IDENTIFICATION AND LOCALIZATION OF IMMUNOREACTIVE FORMS OF CALDESMON IN SMOOTH AND NONMUSCLE CELLS - A COMPARISON WITH THE DISTRIBUTIONS OF TROPOMYOSIN AND ALPHA-ACTININ
IDENTIFICATION AND LOCALIZATION OF IMMUNOREACTIVE FORMS OF CALDESMON IN SMOOTH AND NONMUSCLE CELLS - A COMPARISON WITH THE DISTRIBUTIONS OF TROPOMYOSIN AND ALPHA-ACTININ
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DOI:
10.1083/jcb.100.5.1656
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发表时间:
1985-01-01
影响因子:
7.8
通讯作者:
LYNCH, W
中科院分区:
文献类型:
--
作者:
BRETSCHER, A;LYNCH, W
Caldesmon is an F-actin cross-linking protein of chicken gizzard smooth muscle whose F-actin binding activity can be regulated in vitro by Ca2+-calmodulin. It is a rod-shaped, heat-stable, F-actin bundling protein and is the most abundant F-actin cross-linking protein of chicken gizzard smooth muscle presently known. Polyclonal antibodies to caldesmon are used to investigate its distribution and localization in other cells. Immune blotting procedures, detected immunoreactive, heat-stable forms of caldesmon in cultured cells having either approximately the same apparent polypeptide MW as gizzard caldesmon (120,000-140,000) or a substantially lower MW (71,000-77,000). Through use of affinity-purified antibodies in indirect immunofluorescence microscopy, the immunoreactive forms were localized to the terminal web of the brush border of intestinal epithelial cells and to the stress fibers and ruffling membranes of cultured cells. At the light microscope level caldesmon is distributed in a periodic fashion along stress fibers that is coincident with the distribution of tropomyosin and complementary to the distribution of .alpha.-actinin.