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Structural and immunological differences between human platelet and endothelial thrombospondins
Author(s) -
Clezardin Philippe,
Hunter Nikolas R.,
McGregor John L.,
Pepper Duncan S.,
Dawes Joan
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80212-5
Subject(s) - thrombospondins , thermolysin , polyclonal antibodies , thrombospondin , monoclonal antibody , biology , trypsin , antibody , biochemistry , chemistry , microbiology and biotechnology , immunology , enzyme , metalloproteinase
The structural and immunological properties of human thrombospondins isolated from platelets and from endothelial cells were compared. Both thrombospondins were digested with either trypsin or thermolysin, in the presence or absence of calcium, then injected onto a Superose 12 gel filtration column. The isolated thermolysin‐generated fragments of thrombospondins were identified by radioimmunoassays using either different monoclonal antibodies or a polyclonal antibody directed against platelet thrombospondin. The results show that platelet and endothelial thrombospondins are both partially protected from trypsin digestion in the presence of calcium but have different trypsin and thermolysin fragmentation patterns. The thermolysin‐generated fragments from platelet and endothelial thrombospondins are recognized differently by a monoclonal antibody whereas all of them are identified by a polyclonal antibody.