Platelets Express a Membrane Protein Complex Immunologically Related to the Fibroblast Fibronectin Receptor and Distinct From GPIIb/IIIa

We have previously identified and characterized a membrane glycoprotein complex (GP150/135) that functions as fibronectin receptor (FN-R) in fibroblast adhesion. Here we report that an immunologically related protein complex is expressed at the surface of human platelets. Antibodies monospecific for...

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Bibliographic Details
Published in:Blood 1987-05, Vol.69 (5), p.1535-1538
Main Authors: Giancotti, Filippo G., Languino, Lucia R., Zanetti, Adriana, Peri, Giuseppe, Tarone, Guido, Dejana, Elisabetta
Format: Article
Language:English
Subjects:
Antibodies - immunology
Biological and medical sciences
Blood coagulation. Blood cells
Blood Platelets - immunology
Blood Platelets - ultrastructure
Collodion
Electrophoresis, Polyacrylamide Gel
Fibroblasts - ultrastructure
Fundamental and applied biological sciences. Psychology
Humans
Membrane Proteins - analysis
Membrane Proteins - immunology
Membrane Proteins - isolation & purification
Molecular and cellular biology
Molecular Weight
Platelet
Platelet Membrane Glycoproteins - analysis
Platelet Membrane Glycoproteins - immunology
Platelet Membrane Glycoproteins - isolation & purification
Precipitin Tests
Receptors, Fibronectin
Receptors, Immunologic - immunology
Receptors, Immunologic - isolation & purification
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Summary:We have previously identified and characterized a membrane glycoprotein complex (GP150/135) that functions as fibronectin receptor (FN-R) in fibroblast adhesion. Here we report that an immunologically related protein complex is expressed at the surface of human platelets. Antibodies monospecific for the smaller subunit (GP135) of the fibroblast FN-R in fact specifically stained the platelet surface, as determined by FACS analysis, and reacted with a component of molecular weight (mol wt) 138,000 as shown in western blots of platelet membranes. Moreover, the same antibodies precipitated the 138,000 component together with a 160,000 protein, suggesting that the two molecules are associated in a supramolecular complex. A comparative analysis indicated that this protein complex is distinct from the GPIIb/IIIa complex, known to function as a receptor of wide specificity for fibrinogen, fibronectin, and von Willebrand factor. Differential extraction experiments revealed that the platelet 138,000 component is an intearal membrane protein.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood.V69.5.1535.1535