Effects of thrombin on washed, human platelets: Chnages in the subcellular fractions

Hagen, Inger

doi:10.1016/0304-4165(75)90006-9

Cited by 48 publications

(27 citation statements)

References 22 publications

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“…Thrombospondin (TSP)' is a major glycoprotein located in the a-granules of human platelets (1,2). TSP is a 450-kD protein and is composed of three disulfide-linked subunits (3,4).…”

Section: Introductionmentioning

confidence: 99%

Complex formation of platelet thrombospondin with histidine-rich glycoprotein.

Leung¹,

Nachman²,

Harpel³

1984

J. Clin. Invest.

152

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“…Thrombospondin (TSP)' is a major glycoprotein located in the a-granules of human platelets (1,2). TSP is a 450-kD protein and is composed of three disulfide-linked subunits (3,4).…”

Section: Introductionmentioning

confidence: 99%

Complex formation of platelet thrombospondin with histidine-rich glycoprotein.

Leung¹,

Nachman²,

Harpel³

1984

J. Clin. Invest.

152

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“…It is stored within secretory granules of platelets (11,12) and is the major protein released from these cells when they are stimulated with agonists (11)(12)(13). Although a variety of functions have been ascribed to TSP-1 and its domains (14,15), the region harboring the N700S SNP is devoid of such known functional assignments with respect to platelet and other vascular cell responses (14,16).…”

mentioning

confidence: 99%

Molecular and Functional Differences Induced in Thrombospondin-1 by the Single Nucleotide Polymorphism Associated with the Risk of Premature, Familial Myocardial Infarction

Narizhneva

Byers-Ward

Quinn

et al. 2004

Journal of Biological Chemistry

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A serine (Ser-700) amino acid rather than an asparagine (Asn-700) at residue 700 of thrombospondin-1 has been linked to an increased risk for development of premature, familial heart attacks. We now have identified both functional and structural differences between the Ser-700 and Asn-700 thrombospondin-1 variants. The Ser-700 variant increased the rate and extent of platelet aggregation and showed increased surface expression on platelets compared with the Asn-700 variant. These differences could be ascribed to an enhanced interaction of the Ser-700 variant with fibrinogen on the platelet surface and are consistent with a prothrombotic phenotype in Ser-700 individuals. The Ser-700 variant thrombospondin-1 was conformationally more labile than the Asn-700 variant as demonstrated by increased susceptibility to proteolytic digestion and enhanced susceptibility to unfolding by denaturants. These data suggest a potential molecular and cellular basis for a genetic risk factor associated with early onset myocardial infarction.

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“…Cultured human foreskin and fetal lung fibroblasts secreted thrombospondin (determined by enzyme-linked immunosorbent assay) into the culture medium in a time-dependent manner (15.7 and 5.8 Thrombospondin is a major platelet a granule glycoprotein that is secreted and then partially bound to platelet membranes when human platelets aggregate in response to thrombin (1)(2)(3)(4)(5)(6)(7)(8). Thrombospondin is a 450-kilodalton (kDal) protein and is composed of three large disulfide-linked subunits (9, 10).…”

mentioning

confidence: 99%

“…Thrombospondin is a major platelet a granule glycoprotein that is secreted and then partially bound to platelet membranes when human platelets aggregate in response to thrombin (1)(2)(3)(4)(5)(6)(7)(8).…”

mentioning

confidence: 99%

Cultured human fibroblasts synthesize and secrete thrombospondin and incorporate it into extracellular matrix.

Jaffe¹,

Ruggiero²,

Leung³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

253

125

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Thrombospondin, a major glycoprotein released from a granules of thrombin-stimulated platelets, is a disulfidebonded trimer of 160-kilodalton subunits. Cultured human foreskin and fetal lung fibroblasts secreted thrombospondin (determined by enzyme-linked immunosorbent assay) into the culture medium in a time-dependent manner (15.7 and 5.8 Thrombospondin is a major platelet a granule glycoprotein that is secreted and then partially bound to platelet membranes when human platelets aggregate in response to thrombin (1)(2)(3)(4)(5)(6)(7)(8). Thrombospondin is a 450-kilodalton (kDal) protein and is composed of three large disulfide-linked subunits (9, 10). During platelet aggregation, thrombin-stimulated platelets develop a membrane-bound lectin-like activity (11-13), which originates from a granules and appears to play a role in mediating platelet aggregation by binding to a specific receptor on other platelets (14,15 3.7 X 10'°Bq). The radioactive postculture medium was removed, centrifuged at 8,000 x g for 2 min to remove cells and debris, and frozen at -35°C. The radioactive cell layers were washed twice, removed with a rubber policeman, pelleted by centrifugation, dissolved by boiling for 5 min in 2% NaDodSO4 containing protease inhibitors as described (20), and frozen until analyzed.In experiments in which the accumulation of thrombospondin antigen was measured by enzyme-linked immunosorbent assay (ELISA), fibroblasts were cultured in minimal essential medium containing 20% rabbit serum in 2-cm2 wells of multiwell plates. When the cells were confluent, the cells were washed, and the medium was replaced with 1 ml of fresh minimal essential medium containing 20% rabbit serum. At various times after the medium change, the postculture medium was removed, centrifuged at 8,000 X g for 2 min, and frozen until assayed. 998The publication costs ofthis article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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Effects of thrombin on washed, human platelets: Chnages in the subcellular fractions

Cited by 48 publications

References 22 publications

Complex formation of platelet thrombospondin with histidine-rich glycoprotein.

Complex formation of platelet thrombospondin with histidine-rich glycoprotein.

Molecular and Functional Differences Induced in Thrombospondin-1 by the Single Nucleotide Polymorphism Associated with the Risk of Premature, Familial Myocardial Infarction

Cultured human fibroblasts synthesize and secrete thrombospondin and incorporate it into extracellular matrix.

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