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 Resjournal_title
Neurochemical researchauthors
Lau YSdoi
10.1007/BF00968670subject
Has Abstractpub_date
1990-03-01 00:00:00pages
265-72issue
3eissn
0364-3190issn
1573-6903journal_volume
15pub_type
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