Compounds > adenosine-5--o-(3-thiotriphosphate)

adenosine-5--o-(3-thiotriphosphate) and protein-kinase-inhibitor-peptide

adenosine-5--o-(3-thiotriphosphate) has been researched along with protein-kinase-inhibitor-peptide* in 1 studies

Other Studies

1 other study(ies) available for adenosine-5--o-(3-thiotriphosphate) and protein-kinase-inhibitor-peptide

Article	Year
Activation of KCa channels in airway smooth muscle cells by endogenous protein kinase A. The American journal of physiology, 1996, Volume: 271, Issue:1 Pt 1 The regulation of calcium-activated potassium (KCa) channels by endogenous protein kinase A (PKA) was examined in inside-out patches from equine tracheal myocytes. In the absence of exogenous protein kinases, ATP (500 microM) significantly augmented KCa channel activity when applied to the cytosolic patch surface [open-state probability (nP0, mean +/- SE) increased from 0.010 +/- 0.001 to 0.034 +/- 0.005 (n = 24)]. The stimulatory effect of ATP was mimicked by ATP-gamma-S but not by AMP-PNP. Rather, AMP-PNP significantly inhibited channel activity. The PKA inhibitory peptide (PKI) significantly reduced nPo and prevented the augmenting effect of subsequent ATP. Ht 31, an inhibitory peptide for A-kinase-anchoring proteins (AKAP), but not its proline-substituted mutant, also blocked the stimulatory effect of ATP. These results suggest that 1) ATP augments KCa channel activity through phosphorylation; 2) the phosphorylation is catalyzed by endogenous PKA; 3) anchoring via AKAP is required to maintain association of PKA with the membrane; and 4) in a newly obtained patch, some of the KCa channels are probably already in a phosphorylated state. Topics: Adenosine Triphosphate; Adenylyl Imidodiphosphate; Animals; Calcium; Cyclic AMP-Dependent Protein Kinases; Electrophysiology; Horses; Muscle, Smooth; Peptides; Potassium Channels; Trachea	1996

Article

Year

Activation of KCa channels in airway smooth muscle cells by endogenous protein kinase A.

The American journal of physiology, 1996, Volume: 271, Issue:1 Pt 1

The regulation of calcium-activated potassium (KCa) channels by endogenous protein kinase A (PKA) was examined in inside-out patches from equine tracheal myocytes. In the absence of exogenous protein kinases, ATP (500 microM) significantly augmented KCa channel activity when applied to the cytosolic patch surface [open-state probability (nP0, mean +/- SE) increased from 0.010 +/- 0.001 to 0.034 +/- 0.005 (n = 24)]. The stimulatory effect of ATP was mimicked by ATP-gamma-S but not by AMP-PNP. Rather, AMP-PNP significantly inhibited channel activity. The PKA inhibitory peptide (PKI) significantly reduced nPo and prevented the augmenting effect of subsequent ATP. Ht 31, an inhibitory peptide for A-kinase-anchoring proteins (AKAP), but not its proline-substituted mutant, also blocked the stimulatory effect of ATP. These results suggest that 1) ATP augments KCa channel activity through phosphorylation; 2) the phosphorylation is catalyzed by endogenous PKA; 3) anchoring via AKAP is required to maintain association of PKA with the membrane; and 4) in a newly obtained patch, some of the KCa channels are probably already in a phosphorylated state.

Topics: Adenosine Triphosphate; Adenylyl Imidodiphosphate; Animals; Calcium; Cyclic AMP-Dependent Protein Kinases; Electrophysiology; Horses; Muscle, Smooth; Peptides; Potassium Channels; Trachea

1996