Human platelet glycoprotein V: A surface leucine-rich glycoprotein related to adhesion

Roth, Gerald J.; Church, Todd A.; McMullen, Brad A.; Williams, Stuart A.

doi:10.1016/0006-291x(90)91253-o

Cited by 28 publications

(7 citation statements)

References 19 publications

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“…Like the three subunits of the GPIb-IX complex, GPV contains a number of leucine-rich domains in its extracellular domain (52,53). The presence of GPV apparently has little effect on the expression of GPIb-IX in the plasma membrane or on the ability of GPIb-IX to bind vWf (37).…”

Section: Discussionmentioning

confidence: 99%

Signaling across the Platelet Adhesion Receptor Glycoprotein Ib-IX Induces αIIbβ3 Activation Both in Platelets and a Transfected Chinese Hamster Ovary Cell System

Zaffran¹,

Meyer²,

Negrescu³

et al. 2000

Journal of Biological Chemistry

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In platelets, ␣ IIb ␤ 3 exists in a form that cannot bind adhesive proteins in the plasma; although it can interact with immobilized fibrinogen it cannot interact with immobilized von Willebrand factor in the vessel wall. Soluble agonists such as thrombin convert ␣ IIb ␤ 3 to a form that recognizes soluble and immobilized ligands. Attempts to reconstitute ␣ IIb ␤ 3 activation in a non-hematopoietic, nucleated cell system have been unsuccessful. In the present study, we have developed a transfected Chinese hamster ovary cell model in which ␣ IIb ␤ 3 activation is induced by signaling across glycoprotein (GP) Ib-IX by its ligand, von Willebrand factor. GPIb-IX activates not only the transfected ␣ IIb ␤ 3 but also endogenous ␣ v ␤ 3 . Activation of the pathways leading to integrin activation occurred even in cells transfected with GPIb-IX lacking the domain on GPIb␣ that binds 14-3-3 or that which binds actin-binding protein. These studies demonstrate that signals induced by interaction of GPIb-IX with von Willebrand factor lead to ␣ IIb ␤ 3 activation and suggest that the signaling pathways by which GPIb-IX induces ␣ IIb ␤ 3 activation are different to those used by thrombin. Elucidation of these differences may provide insights into therapeutic ways in which to inhibit integrin activation in selective clinical settings.

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Section: Discussionmentioning

confidence: 99%

Signaling across the Platelet Adhesion Receptor Glycoprotein Ib-IX Induces αIIbβ3 Activation Both in Platelets and a Transfected Chinese Hamster Ovary Cell System

Zaffran¹,

Meyer²,

Negrescu³

et al. 2000

Journal of Biological Chemistry

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“…With the exception of the N-terminal region, which may contain a C7 zinc finger, this protein is almost entirely made up of leucine-rich repeats of 23 amino acids. These repeats can be aligned with those found in a variety of proteins, such as adenylate cyclase from yeast (11), chaoptin and the toll protein from Drosophila (12, 13), many serum glycoproteins and proteoglycans (14)(15)(16)(17)(18)(19)(20), the oligodendrocyte-myelin glycoprotein (21), the monocyte/granulocyte cell surface glycoprotein CD14 (22), the lutropin-choriogonadotropin receptor (23) and the placental ribonuclease inhibitor (24,25). With the exception of the latter, all these proteins are either extracellular, or bound to the plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

“…ES8 = ESAG 8 (Fig. 3); PRI = placental ribonuclease inhibitor (24,25); SC-AC = Saccharomyces cerevisiae adenylate cyclase (11); LRG = consensus of five serum glycoproteins: GP MO2 (14), Ibca (15), Ib,B (16), V (17) and IX (18); TOLL = Drosophila toll protein (13); CHAO = Drosophila chaoptin (12); hPGI = human proteoglycan I (19); PG40 = proteoglycan PG40 (20); OMgp = oligodendrocyte-myelin glycoprotein (21); LCGR = lutropin-choriogonadotropin receptor (23); CD14 = monocyte/granulocyte glycoprotein CD14 (22).…”

Section: Cd14mentioning

confidence: 99%

A gene from the VSG expression site ofTrypanosoma bruceiencodes a protein with both leucine-rich repeats and a putative zinc finger

Revelard¹,

Lips²,

Pays³

1990

Nucl Acids Res

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The transcription unit of the gene for the variant specific glycoprotein (VSG) AnTat 1.3A of Trypanosoma brucei contains several associated genes (ESAGs, for Expression Site-Associated Genes), 7 of which have already been described. We report here the characterization of a further ESAG, which we term ESAG 8, present 1 kb downstream from the putative adenylate cyclase gene ESAG 4. ESAG 8 encodes a 70 kd protein whose sequence indicates that it is probably not exposed at the cell surface. With the exception of the N-terminal domain which contains a presumptive DNA-binding zinc finger, the ESAG 8 protein consists exclusively of leucine-rich repeats of 23 amino acids, typical of protein-interacting domains such as the RAS-interacting region of the yeast adenylate cyclase. ESAG 8 transcripts are only found in bloodstream forms, and their level is particularly low, suggesting a high rate of degradation. The ESAG 8 protein may be involved in stage-specific regulatory processes, such as gene expression control or adenylate cyclase activation.

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“…Glycoprotein Ib/IX/V complex (GP Ib/IX/V) is the major von Willebrand factor (vWf) receptor on the platelet membrane. GP Ib, consisting of a large a subunit of 145kD disulphide linked to a small , B subunit of 2 4 0 , is non-covalently associated with GP IX of 22 kD and GP V of 82 kD (Du et Roth et al, 1990;Modderman et al, 1992: Shimomura rt al, 1990. All four subunits of the GP Ib/IX/V complex belong to a family characterized by leucinerich repetitive modules (Clemetson et al, 1991).…”

mentioning

confidence: 99%

Cys209 Ser mutation in the platelet membrane glycoprotein ibα gene is associated with Bernard‐Soulier syndrome

et al. 1994

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Molecular genetic analysis has been performed on a patient with Bernard-Soulier syndrome (BSS). The patient had characteristically giant platelets and was deficient in the glycoprotein (GP) Ib/IX/V complex, the von Willebrand factor (vWf) receptor on platelets. Previous studies with monoclonal antibodies directed against GP Ib alpha (CD 42b) and GP IX (CD 42a) demonstrated the absence of GP Ib alpha and presence of small amounts of GP IX on the surface of the patient's platelets. In this study the presence of GP V (CD 42d) is also demonstrated. This indicates a defect in the alpha-subunit of glycoprotein Ib. Therefore polymerase chain reaction (PCR)-amplification of the genomic DNA coding for GP Ib alpha was performed. Nucleotide sequence analysis of the entire coding region of GP Ib alpha revealed a homozygous single base pair mutation T-->A, leading to a single amino acid substitution cysteine-->serine at position 209 of the mature protein. We took advantage of the Mse I target site in the mutant allele, created by the T-->A mutation, to analyse all available family members. PCR-ASRA (allele-specific restriction enzyme analysis) using the restriction enzyme Mse I, revealed the heterozygosity of the mother and the two children of the patient, whereas homozygosity of the patient for the Cys209Ser mutation was confirmed. The sister of the patient was not found to be a carrier of the mutant allele. The mutation identified in the family studied, responsible for the deficiency of the GP Ib/IX/V complex, suggests that the cysteine at amino acid position 209 may be involved in disulphide bonding.

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Human platelet glycoprotein V: A surface leucine-rich glycoprotein related to adhesion

Cited by 28 publications

References 19 publications

Signaling across the Platelet Adhesion Receptor Glycoprotein Ib-IX Induces αIIbβ3 Activation Both in Platelets and a Transfected Chinese Hamster Ovary Cell System

Signaling across the Platelet Adhesion Receptor Glycoprotein Ib-IX Induces αIIbβ3 Activation Both in Platelets and a Transfected Chinese Hamster Ovary Cell System

A gene from the VSG expression site ofTrypanosoma bruceiencodes a protein with both leucine-rich repeats and a putative zinc finger

Cys209 Ser mutation in the platelet membrane glycoprotein ibα gene is associated with Bernard‐Soulier syndrome

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