Abstract：
:We previously found in single channel studies that ryanodine receptor (RyR) channel activity can be made insensitive to block by Mg2+ when terminal cisternae of sarcoplasmic reticulum, incorporated into planar bilayers, are treated with protein kinase A (PKA) or Ca2+/calmodulin dependent protein kinase type II (CamPK II), and then again made sensitive by treatment with protein phosphatases [Hain J. Nath S. Mayrleitner M. Fleischer S. Schindler H. (1994) Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from skeletal muscle. Biophys. J., 67, 1823-1833]. In this study, modulation by protein kinases and phosphatases on net Ca2+ uptake by TC is presented. Phosphorylation of TC vesicles with PKA, CamPK II, or protein kinase C (PKC) reduced the calcium loading rate of TC vesicles 3-fold, 2.1-fold and 1.7-fold, respectively, measured in the presence of 1 mM MgCl2. There is no effect when AMP-PNP is substituted for ATP. Phosphorylation of the RyR was also measured by incorporation of [gamma-32P]-phosphate from ATP. A phosphorylation stoichiometry of 1.94 +/- 0.1 (32P/RyR) for PKA, 0.89 +/- 0.08 for CamPK II and 0.95 +/- 0.16 for PKC was obtained under these conditions. A study of the time dependence of phosphorylation with PKA and CamPK shows a direct correlation of reduction in calcium loading rate with increased phosphorylation of the ryanodine receptor. Treatment with protein phosphatase 1 enhanced the calcium loading rate again, after it was reduced by PKA phosphorylation. Investigation of the magnesium dependency shows that even at higher [Mg2+] (6 mM), PKA phosphorylated TC vesicles have a 2.3-fold reduced calcium loading rate indicating insensitivity to block by Mg2+.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Cell Calciumjournal_title
Cell calciumauthors
Mayrleitner M,Chandler R,Schindler H,Fleischer Sdoi
10.1016/0143-4160(95)90064-0subject
Has Abstractpub_date
1995-09-01 00:00:00pages
197-206issue
3eissn
0143-4160issn
1532-1991pii
0143-4160(95)90064-0journal_volume
18pub_type
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