calcimycin and 8-((4-bromo-2-3-dioxobutyryl)thio)adenosine-5-diphosphate

calcimycin has been researched along with 8-((4-bromo-2-3-dioxobutyryl)thio)adenosine-5-diphosphate* in 1 studies

Other Studies

1 other study(ies) available for calcimycin and 8-((4-bromo-2-3-dioxobutyryl)thio)adenosine-5-diphosphate

Article	Year
Inhibition of ADP-induced platelet responses by covalent modification of aggregin, a putative ADP receptor, by 8-(4-bromo-2,3-dioxobutylthio)ADP. The Journal of biological chemistry, 1995, Oct-13, Volume: 270, Issue:41 ADP is an important platelet agonist which initiates platelet shape change, aggregation, exposure of fibrinogen receptors, and calcium mobilization. Because of the limitations of previously used affinity analogs and photo-labeling studies as well as controversies surrounding the identity of an ADP receptor on platelets, we have used an affinity label capable of alkylating a putative exofacial receptor on platelets. We now report that 8-(4-bromo-2,3-dioxobutylthio)adenosine-5'-diphosphate (8-BDB-TADP), which is an analog of the natural ligand ADP, blocked ADP-induced platelet shape change, aggregation, exposure of fibrinogen-binding sites, secretion, and calcium mobilization. Following modification by 8-BDB-TADP, the rates of aggregation of platelets induced by thrombin, a calcium ionophore (A23187) or a stimulator of protein kinase C (phorbol myristate acetate) were minimally affected. However, the 8-BDB-TADP-modified platelets exhibited decreased rates of aggregation in response to ADP, as well as collagen and a thromboxane mimetic (U46619), both of which partially require ADP. Autoradiograms of the gels obtained by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of solubilized platelets modified by either [beta-32P]8-BDB-TADP, or 8-BDB-TADP and NaB[3H]4 showed the presence of a single radiolabeled protein band at 100 kDa. The intensity of this band was reduced when platelets were preincubated with ADP, ATP, and 8-bromo-ADP prior to labeling by the radioactive 8-BDB-TADP. The results show that 8-BDB-TADP selectively and covalently labeled aggregin (100 kDa), a putative ADP receptor, resulting in a loss of ADP-induced platelet responses. Topics: Adenosine Diphosphate; Affinity Labels; Autoradiography; Binding Sites; Blood Platelets; Calcimycin; Electrophoresis, Polyacrylamide Gel; Fibrinogen; Humans; In Vitro Techniques; Ionophores; Kinetics; Molecular Structure; Molecular Weight; Phosphorus Radioisotopes; Platelet Aggregation; Platelet Aggregation Inhibitors; Platelet Membrane Glycoproteins; Receptors, Purinergic P2; Thionucleotides; Thrombin	1995

Article

Year

Inhibition of ADP-induced platelet responses by covalent modification of aggregin, a putative ADP receptor, by 8-(4-bromo-2,3-dioxobutylthio)ADP.

The Journal of biological chemistry, 1995, Oct-13, Volume: 270, Issue:41

ADP is an important platelet agonist which initiates platelet shape change, aggregation, exposure of fibrinogen receptors, and calcium mobilization. Because of the limitations of previously used affinity analogs and photo-labeling studies as well as controversies surrounding the identity of an ADP receptor on platelets, we have used an affinity label capable of alkylating a putative exofacial receptor on platelets. We now report that 8-(4-bromo-2,3-dioxobutylthio)adenosine-5'-diphosphate (8-BDB-TADP), which is an analog of the natural ligand ADP, blocked ADP-induced platelet shape change, aggregation, exposure of fibrinogen-binding sites, secretion, and calcium mobilization. Following modification by 8-BDB-TADP, the rates of aggregation of platelets induced by thrombin, a calcium ionophore (A23187) or a stimulator of protein kinase C (phorbol myristate acetate) were minimally affected. However, the 8-BDB-TADP-modified platelets exhibited decreased rates of aggregation in response to ADP, as well as collagen and a thromboxane mimetic (U46619), both of which partially require ADP. Autoradiograms of the gels obtained by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of solubilized platelets modified by either [beta-32P]8-BDB-TADP, or 8-BDB-TADP and NaB[3H]4 showed the presence of a single radiolabeled protein band at 100 kDa. The intensity of this band was reduced when platelets were preincubated with ADP, ATP, and 8-bromo-ADP prior to labeling by the radioactive 8-BDB-TADP. The results show that 8-BDB-TADP selectively and covalently labeled aggregin (100 kDa), a putative ADP receptor, resulting in a loss of ADP-induced platelet responses.

Topics: Adenosine Diphosphate; Affinity Labels; Autoradiography; Binding Sites; Blood Platelets; Calcimycin; Electrophoresis, Polyacrylamide Gel; Fibrinogen; Humans; In Vitro Techniques; Ionophores; Kinetics; Molecular Structure; Molecular Weight; Phosphorus Radioisotopes; Platelet Aggregation; Platelet Aggregation Inhibitors; Platelet Membrane Glycoproteins; Receptors, Purinergic P2; Thionucleotides; Thrombin

1995