(redirected from Thrombospondin)
Also found in: Dictionary, Medical, Encyclopedia, Wikipedia.
Related to Thrombospondin: endostatin, Vitronectin, Thrombospondin receptor
THBSTorry Harris Business Solutions
THBSThat Having Been Said
THBSThe Hague Business School (The Hague, Holland)
THBSThe Hives Broadcasting Sercice (Swedish Band)
References in periodicals archive ?
A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family.
72 (%) APS: Antiphospholipid syndrome; aPLA: antiphospholipid antibodiesi lgM: Immunoglobulin M; lgG: immunoglobulin G; mRNA: messenger ribonucleic acid; ADAMTS-13: A disintegrin and metalloproteinase with a thrombospondin type l motif, member 13; Ct: cycle threshold
Plasmodium vivax thrombospondin related adhesion protein: immunogenicity and protective efficacy in rodents and Aotus monkeys.
It is also suggested that another enzyme, aggrecanase-2, or ADAMTS-5 (a disintegrin and MMP domain with thrombospondin motifs), plays a predominant role in the proteolysis of OA cartilage aggrecan.
They are cleaved into typical VWF multimers by a plasma VWF-cleaving metalloprotease, also called "a disintegrin-like and metalloprotease domain with thrombospondin type I motifs" (ADAMTS 13).
3,4) This protease has recently been identified as a new member of the zinc metalloproteases, ADAMTS13 (A Disintegrin And Metalloprotease with ThromboSpondin Type 1 motifs).
Brittain and her colleagues found that the integrin molecules could bind a cell to a vessel wall by attaching to thrombospondin there.
She is a postdoctoral fellow at the University of Maryland School of Medicine, pursuing studies of thrombospondin in human microvascular endothelial cells.
Another study involving the CARDIoGRAM investigators (57) identified 2 novel variants for CAD: ADAMTS7 (ADAM metallopeptidase with thrombospondin type 1 motif, 7) and the locus encoding the ABO blood group.
Flow cytometric studies in whole blood show increased platelet surface expression of P-selectin, increased binding of thrombospondin to platelets and increased amounts of platelet-leukocyte aggregates in MPN patients compared to controls (22), (23).
According to Vallejo and coworkers, (16) consistent with the idea that lesions in rheumatoid synovitis are sites of antigenic recognition, the characteristic focal expression of thrombospondin and its receptor CD36 on antigen presenting cells such as macrophage and fibroblast-like synoviocytes suggest a central role of this molecular interaction in the expansion of tissue infiltrating T cells.