NDLI: Myosin filament polymerization and depolymerization in a model of partial length adaptation in airway smooth muscle.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ijpma, Gijs Al-Jumaily, Ahmed M. Cairns, Simeon P. Sieck, Gary C.
Description	Country affiliation: New Zealand Author Affiliation: Ijpma G ( Institute of Biomedical Technologies, Auckland University of Technology, Auckland, New Zealand.)
Abstract	Length adaptation in airway smooth muscle (ASM) is attributed to reorganization of the cytoskeleton, and in particular the contractile elements. However, a constantly changing lung volume with tidal breathing (hence changing ASM length) is likely to restrict full adaptation of ASM for force generation. There is likely to be continuous length adaptation of ASM between states of incomplete or partial length adaption. We propose a new model that assimilates findings on myosin filament polymerization/depolymerization, partial length adaptation, isometric force, and shortening velocity to describe this continuous length adaptation process. In this model, the ASM adapts to an optimal force-generating capacity in a repeating cycle of events. Initially the myosin filament, shortened by prior length changes, associates with two longer actin filaments. The actin filaments are located adjacent to the myosin filaments, such that all myosin heads overlap with actin to permit maximal cross-bridge cycling. Since in this model the actin filaments are usually longer than myosin filaments, the excess length of the actin filament is located randomly with respect to the myosin filament. Once activated, the myosin filament elongates by polymerization along the actin filaments, with the growth limited by the overlap of the actin filaments. During relaxation, the myosin filaments dissociate from the actin filaments, and then the cycle repeats. This process causes a gradual adaptation of force and instantaneous adaptation of shortening velocity. Good agreement is found between model simulations and the experimental data depicting the relationship between force development, myosin filament density, or shortening velocity and length.
File Format	HTM / HTML
ISSN	87507587
e-ISSN	15221601
DOI	10.1152/japplphysiol.00114.2011
Journal	Journal of Applied Physiology
Issue Number	3
Volume Number	111
Language	English
Publisher	American Physiological Society
Publisher Date	2011-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Physiology Cell Size Cytoskeleton Metabolism Lung Models, Biological Muscle Contraction Muscle, Smooth Myocytes, Smooth Muscle Myosins Actins Adaptation, Physiological Animals Biomechanical Phenomena Compliance Cytology Muscle Strength Protein Multimerization Reproducibility Of Results Stochastic Processes Time Factors
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Sports Science

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