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A naturally occurring, warm‐reactive macroglobulin specific for papain‐treated human platelets: Preliminary characterization
Author(s) -
Gill Joan C.,
Carlson Patricia,
Kunicki Thomas J.,
Aster Richard H.
Publication year - 1986
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830210208
Subject(s) - papain , platelet , trypsin , thrombasthenia , antibody , chemistry , chymotrypsin , biochemistry , proteolysis , glycoprotein , macroglobulin , immunology , agglutination (biology) , enzyme , biology , platelet aggregation
Sera from 28 of the 113 normal children and adults (25%) studied were found to contain an immunoglobulin capable of causing complement‐dependent lysis of normal platelets treated with small quantities of papain. This factor reacts equally well at 4°C and at 37°C with a determinant induced on platelets from normal subjects by treatment with papain or bromelain, but not by trypsin, chymotrypsin, or neuraminidase. It does not bind to red cells treated with any of these enzymes. The site(s) for which the factor was specific could not be induced on platelets from six patients with type I Glanzmann's thrombasthenia (lacking glycoproteins IIb and IIIa), in contrast to platelets from each of 20 normal donors. Isolation and characterization of the factor has been difficult because of its intolerance to chemical and physical manipulation. In 11 of the 20 individuals studied, however, it was found to have the properties of an IgM immunoglobulin. The factor appears to be different from any previously described, naturally occurring human immunoglobulin. It has not yet been shown to be associated with any disease state, but in the presence of complement, it is capable of causing profound damage to platelets previously subjected to minimal proteolysis, and the possibility that it can provoke platelet destruction in some conditions deserves further study.