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This Article Full Text Full Text (PDF) Supplemental Material All Versions of this Article: 289/5/C1277    most recent 00244.2004v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Web of Science (7) Citing Articles via Google Scholar Google Scholar Articles by Léguillette, R. Articles by Lauzon, A.-M. Search for Related Content PubMed PubMed Citation Articles by Léguillette, R. Articles by Lauzon, A.-M.

MUSCLE CELL BIOLOGY AND CELL MOTILITY

(+)Insert smooth muscle myosin heavy chain (SM-B) isoform expression in human tissues

¹Meakins-Christie Laboratories, McGill University, Montreal, Quebec, Canada; and ²Institute for Biomedical Aging Research, Austrian Academy of Sciences, Innsbruck, Austria

Submitted 14 May 2004 ; accepted in final form 28 June 2005

Two smooth muscle myosin heavy chain isoforms differ in their amino terminus by the presence [(+)insert] or absence [(–)insert] of a seven-amino acid insert. Animal studies show that the (+)insert isoform is predominantly expressed in rapidly contracting phasic muscle and the (–)insert isoform is mostly found in slowly contracting tonic muscle. The expression of the (+)insert isoform has never been demonstrated in human smooth muscle. We hypothesized that the (+)insert isoform is present in humans and that its expression is commensurate with the organ's functional requirements. We report, for the first time, the sequence of the human (+)insert isoform and quantification of its expression by real-time PCR and Western blot analysis in a panel of human organs. The (+)insert isoform mRNA and protein expression levels are significantly greater in small intestine compared with all organs studied except for trachea and are significantly greater in trachea compared with uterus and aorta. To assess the functional significance of this differential myosin isoform expression between organs, we measured the rate of actin filament movement (_max) when propelled by myosin purified from rat organs, because the rat and human inserts are identical and their remaining sequences show 93% identity. _max exhibits a rank correlation from the most tonic to the most phasic organ. The selective expression of the (+)insert isoform observed among human organs suggests that it is an important determinant of tissue shortening velocity. A differential expression of the (+)insert isoform could also account for altered contractile properties observed in human pathology.

phasic and tonic smooth muscle; real-time polymerase chain reaction; in vitro motility assay

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