Cloning and characterization of the gene encoding the human platelet glycoprotein V. A member of the leucine-rich glycoprotein family cleaved during thrombin-induced platelet activation.

Abstract Hybridomas secreting monoclonal antibodies (MoAbs) to human platelet membrane glycoprotein IIb (GPIIb) were prepared by fusing cells of a mouse myeloma line to spleen cells from a BALB/c mouse immunized with purified GPIIb. Six of the hybridomas secreted MoAbs that recognized epitopes on the 23,000-dalton, disulfide-linked subunit of GPIIb, GPIIb beta. All six of these MoAbs agglutinated platelets in the absence of calcium. The agglutination titers of three of the MoAbs, however, were enhanced between 2 and 6 log2 dilutions when titrated in the presence of mmol/L of calcium. The enhancement in titer was the result of MoAb- induced platelet activation followed by platelet aggregation, a reaction that could also be initiated by the monovalent Fab fragments prepared from one of the MoAbs. The MoAbs did not significantly agglutinate platelets from patients with Glanzmann's thrombasthenia, confirming biochemical evidence that there is a paucity of GPIIb beta in the membranes of these cells. Our results show that MoAbs to epitopes on GPIIb beta initiate distinct platelet responses; therefore, they should be useful for studying the ways in which regions of surface glycoproteins are involved in platelet-platelet interactions. In addition, these reagents may prove of value in diagnosing and typing patients with Glanzmann's thrombasthenia.

Download Full-text

Human platelet glycoprotein V: characterization of the polypeptide and the related Ib-V-IX receptor system of adhesive, leucine-rich glycoproteins.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.90.18.8327 ◽

1993 ◽

Vol 90 (18) ◽

pp. 8327-8331 ◽

Cited By ~ 45

Author(s):

M. J. Hickey ◽

F. S. Hagen ◽

M. Yagi ◽

G. J. Roth

Keyword(s):

Human Platelet ◽

Platelet Glycoprotein ◽

Receptor System

Download Full-text

Characterization of the inhibition of U46619-mediated human platelet activation by the trimetoquinol isomers

Biochemical Pharmacology ◽

10.1016/0006-2952(88)90292-4 ◽

1988 ◽

Vol 37 (15) ◽

pp. 3023-3033 ◽

Cited By ~ 17

Author(s):

Ahn Chang-Ho ◽

Karl J. Romstedt ◽

Lane J. Wallace ◽

Duane D. Miller ◽

Dennis R. Feller

Keyword(s):

Platelet Activation ◽

Human Platelet

Download Full-text

Monoclonal antibodies to human platelet glycoprotein IIb beta that initiate distinct platelet responses

Blood ◽

10.1182/blood.v65.5.1112.bloodjournal6551112 ◽

1985 ◽

Vol 65 (5) ◽

pp. 1112-1119

Author(s):

LK Jennings ◽

DR Phillips ◽

WS Walker

Keyword(s):

Monoclonal Antibodies ◽

Platelet Aggregation ◽

Platelet Activation ◽

Human Platelet ◽

Platelet Glycoprotein ◽

Membrane Glycoprotein ◽

Spleen Cells ◽

Glanzmann’S Thrombasthenia ◽

Glanzmann's Thrombasthenia ◽

Mouse Myeloma

Hybridomas secreting monoclonal antibodies (MoAbs) to human platelet membrane glycoprotein IIb (GPIIb) were prepared by fusing cells of a mouse myeloma line to spleen cells from a BALB/c mouse immunized with purified GPIIb. Six of the hybridomas secreted MoAbs that recognized epitopes on the 23,000-dalton, disulfide-linked subunit of GPIIb, GPIIb beta. All six of these MoAbs agglutinated platelets in the absence of calcium. The agglutination titers of three of the MoAbs, however, were enhanced between 2 and 6 log2 dilutions when titrated in the presence of mmol/L of calcium. The enhancement in titer was the result of MoAb- induced platelet activation followed by platelet aggregation, a reaction that could also be initiated by the monovalent Fab fragments prepared from one of the MoAbs. The MoAbs did not significantly agglutinate platelets from patients with Glanzmann's thrombasthenia, confirming biochemical evidence that there is a paucity of GPIIb beta in the membranes of these cells. Our results show that MoAbs to epitopes on GPIIb beta initiate distinct platelet responses; therefore, they should be useful for studying the ways in which regions of surface glycoproteins are involved in platelet-platelet interactions. In addition, these reagents may prove of value in diagnosing and typing patients with Glanzmann's thrombasthenia.

Download Full-text