High-affinity [3H]PN200-110 and [3H]ryanodine binding to rabbit and frog skeletal muscle.

Published

Journal Article

In vertebrate skeletal muscle, the voltage-dependent mechanism of sarcoplasmic reticulum (SR) Ca2+ release, commonly referred to as excitation-contraction (E-C) coupling, is mediated by the voltage-sensing dihydropyridine receptor (DHPR), which is believed to affect SR Ca2+ release through a physical interaction with the SR ryanodine receptor (RYR)/Ca2+ release channel. Scatchard analysis of ligand binding of [3H]PN200-110 to the DHPR and [3H]ryanodine to the RYR indicated the presence of high-affinity sites in muscle homogenates, with maximum binding (Bmax) values of 72 +/- 26 and 76 +/- 30 pmol/g wet wt for rabbit skeletal muscle, and 27 +/- 14 and 44 +/- 13 pmol/g wet wt for frog skeletal muscle, respectively. The Bmax values corresponded to a PN200-110-to-ryanodine binding ratio of 0.98 +/- 0.26 and 0.61 +/- 0.24 for rabbit and frog skeletal muscle, respectively, and were found by Student's t test to be significantly different (P < 0.02, n = 7). These results are compared with measurements with isolated rabbit skeletal muscle membrane fractions and discussed in relation to our current understanding of the mechanism of E-C coupling in skeletal muscle.

Full Text

Duke Authors

Cited Authors

  • Anderson, K; Cohn, AH; Meissner, G

Published Date

  • February 1994

Published In

Volume / Issue

  • 266 / 2 Pt 1

Start / End Page

  • C462 - C466

PubMed ID

  • 8141261

Pubmed Central ID

  • 8141261

International Standard Serial Number (ISSN)

  • 0002-9513

Digital Object Identifier (DOI)

  • 10.1152/ajpcell.1994.266.2.C462

Language

  • eng

Conference Location

  • United States