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PMID: 6282935 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Human platelets contain gelsolin. A regulator of actin filament length.

The Journal of clinical investigation ·Vol. 69 ·No. 6 ·1982-06-00 ·Pages 1384-7

Lind SE, Yin HL, Stossel TP

Abstract

Morphologic and biochemical studies suggest that actin in human platelets polymerizes in response to various stimuli and that shortening of actin filaments can be regulated by calcium. We report that human platelets contain gelsolin, a protein of Mr 91,000 that binds reversibly to actin in the presence of calcium. Platelet gelsolin exhibits immunologic crossreactivity with rabbit macrophage gelsolin and shortens actin filaments as demonstrated by viscosity measurements and gel point determinations. Gelsolin is active in micromolar calcium concentrations and its effects upon actin filaments are reversible. Gelsolin may be a dynamic regulator of actin filament length in the human platelet.

MeSH Terms
Actins/metabolism Blood Platelets/analysis Calcium/metabolism Calcium-Binding Proteins/isolation & purification,metabolism Chromatography, Affinity Cytoskeleton Gelsolin Humans Macrophages
Chemicals
Actins Calcium-Binding Proteins Gelsolin Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Lind S E
Yin H L
Stossel T P
References (15)
15 references, click to expand
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Article Info
Journal
The Journal of clinical investigation
Abbr.
J Clin Invest
ISSN
0021-9738
Published
1982-06-00
Pages
1384-7
Language
English
Region
United States
NLM ID
7802877
PMCID
PMC370211
Subset
IM
Grants
NCI NIH HHS · CA 09321 · United States
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