Identification of PP1 Catalytic Subunit Isotypes PP1γ1, Pp1δ and Pp1α in Various Rat Tissues

Shima, Hiroshi; Hatano, Yoshiaki; Chun, Yang Suk; Sügimura, Takashi; Zhang, Zhongjian J.; Lee, Ernest Y.C.; Nagao, Minako

doi:10.1006/bbrc.1993.1556

Cited by 93 publications

(64 citation statements)

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“…The present study also showed that the PP1y1 antibody recognized a major protein with an estimated molecular mass of 36 kDa in the rat parotid gland, which is in good agreement with that calculated from the amino acid sequence of the rat PP1y1 protein [5,6]. Two minor proteins with estimated molecular masses of 70 and 58 kDa were also recognized.…”

Section: Discussionsupporting

confidence: 89%

“…The antisera used were those reported previously [6]. Briefly, antibody was raised against oligopeptide corresponding to the predicted amino acid sequence of the carboxy-terminal domain *Corresponding author.…”

Section: Antiseramentioning

confidence: 99%

“…The antisera were developed in rabbits against peptides from the carboxy-termini of the four types of PP1 catalytic subunits. Characterization of the specificity of these antisera has recently been described [6]. Although the expression of PPls has been investigated at the mRNA and protein levels [6], the distribution of PPls in histological localization at the protein level is still unclear.…”

Section: Introductionmentioning

confidence: 99%

“…Characterization of the specificity of these antisera has recently been described [6]. Although the expression of PPls has been investigated at the mRNA and protein levels [6], the distribution of PPls in histological localization at the protein level is still unclear. Immunohistochemical studies have been performed in rat cerebellum [7] and testis [8] with PP1y1 and PP1y2, respectively.…”

Section: Introductionmentioning

confidence: 99%

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Immunohistochemical and immunoblotting identification of protein phosphatase 1γ1 in rat salivary glands

Shirakawa¹,

Mochizuki²,

Kobayashi³

et al. 1996

FEBS Letters

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We have analyzed the distribution of the ~1 isotype of rat protein phosphatase type 1 catalytic subunit in rat salivary glands. Formaldehyde-fixed paraffin sections were reacted with the PP1T1 antibody using an immunohistochemical method. Positive staining occurred in striated ducts of parotid gland. However, the staining reaction was less intense in submandibular gland. Proteins were also prepared from rat salivary glands and subjected to SDS-PAGE, followed by Western blotting analysis with the PP171 antibody. The antibody interacted with protein corresponding to an estimated molecular mass of 36 kDa present in the parotid gland. The staining reaction was considerably weaker with the proteins from submandibular gland.

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Section: Discussionsupporting

confidence: 89%

Section: Antiseramentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Immunohistochemical and immunoblotting identification of protein phosphatase 1γ1 in rat salivary glands

Shirakawa¹,

Mochizuki²,

Kobayashi³

et al. 1996

FEBS Letters

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“…Anti-glu and anti-myc monoclonal antibodies were gifts from Dr Larry A Feig (Tufts University, Boston, MA, USA). Polyclonal antibodies speci®c to PP1c isoforms and PP2Ac have been described (Ishizaka et al, 1992;Shima et al, 1993). Anti-Aurora-B monoclonal antibody (H7-4) will be described elsewhere (manuscripts in preparation).…”

Section: Methodsmentioning

confidence: 99%

Aurora-B associated protein phosphatases as negative regulators of kinase activation

et al. 2002

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The human serine/threonine kinase Aurora-B is structurally related to the protein kinase Ipl1p from S cerevisiae and aurora from Drosophila melanogaster, which are key regulators of mitosis. The present study shows that human Aurora-B is activated by okadaic acid and forms complexes with the protein serine/threonine phosphatase type 1 (PP1) or PP2A, but not with PP5. These data identi®ed Aurora-B associated protein phosphatases as negative regulators of kinase activation. We then used a series of substrates based on a histone H3 phosphorylation site (residues 5 ± 15) to determine the substrate speci®city of human Aurora-B. We found that this enzyme is an arginine-directed kinase that can phosphorylate histone H3 at serines 10 and 28 in vitro, suggesting that human Aurora-B is a mitotic histone H3 kinase.

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Differential cellular and subcellular localization of protein phosphatase 1 isoforms in brain

et al. 1999

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Identification of PP1 Catalytic Subunit Isotypes PP1γ1, Pp1δ and Pp1α in Various Rat Tissues

Cited by 93 publications

References 0 publications

Immunohistochemical and immunoblotting identification of protein phosphatase 1γ1 in rat salivary glands

Immunohistochemical and immunoblotting identification of protein phosphatase 1γ1 in rat salivary glands

Aurora-B associated protein phosphatases as negative regulators of kinase activation

Differential cellular and subcellular localization of protein phosphatase 1 isoforms in brain

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