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Calcium-activated, calmodulin-dependent protein kinase activity in bovine thyroid cytosol.

Abstract：

:Bovine thyroid 100,000 X g supernatant contained calcium-activated, calmodulin-dependent protein kinase (PK-CaM) activity. The PK-CaM was partially purified using ion-exchange chromatography and characterized. PK-CaM, using casein as exogenous substrate, was not stimulated by Ca2+(0-500 microM) or calmodulin (1-10 micrograms) by themselves, but was stimulated by the combination of the two by 100%. The activation of the enzyme by Ca2+ and calmodulin was dose-dependent with maximal stimulation evident at 1 microM free-Ca2+ and 3 micrograms calmodulin. Both chlorpromazine and trifluoperazine inhibited the thyroid enzyme in a dose-related manner. The molecular weight (MW) of the PK-CaM, based on gel filtration, was approximately 500,000. PK-CaM could also be demonstrated using endogenous thyroid cytosol proteins as substrate. Separation of these 32P-labelled proteins by SDS-PAGE and subsequent autoradiography revealed that one major protein of approximately 56,000 MW was phosphorylated by PK-CaM. In some experiments, a second, less-intense protein band of approximately 64,000 MW was also phosphorylated. Evidence is presented, suggesting that these two protein bands may result from the autophosphorylation of the PK-CaM holoenzyme. These results offer a molecular mechanism, in addition to protein kinase C, by which Ca2+ effects may be mediated in thyroid.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Friedman Y,Henricks L,Poleck T,Levasseur S,Burke G

doi

10.1016/0006-291x(86)91066-1

subject

Has Abstract

pub_date

1986-10-15 00:00:00

pages

120-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(86)91066-1

journal_volume

140

pub_type

杂志文章

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