Interaction of fibrinogen with staphylococcal clumping factor and with platelets.

Abstract:

:Fibrinogen, a clottable plasma glycoprotein, participates in cell adhesion phenomena involving prokaryotic cells, e.g. staphylococci, and eukaryotic cell fragments, e.g. platelets. Among the three chains (alpha, beta, gamma) of human fibrinogen, the gamma chain bears the main site recognizing the staphylococcal clumping receptor and human platelet receptor induced by ADP. The platelet receptors are also recognized, albeit less avidly, by a site associated with the alpha chain. The gamma chain site recognizing staphylococcal clumping factor exists on the COOH-terminal segment of this chain encompassing the 15 residues (gamma 397-411) including the COOH-terminal valine. The location of the gamma chain site interacting with the human platelet receptor had been pinpointed to the 27 residue CNBr COOH-terminal segment (gamma 385-411). The results of enzymatic degradation of the 27-residue peptide indicate that the continuity of the last 15 amino acid residues at the COOH-terminal end of the gamma chain of human fibrinogen seems to be essential for its interaction with human platelets. The sequence of the gamma chain interacting with the platelet receptor (gamma 385-411) indicates that this segment is a unique region of fibrinogen endowed with three important functions: cross-linking of fibrin, clumping of staphylococci, and aggregation of platelets. [Note added in proof: Recently we obtained evidence that dodecapeptide gamma 393-411 fully retains platelet receptor recognition site (Kloczewiak et al. 1983. Clin. Res 31:534A.)]

journal_name

Ann N Y Acad Sci

authors

Hawiger J,Kloczewiak M,Timmons S,Strong D,Doolittle RF

doi

10.1111/j.1749-6632.1983.tb23270.x

subject

Has Abstract

pub_date

1983-06-27 00:00:00

pages

521-35

eissn

0077-8923

issn

1749-6632

journal_volume

408

pub_type

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