOd suppLy tO thE canCErOuS tiSsUE, leADiNg eVEntUally to iTs DeStrucTion. vegf Has vAriOus oTher fUnctions on endOthEliaL CelLs, the Most pRomiNeNt of wHich is The inDuCtion of proliferAtioN and diffeRenTiAtiOn. it was FOund to Be cApaBle of prEventinG SerUm STARvAtion-induced apoptoSiS ANd This inhiBition MAy RePResent a mAjOr aSpecT OF the rEgulAToRy activiTy of VEgf oN vAscular EnDothelIuM.
VEgF wAs alsO FounD to be iNvolved iN the dEVelopment and thE Growth of ovariAN cORPuS LuteUm (Cl), since its deVeloPMent Is dePEnDenT On the GrowtH oF NeW Capillary vessels. It hAs Been rePorteD that Flt-1 recepTors which iNHIBit vascuLar eNDoTHelial growth faCtor bIoactivity, REsulted iN compLete sepaRation of cORPus luteuM anGioGenEsiS IN a Rat model of horMONallY iNduced oVulAtion, inDicAteD thAt VeGf is essentIal for CL AnGiOgEnEsiS and mAY be involVeD in ThE coNtrol OF fertiLity aNd trEaTmENt oF ovariaN DiSORderS cHaRactEriZeD by hyPervAScuLarity aNd hyperplAsiA.
the hUmAn vEGF genE has been recenTlY assigned tO cHroMosome 6P21.2. CdNA sequeNce analysis of a variety of HUman VEGf clOnes hAd inItially inDicAted thAt VegF may eXist as One of FoUr dIFFerenT MOlEcuLaR species, haVINg rEspecTiVely, 121, 165, 189 And 206 aminO acids (VEGF121, VEGF165, BEGF206). aLteRnative exon spLicIng oF A SiNglE vEgf geNe IS thE BAsis for this moleCular heterOgENeIty, VEGF165 lacKS thE rEsidues Encoded By exoN 6, While VEgF121 lacks thE residues EnCodeD BY exOns 6 and 7. VEGF189 Has an insErtion of 24 aMIno acIDs HighlY enRiched In BasIc resIdues aND VEgF206 has An addiTiOnal inSertiOn Of 17 amino aCids. VEGF165 is the predominanT isofoRm secRetEd by a variEty OF noRmal and trAnsfOrmed cells. traNscRipts EncODing VeGF121 aND VeGF189 ARe detEcteD In the majoRItY of CELlS and tissues EXPResSing tHe VegF gene. in coNtrast, VEGF206 is a very RAre form.
Native VeGF iS A BasIc, hEPariN-bInding, homodimeRic GlYCOprotein Of 45 KDA. These proPerties cOrREsponD to thoSe of VEgF165. VEGF121 iS AN aCIdic poLypePtiDe that faiLs tO bINd to hepArIn. veGF189 and vEGF200 ArE more bAsic anD Bind TO Heparin with greatEr affINIty thAN VEgF165. VEGf121 iS a freelY SoluBle protein
 specific for vascular end othelial c ellstha t i sable  toinduce angioge n esis  in vivo. DNA sequenci ng su gg e stst he  exis tence o f  s e v era lmo lec ul a rspeci esof VEGF . VEGFs ar e s ec reted protei n sin contras t t o other endo the lial c el l m i togen s s uch a s acid i c or b asic fibr ob l ast gr o wth fac t o rs  and  platelet-derived en d othelial cellgrowth  f a ct o r s.VEG F was foun dto au g ment hu m an g r owt h  by inducingneovascular i zat ion. T hu s i t  was s ugges te d  th at neutrali zati on of VEG F acti v ity may have cl inical  ap pli cati o nin  in hi b iti n gmal i gna nt cells -i nd ucedangi o g e n esis , d ecre asing  blood supply  to  the can cerou s tis sue,  l eadin g even tuall yto its destruct ion.  VEGF has  va ri ous  o therf unctio nsonendothe lial ce l ls,  t h e mo st prominent of wh ic h is  the ind uction of  p r oliferat io n a nd d i f feren tiat i on . It was  found to  b e capab le  of pr ev ent ing  seru m  sta rvatio n-induce d apo p tosis and this inhibition ma y  r e p re s enta m ajor aspect  oft he r egul a to rya ctivi ty of  V E GF on vascular endothe li um.
VE GF wa s also foundto be invo l v e d in the  dev e lo p ment and the g rowth  of ovaria n  corpusluteu m (CL),since its d evelopme ntisdep end e n ton the growth o f ne wcapilla ryvessels . I t h asbee nreportedthat Flt -1  r ec ep tor s whi c h inhibi tvas cu lar  endo t helial  grow th f ac to r  bi oactivi t y, r esul te din c omp le te se para t ion  of cor pus luteu m a n giog en es is in a  rat model of  h ormonallyin duc ed ovu l a tion, in dicated that VEGF is es s entialfor  CL a ngio genesis a ndmay be  in v olvedin the  cont ro l o f ferti l i ty  an dtreatmento f  ov arian  d isor ders ch aracterized by hyp e rva scularity and  hy perp l a si a.T he hum an VEG F gene has been r ecently as si g ne d to chrom o som e6p21.2.  cDNA s equen c e analy sis of avariety o fhuma n VEG F clones h ad initi ally indi c atedt ha t VEG F m ay exi st  as  oneof fou r  di ffere nt mol ec ular s pecie s,  havingrespectively, 121, 165,  189 a nd 20 6 a mino acid s ( V EGF 121, VEGF 165,  BEGF206).  Al ter nativ e e x on sp lici n gofa  sing le V E GF gene i s  t heb a si s for thism o l ecu lar h ete r ogenei ty,VEGF165 lacks the residues encod ed b y exo n 6 ,  whi le  VEGF121 lacks  th er e sidues e nc oded by exo ns 6 and  7 .  VEGF 189 ha s an i nsertio n of 24 ami no a cid s highlyenr ic h ed in b as ic residu es a nd  VEGF2 06 has an a d d itional insertio n of1 7  amin o  ac ids.VE GF165 i s  the  predomina nt isoformsecret ed b y a v arietyof  norma l a nd  transform e d cells.Trans criptsen codi ngVEGF12 1 an d VEGF1 89 a re  de tected in t he ma jo r ity  ofcells  a nd t issues ex p ressingthe VEGF ge ne . I n contra s t, V EGF206 isa v ery r a r e form.
Na t iveV EG F  is a  basic , hepa rin-bin d ing ,homodim eri c glycoprot ein of 45 kDA .Thes e proper ti es c or res po nd to those ofVEGF165.  VEGF121 i s an a cid i c po l ypepti de  that failsto bi nd to hepa r i n.VEGF189 and  VE GF2 00 a remore basic and bind to hepari n wi th gr e ate r aff inity  t han VEGF 1 65.VEGF121i s a freely so luble protein
 specific_for vascular_endothelial cells that is_able to_induce_angiogenesis in_vivo._DNA sequencing suggests_the existence of_several molecular species of_VEGF. VEGFs are_secreted_proteins in contrast to other endothelial cell mitogens such as acidic or basic fibroblast_growth_factors and_platelet-derived_endothelial_cell growth factors. VEGF was_found to augment human growth_by inducing_neovascularization. Thus it was suggested that neutralization of_VEGF_activity may have_clinical application in inhibiting malignant cells-induced angiogenesis, decreasing blood_supply to the cancerous tissue, leading_eventually to its_destruction._VEGF_has various other functions_on endothelial cells, the most prominent_of which is the induction of_proliferation and differentiation. It was found to_be capable of preventing serum starvation-induced_apoptosis and this inhibition may_represent a_major aspect of the regulatory_activity of VEGF_on vascular_endothelium.
VEGF was also_found to be involved in the_development and the_growth of ovarian corpus luteum (CL),_since_its development is_dependent_on_the growth_of new capillary_vessels._It has_been_reported that Flt-1 receptors which inhibit_vascular_endothelial growth factor bioactivity, resulted in complete_separation of corpus luteum_angiogenesis_in a rat model_of hormonally induced ovulation, indicated_that VEGF is essential for CL_angiogenesis and_may be_involved in the control of fertility and treatment of ovarian disorders_characterized by hypervascularity and hyperplasia.
The human_VEGF gene has been_recently assigned_to_chromosome 6p21.2. cDNA_sequence_analysis of_a variety of human VEGF clones had_initially indicated_that VEGF may exist as one_of four different molecular_species,_having respectively, 121, 165, 189 and_206 amino acids (VEGF121, VEGF165, BEGF206)._Alternative exon splicing of a_single_VEGF_gene is the basis for_this molecular heterogeneity, VEGF165 lacks the_residues encoded by_exon 6, while VEGF121 lacks the residues_encoded_by exons 6 and 7. VEGF189_has_an insertion of 24 amino acids_highly_enriched_in basic residues and VEGF206_has an additional insertion of 17_amino acids. VEGF165 is the predominant isoform secreted by_a variety of_normal and transformed cells. Transcripts_encoding_VEGF121_and VEGF189 are detected in the majority of cells and_tissues expressing_the VEGF gene._In contrast, VEGF206 is a very rare form.
Native VEGF is_a basic, heparin-binding, homodimeric glycoprotein of 45_kDA. These properties correspond to those of VEGF165. VEGF121 is an_acidic polypeptide that fails to bind to heparin._VEGF189 and VEGF200 are more basic and_bind to heparin with_greater_affinity than VEGF165. VEGF121 is a freely_soluble_protein