Thrombospondin 1 as an enzyme inhibitor
PJ Hogg - Thrombosis and haemostasis, 1994 - thieme-connect.com
Thrombosis and haemostasis, 1994•thieme-connect.com
Thrombospondins (TSP's) are a family of multidomain glycoproteins from platelets and most
normal and transformed cells. TSPl, the platelet TSP, is the best studied and most pervasive
and has been shown to play a fundamental role in cell-cell and cell-matrix interactions
(reviewed in 1-4). TSPl was first recognised more than 20 years ago as a protein released
from platelet a-granules in response to activation by thrombin (5, 6). Structural studies of
TSPl established it as a calcium-sensitive, disulfide-bonded trimer with a subunit molecular …
normal and transformed cells. TSPl, the platelet TSP, is the best studied and most pervasive
and has been shown to play a fundamental role in cell-cell and cell-matrix interactions
(reviewed in 1-4). TSPl was first recognised more than 20 years ago as a protein released
from platelet a-granules in response to activation by thrombin (5, 6). Structural studies of
TSPl established it as a calcium-sensitive, disulfide-bonded trimer with a subunit molecular …
Thrombospondins (TSP's) are a family of multidomain glycoproteins from platelets and most normal and transformed cells. TSPl, the platelet TSP, is the best studied and most pervasive and has been shown to play a fundamental role in cell-cell and cell-matrix interactions (reviewed in 1-4).
TSPl was first recognised more than 20 years ago as a protein released from platelet a-granules in response to activation by thrombin (5, 6). Structural studies of TSPl established it as a calcium-sensitive, disulfide-bonded trimer with a subunit molecular mass of 150,000 kDa (7-9). Upon release, TSPl binds to the platelet surface and to components of the nascent and mature clot (10) and influences clot formation and stability (11). The characterization of eDNA clones for human TSPl provided a detailed molecular structure of this protein (12, Fig. 1).
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