HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: 285/2/C419    most recent 00502.2002v1 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 ISI 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 ISI Web of Science (10) Citing Articles via Google Scholar Google Scholar Articles by Ramamurthy, B. Articles by Larsson, L. Search for Related Content PubMed PubMed Citation Articles by Ramamurthy, B. Articles by Larsson, L.

MUSCLE CELL BIOLOGY AND CELL MOTILITY

Glutathione reverses early effects of glycation on myosin function

¹Noll Physiological Research Center and ²Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802; ³Department of Cellular and Molecular Physiology, Hershey Medical Center, Pennsylvania State University, Hershey, Pennsylvania 17033; and ⁴Department of Clinical Neurophysiology, University Hospital, SE-751 85 Uppsala, Sweden

Submitted 29 October 2002 ; accepted in final form 13 April 2003

Nonenzymatic glycosylation (glycation) has been recognized as an important posttranslational modification underlying alterations of structure and function of extracellular proteins during aging and diabetes. Intracellular proteins may also be affected by this modification, and glycation has been suggested to contribute to aging-related impairment in skeletal muscle function. Glycation is the chemical reaction of reducing sugars with primary amino groups resulting in the formation of irreversible advanced glycation end products. Glutathione is an abundant tripeptide in skeletal muscle. To understand the effect of glutathione on glycated myosin function, we used a single-fiber in vitro motility assay in which myosin is extracted from a single muscle fiber segment to propel fluorescent-labeled actin filaments. Myosin function responded to glucose exposure in a dose-dependent manner, i.e., motility speeds were reduced by 10, 34, and 90% of preincubation values after 30-min exposure to 1, 3, and 6 mM glucose, respectively. The 30-min 6 mM glucose incubation was followed by a 20-min 10 mM glutathione incubation. Glutathione treatment restored motility (0.98 ± 0.06 µm/s, n = 3; P < 0.001) after glucose exposure (0.10 ± 0.07 µm/s, n = 3), close to preincubation levels (1.12 ± 0.06 µm/s, n = 3). It is concluded that glucose modifies myosin function in a dose-dependent manner and that glutathione reverses the effect of glucose on myosin function.

in vitro motility; skeletal muscle fibers; speed of contraction

This article has been cited by other articles:

				A.A. Sayer, H.E. Syddall, E.M. Dennison, H.J. Martin, D.I.W. Phillips, C. Cooper, and C.D. Byrne Grip strength and the metabolic syndrome: findings from the Hertfordshire Cohort Study QJM, November 1, 2007; 100(11): 707 - 713. [Abstract] [Full Text] [PDF]

				M. Canepari, R. Rossi, M. A. Pellegrino, R. W. Orrell, M. Cobbold, S. Harridge, and R. Bottinelli Effects of resistance training on myosin function studied by the in vitro motility assay in young and older men J Appl Physiol, June 1, 2005; 98(6): 2390 - 2395. [Abstract] [Full Text] [PDF]

				A. M. Payne, S. L. Dodd, and C. Leeuwenburgh Life-long calorie restriction in Fischer 344 rats attenuates age-related loss in skeletal muscle-specific force and reduces extracellular space J Appl Physiol, December 1, 2003; 95(6): 2554 - 2562. [Abstract] [Full Text]