Loading…

Co-Localization of Immunoreactive Forms of Calponin with Actin Cytoskeleton in Platelets, Fibroblasts, and Vascular Smooth Muscle

Calponin is an actin binding protein found in the smooth muscle cells of chicken gizzard. The localization of the protein was examined in bovine platelets, mouse fibroblasts, and the smooth muscle cells of the bovine aorta. Immunoblotting of whole platelet lysates revealed that the antibody to chick...

Full description

Saved in:
Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1991-02, Vol.109 (2), p.311-316
Main Authors: Takeuchi, Kikuko, Takahashi, Kastuhito, Abe, Masahiro, Nishida, Wataru, Hiwada, Kunio, Nabeya, Takashi, Maruyama, Koscak
Format: Article
Language:English
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Calponin is an actin binding protein found in the smooth muscle cells of chicken gizzard. The localization of the protein was examined in bovine platelets, mouse fibroblasts, and the smooth muscle cells of the bovine aorta. Immunoblotting of whole platelet lysates revealed that the antibody to chicken gizzard calponin recognized two proteins with apparent molecular masses of 37 and 23 kDa in the resting state and an additional high-molecular-weight component (approximately 40 kDa) in the activated state. The localizations of calponin and caldesmon, and the correlation of their localizations with that of the actin cytoskeleton were analyzed by immunofluorescence microscopy using appropriate antibodies and rhodamine-phalloidin. In resting bovine platelets, calponin exhibited the same distribution as actin filaments, which are organized in a characteristic wheel-like structure. A similar distribution was observed with the anti-caldesmon antibody. Co-localizations of calponin and actin were shown in activated platelets and along stress fibers of both fibroblasts and smooth muscle cells. These results suggest not only a cytoskeletal role associated with microfilaments but also a regulatory role of these proteins for actin-myosin interaction.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a123379