Faculty Research 1980 - 1989
A spectrin-like protein from mouse brain membranes: phosphorylation of the 235,000-dalton subunit.
Document Type
Article
Publication Date
1984
Keywords
Autoradiography, Brain: me, Electrophoresis-Polyacrylamide-Gel, Erythrocyte-Membrane: me, Erythrocytes: me, Fluorescent-Antibody-Technic, Membrane-Proteins: ip, me, Mice, Mice-Inbred-C57BL, Phosphorus-Radioisotopes: du, Phosphorylation, Protein-Kinases: me, Spectrin: ip, SUPPORT-NON-U-S-GOVT, SUPPORT-U-S-GOVT-P-H-S
JAX Source
Am-J-Physiol. 1984 Jul; 247(1 pt 1):C61-73.
Grant
RO1NS19357, RO1-HL-26059, AM16095, +
Abstract
A mouse brain spectrin-like protein, which was an immunoreactive analogue of erythrocyte spectrin, has been isolated from demyelinated membranes. This spectrin analogue was a 10.5 S, 972,000 molecular weight (Mr) (alpha beta)2 tetramer containing subunits of 240,000 (alpha) and 235,000 (beta) Mr. We demonstrated that in vivo only the 235,000 Mr beta subunit of the mouse brain spectrin-like protein was phosphorylated, which was an analogous situation to mouse erythrocyte spectrin in which only the 220,000 Mr beta subunit was phosphorylated. Incubation of isolated membrane fractions with [gamma-32P]ATP +/- adenosine 3',5'-cyclic monophosphate (cAMP) indicated that mouse brain spectrin-like protein, mouse erythrocyte spectrin, and human erythrocyte spectrin's beta subunits were all phosphorylated in vitro by membrane-associated cAMP-independent protein kinases.
Recommended Citation
Goodman SR,
Zagon IS,
Whitfield CF,
Casoria LA,
Shohet SB,
Bernstein SE,
McLaughlin PJ,
Laskiewicz TL.
A spectrin-like protein from mouse brain membranes: phosphorylation of the 235,000-dalton subunit. Am-J-Physiol. 1984 Jul; 247(1 pt 1):C61-73.