Structural and immunological differences between human platelet and endothelial thrombospondins

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....

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Bibliographic Details
Published in:FEBS letters 1986-02, Vol.196 (1), p.49-53
Main Authors: Clezardin, Philippe, Hunter, Nikolas R., McGregor, John L., Pepper, Duncan S., Dawes, Joan
Format: Article
Language:English
Subjects:
Antibodies, Monoclonal - immunology
Antibody Specificity
Applied sciences
Biological and medical sciences
Blood coagulation. Blood cells
Blood Platelets - analysis
Calcium - pharmacology
Chromatography, Gel
endothelium
Endothelium - analysis
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
Gel filtration chromatography
Glycoproteins - analysis
Glycoproteins - immunology
Human endothelial cell, Platelet
Humans
man
Molecular and cellular biology
Monoclonal antibody Radioimmunoassay
Other techniques and industries
Peptides - analysis
Platelet
platelets
Radioimmunoassay
Thermolysin
Thrombospondin
Thrombospondins
Trypsin
Umbilical Veins - analysis
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(86)80212-5