476:
Jandrot-Perrus M, Busfield S, Lagrue AH, Xiong X, Debili N, Chickering T, Le
Couedic JP, Goodearl A, Dussault B, Fraser C, Vainchenker W, Villeval JL (September 2000). "Cloning, characterization, and functional studies of human and mouse glycoprotein VI: a platelet-specific collagen receptor from the
494:
ESTAVILLO, RITCHIE, DIACOVO a CRUZ. Functional
Analysis of a Recombinant Glycoprotein Ia/IIa (Integrin α2β1) I Domain That Inhibits Platelet Adhesion to Collagen and Endothelial Matrix under Flow Conditions. The Journal of Biological Chemistry,. s. -. DOI: 10.1074/jbc.274.50.35921. Available online:
556:
Dumin, J A; Dickeson S K, Stricker T P, Bhattacharyya-Pakrasi M, Roby J D, Santoro S A, Parks W C (Aug. 2001). "Pro-collagenase-1 (matrix metalloproteinase-1) binds the alpha(2)beta(1) integrin upon release from keratinocytes migrating on type I collagen". J. Biol. Chem. (United States) 276 (31):
274:
subunit has four cysteine-rich regions and a structure similar to other β-integrins. The interaction with collagen leads to stabilization of the platelets. The surface expression of this complex shows high variability, particularly in relation to the polymorphism of GPIa subunit gene. Different
379:. When bound to ADP, conformational changes occur within the aggregin molecule and consequently, it dissociates from the two subunits. Furthermore, the complex can be activated by thrombin. Thrombin binding to its receptor activates
375:. In the resting state the contact between the two protein subunits (necessary for the complex activation) is prevented by aggregin, which disables their contact necessary for the complex activation. The complex can be activated by
99:. Fibrinogen molecules then interconnect the platelets, serving as the basis for platelet aggregation. In the absence of fibrinogen, the platelets are joined by vWF due to its ability to bind the activated GPIIb / IIIa complex.
507:
SHATTIL, S. J., J. A. HOXIE, M. CUNNINGHAM a BRASS. Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation. The
Journal of Biological Chemistry. September 15, 1985.
452:
LEPAGE, A., M. LEBOEUF, J.P. CAZENAVE, C. SALLE, F. LANZA a G. UZAN. The αIIbβ3 integrin and GPIb-V-IX complex identify distinct stages in the maturation of CD34+cord blood cells to megakaryocytes.
182:. It is an important collagen receptor involved in collagen-induced platelet activation and adhesion. It plays a key role in their procoagulant activity and subsequent
95:(vWF) results in conformational changes within the GPIb-V-IX complex. In consequence, this complex activates GPIIb / IIIa membrane glycoproteins, allowing them to bind
159:. The binding between GPIbα and vWF mediates the capture of platelets to the injured vascular wall. The deficiency in glycoprotein Ib-IX-V complex synthesis leads to
628:
531:
Calvete JJ (1995). "On the structure and function of platelet integrin alpha IIb beta 3, the fibrinogen receptor". Proc. Soc. Exp. Biol. Med. 208 (4): 346–60.
1020:
889:
339:(GPIIIa) forms a single polypeptide chain. These subunits form Ca - dependent complex on the surface of platelet membrane in a 1:1 ratio.
621:
542:
GARNER, CAMPBELL a METCALFE. Glycoprotein V: the predominant target antigen in gold-induced autoimmune thrombocytopenia. Blood. 2002.
1015:
937:
932:
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subunit is 36% identical to the GPIIb subunit. This complex is located mainly on endothelial cells but also on smooth muscle cells,
1066:
391:. Calpain cleaves aggregin, and thus allows for joining of the two subunits. Deficiency in the IIb / IIIa complex is described as
894:
730:
275:
opinions exist on the importance of C - T point mutation at position 807, which is believed to be associated with the risk of
970:
614:
392:
160:
922:
109:
80:
1100:
176:
1010:
140:, while the GPV and GPIX associate non-covalently with the complex. The GPIbα subunit bears the binding site for
590:
586:
1105:
836:
832:
327:. The IIb / IIIa complex is a major platelet membrane component. There are as many as 50 000 copies. The α
581:
951:
695:
664:
465:
384:
376:
288:
276:
179:
141:
92:
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992:
316:
surfaces. Activation of this complex initiates the platelet aggregation and the formation of primary
152:
133:
44:
125:
1002:
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942:
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645:
562:
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230:
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subunit includes a domain homologous to von
Willebrand factor domain binding to collagen. The β
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222:
129:
596:
436:. Its main function is in the adhesion of cells to the extracellular matrix components.
1048:
348:
dodecapeptide located in the C-terminal of the fibrinogen γ chain (the most important)
1094:
861:
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740:
317:
20:
1058:
904:
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36:
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96:
32:
927:
884:
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760:
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433:
360:
79:. The leading role in the elimination of high-stress injury is taken by the
24:
570:
482:
536:
190:
formation. Its procoagulant function may contribute to arterial or venous
823:
813:
808:
352:
312:
and thus plays an important role in platelet aggregation and adhesion to
183:
149:
145:
76:
72:
1075:
917:
388:
356:
606:
116:
This transmembrane glycoprotein complex is composed of four subunits:
842:
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466:
http://bloodjournal.hematologylibrary.org/content/96/13/4169.full.pdf
321:
292:
187:
552:
http://bloodjournal.hematologylibrary.org/content/100/1/344.full.pdf
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117:
387:. Consequently, there is a release of calcium ions that activate
704:
410:
324:
298:
240:
218:
199:
168:
64:
60:
610:
395:. Patients completely lack the ability to aggregate platelets.
343:
Fibrinogen sites recognized by glycoprotein IIb / IIIa complex:
214:
210:
890:
Protein Z-related protease inhibitor (ZPI) (inhibits FX, FXI)
582:
Online
Medical Dictionary, Platelet membrane glycoproteins
206:(GPVI transmembrane domain associates with γ chain FCR),
602:
http://circ.ahajournals.org/content/99/1/e1/F4.large.jpg
895:
Tissue factor pathway inhibitor (TFPI) (inhibits FIII)
597:
http://www.ojrd.com/content/1/1/46/figure/F1?highres=y
477:
immunoglobulin superfamily". Blood 96 (5): 1798–807.
1057:
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1001:
978:
969:
903:
860:
799:
774:
719:
653:
644:
51:
Receptors involved in platelet adhesion to collagen
961:Thrombin-activatable fibrinolysis inhibitor (TAFI)
550:. DOI: 10.1182/blood.V100.1.344.Available online:
87:Interactions of the platelet surface glycoproteins
1021:Activated protein C–protein C inhibitor (APC–PCI)
577:http://www.reference.md/files/D019/mD019038.html
870:Antithrombin (inhibits FII, FIX, FX, FXI, FXII)
331:(GPIIb) is composed of two subunits linked by
622:
517:http://www.jbc.org/content/260/20/11107.short
8:
497:http://www.jbc.org/content/274/50/35921.long
975:
650:
629:
615:
607:
938:Plasminogen activator inhibitor-2 (PAI-2)
933:Plasminogen activator inhibitor-1 (PAI-1)
589:at the U.S. National Library of Medicine
132:. Each of them has a variable number of
445:
731:High-molecular-weight kininogen (HMWK)
557:29368–74. DOI:10.1074/jbc.M104179200.
221:adaptor protein, all participating in
7:
1016:Thrombin–antithrombin complex (TAT)
923:Tissue plasminogen activator (tPA)
880:Protein S (cofactor for protein C)
351:RGD sequence of the α chain → the
287:Glycoprotein IIb / IIIa complex (
180:type I transmembrane glycoproteins
14:
258:. It consists of two subunits (α
229:Glycoprotein Ia / IIa complex (
136:. GPIbα and GPIbβ are linked by
1011:Prothrombin fragment 1+2 (F1+2)
671:Platelet membrane glycoproteins
587:Platelet+membrane+glycoproteins
108:Glycoprotein Ib-IX-V complex (
41:platelet membrane glycoproteins
17:Platelet membrane glycoproteins
875:Protein C (inhibits FV, FVIII)
175:Glycoprotein VI is one of the
1:
367:This complex also binds vWF,
308:This complex interacts with
81:glycoprotein Ib-IX-V complex
751:Factor XII (Hageman factor)
665:von Willebrand factor (vWF)
383:and increases the level of
31:) which play a key role in
1122:
1071:-antiplasmin complex (PAP)
786:Factor III (tissue factor)
393:Glanzmann's thrombasthenia
177:immunoglobulin superfamily
993:β-Thromboglobulin (β-TG)
591:Medical Subject Headings
161:Bernard–Soulier syndrome
988:Platelet factor 4 (PF4)
885:Protein Z (inhibits FX)
819:Prothrombin (factor II)
250:This is a receptor for
55:Membrane glycoproteins
1044:Fibrinopeptide B (FpB)
1039:Fibrinopeptide A (FpA)
711:Glycoprotein VI (GPVI)
676:Glycoprotein Ib (GPIb)
103:Membrane glycoproteins
71:, engaged in platelet
862:Anticoagulant factors
829:Fibrinogen (factor I)
824:Thrombin (factor IIa)
696:Glycoprotein IIb/IIIa
690:Glycoprotein IX (GP9)
657:(platelet activation)
385:inositol triphosphate
277:myocardial infarction
142:von Willebrand factor
93:von Willebrand factor
67:as well, function as
1049:Fibrin monomers (FM)
905:Fibrinolytic factors
723:(contact activation)
515:. Available online:
202:activation involves
134:leucine-rich repeats
45:extracellular matrix
1003:Thrombin generation
980:Platelet activation
971:Coagulation markers
646:Coagulation factors
638:Coagulation cascade
363:amino acid sequence
1101:Coagulation system
843:Fibrin (factor Ia)
655:Primary hemostasis
69:collagen receptors
43:interact with the
1088:
1087:
1084:
1083:
1031:Fibrin generation
856:
855:
776:Extrinsic pathway
721:Intrinsic pathway
333:disulfide bridges
167:Glycoprotein VI (
138:disulfide bridges
39:wall is damaged,
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381:protein kinase C
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778:(tissue factor)
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281:ischemic stroke
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252:collagen type I
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223:phospholipase C
173:
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91:The binding of
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956:-Macroglobulin
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801:Common pathway
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1106:Glycoproteins
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741:Prekallikrein
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63:and probably
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42:
38:
34:
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26:
22:
21:glycoproteins
18:
1076:D-Dimer (DD)
1059:Fibrinolysis
947:-Antiplasmin
670:
669:
503:
490:
472:
453:
448:
419:
399:GPV / IIIa (
366:
342:
341:
307:
289:GPIIb / IIIa
249:
225:activation.
174:
148:, leukocyte
115:
90:
54:
40:
37:blood vessel
29:thrombocytes
19:are surface
16:
15:
913:Plasminogen
848:Factor XIII
766:Factor VIII
430:macrophages
422:heterodimer
403:= integrin
373:vitronectin
369:fibronectin
314:endothelial
291:= integrin
233:= integrin
198:pathway of
35:. When the
1095:Categories
791:Factor VII
746:Kallikrein
736:Bradykinin
440:References
420:This is a
310:fibrinogen
231:GPIa / IIa
208:Src kinase
192:thrombosis
157:P-selectin
146:α-thrombin
97:fibrinogen
33:hemostasis
1067:Plasmin-α
928:Urokinase
761:Factor IX
756:Factor XI
563:0021-9258
548:1528-0020
513:0021-9258
462:1528-0020
434:platelets
401:GPV / IIa
361:Aspartate
110:GPIb-IX-V
25:platelets
23:found on
814:Factor V
809:Factor X
571:11359786
483:10961879
353:Arginine
266:). The α
184:thrombin
150:integrin
77:collagen
73:adhesion
57:GPIa/IIa
918:Plasmin
537:7535429
424:. Its α
389:calpain
357:Glycine
335:. The β
204:γ chain
144:(vWF),
705:GPIIIa
593:(MeSH)
569:
561:
546:
535:
511:
481:
460:
322:fibrin
217:, and
194:. The
188:fibrin
700:GPIIb
685:GP1BB
680:GP1BA
454:Blood
262:and β
122:GPIbβ
118:GPIbα
567:PMID
559:ISSN
544:ISSN
533:PMID
509:ISSN
479:PMID
458:ISSN
456:. .
432:and
371:and
325:clot
320:, a
254:and
200:GPVI
186:and
169:GPVI
155:and
153:αMβ2
130:GPIX
128:and
65:GPIV
61:GPVI
837:FGG
833:FGA
377:ADP
329:IIb
295:IIb
279:or
219:LAT
215:LYN
211:FYN
196:FCR
126:GPV
124:,
75:to
1097::
835:,
565:.
464:.
283:.
256:IV
213:/
163:.
120:,
83:.
59:,
47:.
1069:2
954:2
952:α
945:2
943:α
839:)
831:(
707:)
698:(
692:)
678:(
673::
630:e
623:t
616:v
573:.
539:.
485:.
426:5
416:)
413:1
411:β
407:5
405:α
359:-
355:-
337:3
304:)
301:3
299:β
293:α
272:1
268:2
264:1
260:2
246:)
243:1
241:β
237:2
235:α
171:)
112:)
27:(
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