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PMID: 8033336 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Tropomodulin in rat cardiac muscle. Localization of protein is independent of messenger RNA distribution during myofibrillar development.

Circulation research ·Vol. 75 ·No. 2 ·1994-08-00 ·Pages 221-32

Sussman MA, Sakhi S, Barrientos P, Ito M, Kedes L

Abstract

Tropomodulin is a 40.6-kD protein that colocalizes with actin filament pointed ends in skeletal muscle. We report the sequence of two partial-length complementary DNA (cDNA) clones of rat cardiac tropomodulin that cover 90% of the coding region. The cDNA sequence is 90% conserved between human and rat, with the predicted amino acid sequence similarity even higher at 95%. Anti-tropomodulin antibodies label a single polypeptide with an apparent mobility of 43,000 in Western blot analysis of rat cardiac muscle. Immunofluorescence experiments using this anti-tropomodulin antibody result in labeling that is coincident with thin filament ends, as demonstrated by double localization with alpha-actinin antibody. Tropomodulin protein is organized into a sarcomeric staining pattern with the earliest appearance of myofibrils in rat cardiocytes. The localization of tropomodulin protein at or near thin filament ends led us to examine the distribution of tropomodulin messenger RNA (mRNA) during myofibrillar development in vitro. Fluorescent in situ hybridization experiments using tropomodulin cDNA probe in cardiocytes that have been cultured for 3 to 5 days show a distribution of large mRNA patches. The cytoplasmic location of tropomodulin mRNA at this time, which bears no relation to the developed myofibrils, suggests that tropomodulin protein is targeted to thin filament ends rather than using localized translational machinery. However, the distribution of tropomodulin mRNA in cultured cardiocytes changes over the next 2 weeks from large perinuclear patches to small concentrations arranged along myofibrils throughout the cell. The reorganization of tropomodulin mRNA throughout the cardiocyte appears to be distinct from the pattern of glyceraldehyde-3-phosphate dehydrogenase mRNA within the same time period. Increasing intracellular density of myofibrils within developing cardiocytes may lead to redistribution of selected mRNAs for localized translation.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Blotting, Western Carrier Proteins/genetics,metabolism Cellular Senescence Cloning, Molecular Fluorescent Antibody Technique Glyceraldehyde-3-Phosphate Dehydrogenases/genetics Humans Microfilament Proteins Myofibrils/physiology Papillary Muscles/metabolism RNA, Messenger/metabolism Rats Tissue Distribution Tropomodulin
Chemicals
Carrier Proteins Microfilament Proteins RNA, Messenger TMOD1 protein, human Tmod1 protein, rat Tropomodulin Glyceraldehyde-3-Phosphate Dehydrogenases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Sussman M A
Institute for Genetic Medicine, University of Southern California, School of Medicine, Los Angeles 90033.
Sakhi S
Barrientos P
Ito M
Kedes L
Article Info
Journal
Circulation research
Abbr.
Circ Res
ISSN
0009-7330
Published
1994-08-00
Pages
221-32
Language
English
Region
United States
NLM ID
0047103
Subset
IM
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