PMID: 9178612Jun 1, 1997Paper

Dihydropyridine receptor-ryanodine receptor uncoupling in aged skeletal muscle

The Journal of Membrane Biology
M RenganathanOsvaldo Delbono

Abstract

The mechanisms underlying skeletal muscle functional impairment and structural changes with advanced age are only partially understood. In the present study, we support and expand our theory about alterations in sarcolemmal excitation-sarcoplasmic reticulum Ca2+ release-contraction uncoupling as a primary skeletal muscle alteration and major determinant of weakness and fatigue in mammalian species including humans. To test the hypothesis that the number of RYR1 (ryanodine receptor) uncoupled to DHPR (dihydropyridine receptor) increases with age, we performed high-affinity ligand binding studies in soleus, extensor digitorum longus (EDL) and in a pool of several skeletal muscles consisting of a mixture of fast- and slow-twitch muscle fibers in middle-aged (14-month) and old (28-months) Fisher 344 Brown Norway F1 hybrids rats. The number of DHPR, RYR1, the coupling between both receptors expressed as the DHPR/RYR1 maximum binding capacity, and their dissociation constant for high-affinity ligands were measured. The DHPR/RYR1 ratio was significantly reduced in the three groups of muscles (pool: 1.03 +/- 0.15 and 0.80 +/- 0.11, soleus: 0.44 +/- 0. 12 and 0.26 +/- 0.10, and EDL: 0.95 +/- 0.14 and 0.68 +/- 0.10, for middle-aged and o...Continue Reading

Citations

Jul 11, 2008·The Journal of Nutrition, Health & Aging·D SumukadasM E T McMurdo
Feb 3, 2007·European Journal of Applied Physiology·Giuseppe D'AntonaRoberto Bottinelli
Jan 18, 2012·Pflügers Archiv : European journal of physiology·Zhong-Min WangOsvaldo Delbono
Aug 23, 2007·In Vitro Cellular & Developmental Biology. Animal·Zhong-Min WangOsvaldo Delbono
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Nov 19, 2005·The Journal of Physiology·Anthony M PayneOsvaldo Delbono
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