Calcium-independent contraction and sensitization of airway smooth muscle by p21-activated protein kinase.

Calcium-independent contraction and sensitization of airway smooth muscle by p21-activated protein kinase. Research Abstract Details 

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Calcium-independent contraction and sensitization of airway smooth muscle by p21-activated protein kinase. Abstract Text:

P K McFawn,L Shen,S G Vincent,A Mak,J E Van Eyk,J T Fisher,

In Triton-skinned phasic ileal smooth muscle, constitutively active recombinant p21-activated kinase (PAK3) has been shown to induce Ca(2+)-independent contraction, which is accompanied by phosphorylation of caldesmon and desmin (Van Eyk JE, Arrell DK, Foster DB, Strauss JD, Heinonen TY, Furmaniak-Kazmierczak E, Cote GP, and Mak AS. J Biol Chem 273: 23433-23439, 1998). In the present study, we investigated whether PAK has a broad impact on smooth muscle in general by testing the hypothesis that PAK induces Ca(2+)-independent contractions and/or Ca(2+) sensitization in tonic airway smooth muscle and that the process is mediated via phosphorylation of caldesmon. In the absence of Ca(2+) (pCa > 9), constitutively active glutathione-S-transferase-murine PAK3 (GST-mPAK3) caused force generation of Triton-skinned canine tracheal smooth muscle (TSM) fibers to approximately 40% of the maximal force generated by Ca(2+) at pCa 4.4. In addition, GST-mPAK3 enhanced Ca(2+) sensitivity of contraction by increasing force generation by 80% at intermediate Ca(2+) concentrations (pCa 6.2), whereas it had no effect at pCa 4.4. Catalytically inactive GST-mPAK3(K297R) had no effect on force production. Using antibody against one of the PAK-phosphorylated sites (Ser(657)) on caldesmon, we showed that a basal level of phosphorylation of caldesmon occurs at this site in skinned TSM and that PAK-induced contraction was accompanied by a significant increase in the level of phosphorylation. Western blot analyses show that PAK1 is the predominant PAK isoform expressed in murine, rat, canine, and porcine TSM. We conclude that PAK causes Ca(2+)-independent contractions and produces Ca(2+) sensitization of skinned phasic and tonic smooth muscle, which involves an incremental increase in caldesmon phosphorylation.

Calcium-independent contraction and sensitization of airway smooth muscle by p21-activated protein kinase. Publishing Authors By Initials

PK McFawn,L Shen,SG Vincent,A Mak,JE Van Eyk,JT Fisher,

For similar enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: p21-activated kinases research abstracts see: enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: p21-activated kinases research

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Calcium-independent contraction and sensitization of airway smooth muscle by p21-activated protein kinase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: American journal of physiology. Lung cellular and

VOLUME: 284

Page Numbers: L863-70

Journal Abbreviation: Am. J. Physiol. Lung Cell Mol.

ISSN: 1040-0605

DAY: 3

MONTH: 01

YEAR: 2003

Calcium-independent contraction and sensitization of airway smooth muscle by p21-activated protein kinase. Information

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LANGUAGE: eng

NlmUniqueID: 100901229

Calcium-independent contraction and sensitization of airway smooth muscle by p21-activated protein kinase. Keywords Mesh Terms:

KEYWORDS: p21-Activated Kinases

MESH TERMS: enzymology

Chemical & Substance for Abstract: Calcium-independent contraction and sensitization of airway smooth muscle by p21-activated protein kinase. Information

Substance Name: GTP-Binding Proteins

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Calcium-independent contraction and sensitization of airway smooth muscle by p21-activated protein kinase.

AFFILIATION: Department of Physiology, Queen's University, Kingston, Ontario, Canada K7L 3N6.

Country: United States

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MEDLINETA: Am J Physiol Lung Cell Mol Phy

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