Phosphorylation by protein kinase C of the 20,000-dalton light chain of myosin in intact and chemically skinned vascular smooth muscle.

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Population

Porcine carotid artery smooth muscle (intact and chemically-permeabilized/glycerinated)

Comparison

Phosphorylation of LC20 by purified protein… vs Ca2+/calmodulin-activated muscles or…

Design

Preclinical

Authors

Discussion

PKC phosphorylation of LC20 does not regulate contraction in porcine carotid artery; leaves open its role in other vascular models or species.

Population

Porcine carotid artery smooth muscle (intact and chemically-permeabilized/glycerinated)

Intervention

Phosphorylation of LC20 by purified protein kinase C and oleic acid, or phorbol 12,13-dibutyrate

Comparator

Ca2+/calmodulin-activated muscles or unphosphorylated state

Outcome

Muscle contraction (isometric force and lightly-loaded shortening velocity)surrogate

Phosphorylation of the 20,000-dalton myosin light chain by protein kinase C does not regulate contraction in porcine carotid artery smooth muscle.

Sutton et al. (1990) studied this question.

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PKC phosphorylation of LC20 does not regulate contraction in porcine carotid artery; leaves open its role in other vascular models or species.