Faculty Research 1980 - 1989

Title

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.

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