Plasma thrombospondin in patients with chronic renal failure, liver disease and splenectomy

Trzeciak, Marie‐Christine; McGregor, John L.; Renaux, Jean-Louis; Ville, D; Berruyer, Micheline; Dawes, J.; Dechavanne, M

doi:10.1016/0049-3848(85)90356-1

Cited by 13 publications

(8 citation statements)

References 25 publications

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“…First, the lack of correlation between platelet count and plasma TSP level argues that elevated plasma TSP levels are not simply related to the higher number of circulating platelets manifested by some sickle cell disease subjects. Second, it is reported that plasma TSP levels tend to be elevated in HbAA donors who have been surgically splenectomized [25]. Thus, the "autosplenectomy" state of sickle patients might contribute to the elevated steady state TSP levels for some subjects.…”

Section: Relatlonshlp To Splenic Functionmentioning

confidence: 99%

Disturbance of plasma and platelet thrombospondin levels in sickle cell disease

et al. 1996

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Thrombospondin (TSP), a large protein found in platelet alpha-granules (as TSP-1), mediates adhesion of sickle reticulocytes to cultured vascular endothelium. To further explore the physiologic relevance of this observation, we have measured plasma TSP levels and platelet TSP-1 content in subjects with sickle cell disease. Plasma TSP levels were similar for normal controls (mean 491 ng/ml, range 331-723) and steady-state HbSS patients (mean 536, range 333-1107) and were significantly (P = 0.012) but variably elevated for HbSS patients presenting with acute painful crisis (mean 868, range 442-2780). Some of these elevated plasma TSP levels reached those previously observed to support maximal red cell adhesion to endothelium in vitro. Compared to normals, both steady-state and in-crisis HbSS patients had significantly (P < 0.001) depressed platelet TSP-1 content (82.6 +/- 11.9, 47.1 +/- 16.0 and 45.9 +/- 20.7 ng/l0(6) platelets, respectively, mean +/- SD). HbSC disease patients, all examined during steady state, had low-normal plasma levels of TSP and either normal or depressed platelet TSP-1 content. Serial observations on three sickle cell anemia subjects indicated a probable relationship between platelet TSP-1 release, elevated plasma TSP levels, and acute vaso-occlusive episodes. These results suggest a state of ongoing release and depletion of TSP-1 from activated platelets in patients with sickle cell disease.

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Section: Relatlonshlp To Splenic Functionmentioning

confidence: 99%

Disturbance of plasma and platelet thrombospondin levels in sickle cell disease

et al. 1996

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“…To date, only a limited number of clinical studies have been reported in which the level of TSP in plasma was determined. 6,[63][64][65] These studies have simultaneously measured BTG and PF4 to determine if a correlation exists between these proteins in plasma. Radioimmunoassay has been the method of choice in the quantitation of these plate let α-granule proteins.…”

Section: Thrombospondin As a Marker Of Platelet Activation In Clinicamentioning

confidence: 99%

Thrombospondin in Clinical Disease States

Booth¹,

Berndt²

1987

Semin Thromb Hemost

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“…Monoclonal antibodies P9-Pl2 and P13 -P17 were of the IgG and IgM classes, respectively, as judged by [35S]methionine radiolabelling [15]. Two of the monoclonal antibodies (P10 and P12) and a polyspecific rabbit antibody directed against thrombospondin [16] were used for the work presented in this study.…”

Section: Preparation Of Monoclonal Antibodiesmentioning

confidence: 99%

Characterization of two murine monoclonal antibodies (P10, P12) directed against different determinants on human blood platelet thrombospondin

et al. 1986

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Thrombospondin, a 450-kDa glycoprotein composed of three disulphide linked chains, is located in human blood platelet alpha-granules and is released from platelets upon stimulation. This glycoprotein is thought to play a major role in platelet aggregation. The aim of this study was to characterize two monoclonal antibodies (P10 and P12) directed against human blood platelet thrombospondin. When the released material obtained after stimulation of platelets with thrombin in the presence of 2 mM calcium was immediately treated with EDTA, labelled with ' ' ' I and incubated with monoclonal antibodies PI0 and P12, both immunoprecipitated a major labelled protein band with a molecular mass of 160 kDa and a weaker band at 146 kDa, as analysed on reduced dodecyl sulphate/polyacrylamide gels. The major band corresponds in molecular mass to the thrombospondin subunits. If, however, the released material was left in the presence of Ca2+ for 48 h, then the main band was at 130 kDa and in addition one minor protein band (75 kDa) was immunoprecipitated by P10 whereas P12 recognized two minor protein bands (75 and 60 kDa). When P10 and P12 were incubated with '251-labelled platelet releasates treated for 48 h at 4°C with 10 mM EDTA, three major protein bands (160, 146 and 130 kDa) were immunoprecipitated in addition to the minor bands mentioned above. These results indicate that thrombospondin is probably degraded by the endogenous platelet calcium-dependent protease. Investigation of tryptic peptide fragments of thrombospondin isolated by fast protein liquid chromatography showed that 251-labelled antibody P10 bound to 400-kDa and 120-kDa fragments whereas '2SI-labelled PI2 only recognized a 400-kDa fragment. Competition studies involving solid-phase antibody binding and double antibody sandwich assays showed that P10 and P12 were directed against different determinants of thrombospondin. Purified thrombospondin, isolated in the presence of calcium, either directly or after treatment with EDTA, haemagglutinated trypsinized, formaldehyde-fmed sheep erythrocytes identically. The haemagglutination activity of EDTA-treated thrombospondin was inhibited by P10 and enhanced by P12. On the other hand, P10 and P12, despite their binding to calciumtreated thrombospondin, had no effect on its haemagglutination activity. Monoclonal antibodies PI0 and P12 could be useful tools to investigate the role of thrombospondin in platelet aggregation.Thrombospondin, a calcium-sensitive glycoprotein located in human blood platelet alpha-granules, is released from platelets upon stimulation [l]. Human platelet thrombospondin is composed of three equivalent disulphide-linked chains of 150 -160 kDa [2]. Isolated human platelet thrombospondin has been shown to interact with several proteins [2 -81. These thrombospondin-protein interactions suggest that thrombospondin may have several structural domains with independent functions. However, the functional domains of thrombospondin interacting with most of these proteins have still to be elucidated. The h...

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Plasma thrombospondin in patients with chronic renal failure, liver disease and splenectomy

Cited by 13 publications

References 25 publications

Disturbance of plasma and platelet thrombospondin levels in sickle cell disease

Disturbance of plasma and platelet thrombospondin levels in sickle cell disease

Thrombospondin in Clinical Disease States

Characterization of two murine monoclonal antibodies (P10, P12) directed against different determinants on human blood platelet thrombospondin

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