Studies with synthetic peptide substrates derived from the neuronal protein neurogranin reveal structural determinants of potency and selectivity for protein kinase C

Biochemistry ◽  
1993 ◽  
Vol 32 (4) ◽  
pp. 1032-1039 ◽  
Author(s):  
Shu Jen Chen ◽  
Eric Klann ◽  
Morganne C. Gower ◽  
Craig M. Powell ◽  
J. Suzanne Sessoms ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Synthetic Peptide ◽  
Structural Determinants ◽  
Peptide Substrates ◽  
Neuronal Protein ◽  
Kinase C

scholarly journals Ca2+ phospholipid-dependent and independent phosphorylation of synthetic peptide substrates by protein kinase C

1987 ◽  
Vol 163 (3) ◽  
pp. 481-487 ◽  
Author(s):  
Stefano FERRARI ◽  
Fernando MARCHIORI ◽  
Oriano MARIN ◽  
Lorenzo A. PINNA
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Synthetic Peptide ◽  
Peptide Substrates ◽  
Kinase C

A synthetic peptide substrate for selective assay of protein kinase C

1990 ◽  
Vol 166 (3) ◽  
pp. 1220-1227 ◽  
Author(s):  
Ichiro Yasuda ◽  
Akira Kishimoto ◽  
Shin-ichiro Tanaka ◽  
Masahiro Tominaga ◽  
Atsushi Sakurai ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Synthetic Peptide ◽  
Peptide Substrate ◽  
Kinase C

Calcium mobilization and glycoprotein IIb-IIIa complex ligands in epinephrine-stimulated platelets

1991 ◽  
Vol 260 (5) ◽  
pp. H1619-H1624
Author(s):  
J. A. Ware ◽  
M. T. Decenzo ◽  
M. Smith ◽  
M. Saitoh
Keyword(s):  
Protein Kinase C ◽  
Platelet Aggregation ◽  
Protein Kinase ◽  
Synthetic Peptide ◽  
Platelet Surface ◽  
Epinephrine Administration ◽  
Kinase C ◽  
Fibrinogen Binding ◽  
Peptide Analogues ◽  
Protein Kinase C Activation

In the presence of extracellular Ca2+, epinephrine induces a rise in cytoplasmic Ca2+ ([Ca2+]i) that is associated with fibrinogen binding to the platelet surface, platelet aggregation, and enhancement of the thrombin-stimulated [Ca2+]i rise and protein phosphorylation. Whether the [Ca2+]i rise induced by epinephrine results from Ca2+ entry associated with fibrinogen binding to its receptor on the platelet surface, the glycoprotein (gp) IIb-IIIa complex, is unknown. To determine the importance of the occupancy of the gp IIb-IIIa receptor on platelet function after epinephrine administration, we studied the effects of two monoclonal antibodies (M-148 and 7E3) and two synthetic peptide analogues to fibrinogen (synthetic tetrapeptides Arg-Gly-Asp-Ser (RGDS) and dodecapeptide His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val [gamma-(400-411)]), all of which bind to gp IIb-IIIa and inhibit fibrinogen binding and platelet aggregation on the epinephrine-induced rise in [Ca2+]i and enhancement of thrombin's phosphorylation of the 47-kDa substrate of protein kinase C (p47). None of the gp IIb-IIIa ligands significantly enhanced or inhibited the epinephrine-induced [Ca2+]i rise or its augmentation of p47 phosphorylation after thrombin administration; however, the synergistic [Ca2+]i rise that follows addition of both epinephrine and thrombin was reduced by both antibodies and both peptides. Thus ligand binding of gp IIb-IIIa does not influence the epinephrine-induced [Ca2+]i rise or its promotion of protein kinase C activation by thrombin; these events can be dissociated from the synergistic [Ca2+]i rise.

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