Cytoskeletal remodeling of the airway smooth muscle cell: A mechanism for adaptation to mechanical forces in the lung

Susan J. Gunst, Dale D. Tang, Anabelle Opazo Saez

Research output: Contribution to journalArticle

114 Scopus citations

Abstract

Airway smooth muscle is continuously subjected to mechanical forces caused by changes in lung volume during breathing. These mechanical oscillations have profound effects on airway smooth muscle contractility both in vivo and in vitro. Alterations in airway smooth muscle properties in response to mechanical forces may result from adaptive changes in the organization of the actin cytoskeleton. Recent advances suggest that in airway smooth muscle, two cytosolic signaling proteins that associate with focal adhesion complexes, focal adhesion kinase (FAK) and paxillin, are involved in transducing external mechanical signals. FAK and paxillin regulate changes in the organization of the actin cytoskeleton and the activation of contractile proteins. Actin is in a dynamic state in airway smooth muscle and undergoes polymerization and depolymerization during the contraction-relaxation cycle. The organization of the cytoskeletal proteins, vinculin, talin, and α-actinin, which mediate linkages between actin filaments and transmembrane integrins, is also regulated by contractile stimulation in airway smooth muscle. The fluidity of the cytoskeletal structure of the airway smooth muscle cell may be fundamental to its ability to adapt and respond to the mechanical forces imposed on it in the lung during breathing.

Original languageEnglish (US)
Pages (from-to)151-168
Number of pages18
JournalRespiratory Physiology and Neurobiology
Volume137
Issue number2-3
DOIs
StatePublished - Sep 16 2003

Keywords

  • Adaptive changes
  • Adhesion
  • Airway
  • Cytoskeletal signaling
  • Enzyme
  • FAK
  • Focal
  • Focal adhesion kinase
  • Muscle
  • Paxillin
  • Proteins
  • Smooth
  • Smooth muscle

ASJC Scopus subject areas

  • Physiology
  • Pulmonary and Respiratory Medicine
  • Neuroscience(all)

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