By Richard A. Murphy (auth.)
The ambitions during this distinct factor are (1) to seriously assessment present info at the mechanisms coupling extracellular regulatory signs to rules of cross-bridge biking and proliferation in soft muscle, and (2) determine major gaps or unresolved matters which are vital issues for destiny study. The experimental and analytical problems mentioned above are more and more famous and surmounted. Elucidation of the molecular and mobile occasions underlying the biologal houses of delicate muscle is in the middle of a interval of swift growth. whereas the stories exhibit many gaps to be crammed and illustrate parts of competition, additionally they catch the buzz of recent discoveries.
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Extra resources for Reviews of Physiology Biochemistry and Pharmacology, Volume 134
Example text
Mabuchi et al (1996) concluded that caldesmon was associated selectively with contractile actin, whereas catponin associated selectively with cytoskeletal actin. Biochemical data obtained by Lehman (1991) appears to support ultrastructural evidence that calponin is selectively bound to a subset of actin filaments. Using calponin and caldesmon-specific antibodies to immunoprecipitate thin filament fractions, Lehman et al obtained subsets of actin filaments which were selectively enriched in either calponin and filamin or in caldesmon.
Dependence on tissue type. ] Biol Chem 259:1438314388 Fay FS, Fujiwara K, Rees DD, Fogarty KE (1983) Distribution of alpha-actinin in single isolated smooth muscle cells. J Cell Bio196:783795 Fisher AJ, Smith CA, Thoden J, Smith R, Sutoh K, Holden HM, Rayment I (1995a) Structural studies of myosin:nucleotide complexes: a revised model for the molecular basis of muscte contraction. A1F4-. Biochem 34:89608972 Fowler VM (1996) Regulation of actin filament length in erythrocytes and striated muscle.
Among these are filamin (also called actin binding protein (ABP)), the calponinlike protein SM22, and myosin light chain kinase (Lin et a11997). Very little is currently known about the function of SM22. Filamin is particularly abundant in smooth muscle tissues, estimated as 30-40% of the myosin content. It is not specific for smooth muscle and is also present in many other tissues and cell types (Wang 1977). Filamin is a large homodimer which belongs to a class of rod-shaped Ca2+-insensitive actin cross-linking proteins (Craig and Pollard I982, Geiger 1983).