Characterization of multiple forms of histone phosphatase in rat liver

Tamura, Shinji; Kikuchi, Kunimi; Hiraga, Akira; Kikuchi, H.; Hosokawa, Michiko; Tsuiki, Shigeru

doi:10.1016/0005-2744(78)90171-7

Cited by 43 publications

(22 citation statements)

References 11 publications

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“…Phosphorylation of co-casein by casein kinase II and whole histone by protein kinase A using [y-32P]ATP was performed essentially as described previously [23]. Casein kinase II was purified from bovine …”

Section: Assay Of Proteand Phosphatase Activitiesmentioning

confidence: 99%

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Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

et al. 1996

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Section: Assay Of Proteand Phosphatase Activitiesmentioning

confidence: 99%

“…Protien kinase A was purified as described previously [23]. levels of PP2CI3 isoforms alter during the course of this first wave of spermatogenesis.…”

Section: S Kato Et Al/febs Letters 396 (1996) 293-297mentioning

confidence: 99%

Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

et al. 1996

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“…The [32P]histone phosphatase assay [29] was carried out in a total volume of 200 pl containing a 50-pl aliquot of a DEAE-cellulose column fraction, [ 32P]histone f2b (30 pg), 50 mM Tris (pH 7.9, 1 mM dithiothreitol and 2.5 mM MgClz at 30°C. 32Pi radioactivity was counted following extraction with ammonium molybdate and isobutanol [30].…”

Section: Phosphoprotein Phosphatase Assaysmentioning

confidence: 99%

Insulin-induced increases in the activity of the spontaneously active and ATP . Mg-dependent forms of phosphatase-1 in alloxan-diabetic rat liver

Dragland-Meserve¹,

Webster²,

Botelho³

1985

Eur J Biochem

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Liver supernatant from normal and alloxan-diabetic rats was fractionated by DEAE-cellulose chromatography and the separated phosphoprotein phosphatase fractions were assayed with [32P]histone fzb, [32P]phosphorylase a and [32P]phosphorylase kinase as substrates. In diabetic rat liver, one of the phosphatase fractions found in the normal liver was significantly reduced. This fraction was identified as a mixture of the spontaneously active form and the ATP . Mg-dependent form of phosphoprotein phosphatase-I (F,) based on sensitivity to inhibitor-2, substrate specificity, and the fact that it could be activated 42 -70% by glycogen synthase kinase-3 in the presence of ATP . Mg. Further analysis of this fraction showed that liver cytosol from diabetic rats contained 62-79% lower spontaneously active phosphatase-I activity and 40 -51 % lower combined spontaneously active and ATP . Mg-dependent protein phosphatase-1 (F,) activity. Insulin administration increased the spontaneously active and the ATP . Mg-dependent protein phosphatase-I activities approximately 45% and 36%, respectively, in alloxan-diabetic rats. These data imply that the lower levels of spontaneously active phosphatase-1 activity in diabetic rat liver cannot be explained by presuming phosphatase-1 to have been present as Fc, the inactive form. Moreover, insulin restored the total activity of the spontaneously active and activatable forms of phosphatase-I to those present in normal liver implying that both forms of phosphatase-I activity are under hormonal control.

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“…The catalytic subunits of the major protein serine, threonine phosphatases in eukaryotic cells have been divided into four classes, (types 1, 2A, 2B and 2C) on the basis of their sensitivity to two thermostable proteins (inhibitor-1 and -2) and their divalent cation requirements (Cohen 1989). Type 20 protein phosphatase was originally identified and purified from rat liver by us as a Mg2~ dependent protein phosphatase with Mr. 48,000 (protein phosphatase IA, (Tamura et al 1978;Hiraga et al 1981) ). Subsequently, a cDNA clone (pST 11) encoding the full lenghth of the enzyme protein was isolated from a rat kidney cDNA library (Tamura et al 1989).…”

mentioning

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Alteration of the Level of Protein Phosphatase 2C(IA) mRNA during the Course of Differentiation of Skeleral Muscle Cells.

Ohishi

Kobayashi

Terasawa

et al. 1992

Tohoku J. Exp. Med.

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Characterization of multiple forms of histone phosphatase in rat liver

Cited by 43 publications

References 11 publications

Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

Differentiation‐dependent enhanced expression of protein phosphatase 2Cβ in germ cells of mouse seminiferous tubules

Insulin-induced increases in the activity of the spontaneously active and ATP . Mg-dependent forms of phosphatase-1 in alloxan-diabetic rat liver

Alteration of the Level of Protein Phosphatase 2C(IA) mRNA during the Course of Differentiation of Skeleral Muscle Cells.

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