Smooth muscle length-dependent PI(4,5)P2 synthesis and paxillin tyrosine phosphorylation

Donggeun Sul, Carl B. Baron, Raymond Broome, Ronald F. Coburn

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

We studied effects of increasing the length of porcine trachealis muscle on 5.5 μM carbachol (CCh)-evoked phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] synthesis and other parameters of phosphatidylinositol (PI) turnover. PI(4,5)P2 resynthesis rates in muscle held at 1.0 optimal length (L0), measured over the first 6 min of CCh stimulation, were 140 ± 12 and 227 ± 14% of values found in muscle held at 0.5 L0 and in free-floating muscle, respectively. Time-dependent changes in cellular masses of PI(4,5)P2, PI, and phosphatidic acid, and PI resynthesis rates, were also altered by the muscle length at which contraction occurred. In free-floating muscle, CCh did not evoke increases in tyrosine-phosphorylated paxillin (PTyr-paxillin), an index of β1-integrin signaling; however, there were progressive increases in PTyr-paxillin in muscle held at 0.5 and 1.0 L0 during contraction, which correlated with increases in PI(4,5)P2 synthesis rates. These data indicate that PI(4,5)P2 synthesis rates and other parameters of CCh-stimulated inositol phospholipid turnover are muscle length-dependent and provide evidence that supports the hypothesis that length-dependent β1-integrin signals may exert control on CCh-activated PI(4,5)P2 synthesis.

Original languageEnglish
Pages (from-to)C300-C310
JournalAmerican Journal of Physiology - Cell Physiology
Volume281
Issue number1 50-1
DOIs
Publication statusPublished - 2001
Externally publishedYes

Keywords

  • Airway smooth muscle
  • Integrins
  • Phosphatidylinositol 4,5-bisphosphate
  • Phosphatidylinositol 4-kinase
  • Smooth muscle mechanical strain

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Fingerprint Dive into the research topics of 'Smooth muscle length-dependent PI(4,5)P<sub>2</sub> synthesis and paxillin tyrosine phosphorylation'. Together they form a unique fingerprint.

Cite this