Identification of two distinct proteins that are immunologically related to the alpha 1 subunit of the skeletal muscle dihydropyridine-sensitive calcium channel - PubMed (original) (raw)
Comparative Study
. 1992 Sep 5;267(25):18218-23.
Affiliations
- PMID: 1325462
Free article
Comparative Study
Identification of two distinct proteins that are immunologically related to the alpha 1 subunit of the skeletal muscle dihydropyridine-sensitive calcium channel
R M Brawley et al. J Biol Chem. 1992.
Free article
Abstract
The alpha 1 subunit of the dihydropyridine-sensitive calcium channel is a protein which is critical for excitation-contraction coupling and L-type calcium current in skeletal muscle. Using antibodies generated against peptides from three regions of the deduced amino acid sequence of the alpha 1 subunit, we have identified two distinct proteins in rabbit skeletal muscle. Both proteins appeared to be recognized by antibodies against the amino (N) terminus of the alpha 1 subunit sequence. One protein was also recognized by antibodies against an internal (I) region of the predicted sequence but not by antibodies against the carboxyl (C) terminus. In contrast, the other protein was recognized by antibodies against the carboxyl terminus but not by the antibodies against the internal region. We have designated these proteins pNI and pNC based on their patterns of antibody recognition. No protein was detected which was recognized by all three antibodies. pNI is the protein commonly identified as the alpha 1 subunit of the dihydropyridine-sensitive calcium channel. Of note is that pNI, which apparently lacks sequences from the predicted carboxyl tail, is the protein present in preparations which we have previously demonstrated contain dihydropyridine-sensitive calcium channel activity. pNC is herein identified as a skeletal muscle protein that is immunologically related to the alpha 1 subunit of the dihydropyridine-sensitive calcium channel. Its function is unknown. In addition to their distinct patterns of antibody recognition, pNI and pNC were also distinguishable by several other properties. pNC migrated as a protein of approximately 160 kDa in 5% sodium dodecyl sulfate-polyacrylamide gels versus approximately 165 kDa for pNI. pNI was enriched in transverse tubule membranes, whereas pNC was found to be enriched in triad and junctional sarcoplasmic reticulum membrane fractions and was not found in transverse tubule membranes. Under conditions in which pNI bound to wheat germ agglutinin-Sepharose, pNC did not bind. The results demonstrate that there are two proteins in skeletal muscle which are immunologically related to the alpha 1 subunit of the dihydropyridine-sensitive calcium channel but which are distinguishable by several biochemical and immunological characteristics.
Similar articles
- Subunits of purified calcium channels: a 212-kDa form of alpha 1 and partial amino acid sequence of a phosphorylation site of an independent beta subunit.
De Jongh KS, Merrick DK, Catterall WA. De Jongh KS, et al. Proc Natl Acad Sci U S A. 1989 Nov;86(21):8585-9. doi: 10.1073/pnas.86.21.8585. Proc Natl Acad Sci U S A. 1989. PMID: 2554320 Free PMC article. - Identification of a novel 1,4-dihydropyridine- and phenylalkylamine-binding polypeptide in calcium channel preparations.
Vaghy PL, Striessnig J, Miwa K, Knaus HG, Itagaki K, McKenna E, Glossmann H, Schwartz A. Vaghy PL, et al. J Biol Chem. 1987 Oct 15;262(29):14337-42. J Biol Chem. 1987. PMID: 2443504 - Primary structure of the gamma subunit of the DHP-sensitive calcium channel from skeletal muscle.
Jay SD, Ellis SB, McCue AF, Williams ME, Vedvick TS, Harpold MM, Campbell KP. Jay SD, et al. Science. 1990 Apr 27;248(4954):490-2. doi: 10.1126/science.2158672. Science. 1990. PMID: 2158672 - The dihydropyridine-sensitive calcium channel of the skeletal muscle: biochemistry and structure.
Nastainczyk W, Ludwig A, Hofmann F. Nastainczyk W, et al. Gen Physiol Biophys. 1990 Aug;9(4):321-9. Gen Physiol Biophys. 1990. PMID: 2177019 Review. - Molecular properties of dihydropyridine-sensitive calcium channels in skeletal muscle.
Catterall WA, Seagar MJ, Takahashi M. Catterall WA, et al. J Biol Chem. 1988 Mar 15;263(8):3535-8. J Biol Chem. 1988. PMID: 2450086 Review. No abstract available.
Cited by
- Dihydropyridine receptors in transverse tubules from normal and dystrophic chicken skeletal muscle.
Moro G, Saborido A, Delgado J, Molano F, Megias A. Moro G, et al. J Muscle Res Cell Motil. 1995 Oct;16(5):529-42. doi: 10.1007/BF00126437. J Muscle Res Cell Motil. 1995. PMID: 8567940 - Beta-adrenergic-regulated phosphorylation of the skeletal muscle Ca(V)1.1 channel in the fight-or-flight response.
Emrick MA, Sadilek M, Konoki K, Catterall WA. Emrick MA, et al. Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18712-7. doi: 10.1073/pnas.1012384107. Epub 2010 Oct 11. Proc Natl Acad Sci U S A. 2010. PMID: 20937870 Free PMC article. - Intramembrane charge movements and excitation- contraction coupling expressed by two-domain fragments of the Ca2+ channel.
Ahern CA, Arikkath J, Vallejo P, Gurnett CA, Powers PA, Campbell KP, Coronado R. Ahern CA, et al. Proc Natl Acad Sci U S A. 2001 Jun 5;98(12):6935-40. doi: 10.1073/pnas.111001898. Epub 2001 May 22. Proc Natl Acad Sci U S A. 2001. PMID: 11371610 Free PMC article. - Multiple calcium channel transcripts in rat osteosarcoma cells: selective activation of alpha 1D isoform by parathyroid hormone.
Barry EL, Gesek FA, Froehner SC, Friedman PA. Barry EL, et al. Proc Natl Acad Sci U S A. 1995 Nov 21;92(24):10914-8. doi: 10.1073/pnas.92.24.10914. Proc Natl Acad Sci U S A. 1995. PMID: 7479909 Free PMC article. - Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1.1 channels in skeletal muscle.
Hulme JT, Konoki K, Lin TW, Gritsenko MA, Camp DG 2nd, Bigelow DJ, Catterall WA. Hulme JT, et al. Proc Natl Acad Sci U S A. 2005 Apr 5;102(14):5274-9. doi: 10.1073/pnas.0409885102. Epub 2005 Mar 25. Proc Natl Acad Sci U S A. 2005. PMID: 15793008 Free PMC article.