Characteristics of Ca2+/calmodulin- and Ca2+/phosphatidylserine-stimulated phosphoproteins in rat striatum.

Abstract:

:The characteristics of endogenous Ca2+/calmodulin (CaM)- and Ca2+/phosphatidylserine (PS)-stimulated phosphorylated proteins in the striatum of rat were partially determined and compared in this study. The Ca2+/CaM-dependent phosphoproteins were associated with serine and threonine residues. The sensitivity of these proteins for phosphorylation by Ca2+/CaM was not affected by pretreatment of tissue with Ca2+ chelating agent, EGTA or with non-ionic detergent, Triton X-114. Triton X-114 phase separation experiments revealed that these Ca2+/CaM-dependent phosphoproteins were partitioned in the detergent rich phase suggesting that they are integral proteins of the striatal membrane. On the other hand, the Ca2+/PS-dependent phosphorylated proteins were primarily associated with the serine residue. Phosphorylation of these proteins by Ca2+/PS were abolished after the treatment with EGTA or Triton X-114. These results suggest that Ca2+/PS-dependent striatal phosphoproteins are biochemically unstable in maintaining their state of phosphorylation.

journal_name

Neurochem Res

journal_title

Neurochemical research

authors

Lau YS

doi

10.1007/BF00968670

subject

Has Abstract

pub_date

1990-03-01 00:00:00

pages

265-72

issue

3

eissn

0364-3190

issn

1573-6903

journal_volume

15

pub_type

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