Home LiteratureArticle Details
PMID: 3987897 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Disassembly and reconstitution of the Ca2+-sensitive thin filaments of vascular smooth muscle.

FEBS letters ·Vol. 184 ·No. 1 ·1985-05-06 ·Pages 115-9

Smith CW, Marston SB

Abstract

The Ca2+-sensitive thin filaments of aorta smooth muscle have been, disassembled into their constituent proteins, actin, tropomyosin and a 120-kDa protein. The 120-kDa protein bound to aorta actin-tropomyosin and inhibited its ability to activate myosin MgATPase. This inhibition correlated with the binding of one 120-kDa protein molecule per 29 actin monomers. Upon the addition of calmodulin to the actin-tropomyosin-120-kDa protein complex, the inhibition was relieved in 10(-4) M Ca2+ but not 10(-9) M Ca2+. The full release of inhibition was not accompanied by a full release of 120-kDa protein binding to actin-tropomyosin. A fully active, Ca2+-sensitive aorta thin filament has thus been reconstituted from just four components: actin, tropomyosin, 120-kDa protein and calmodulin.

MeSH Terms
Actins/physiology Animals Aorta/analysis Calcium/pharmacology Calmodulin/pharmacology Muscle Proteins/physiology Muscle, Smooth, Vascular/analysis,metabolism Sheep Tropomyosin/physiology
Chemicals
Actins Calmodulin Muscle Proteins Tropomyosin Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Smith C W
Marston S B
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1985-05-06
Pages
115-9
Language
English
Region
England
NLM ID
0155157
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com