Hyperinsulinemia in PRIP-1 gene deleted mice

Naoko Doira, Takashi Kanematsu, Miho Matsuda, Hiroshi Takeuchi, Hito O. Nakano, Yushi Ito, Keiko Nakayama, Kei Ichi Nakayama, Masato Hirata

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The protein p130, named from its molecular size, was originally identified as an inositol 1, 4,5-trisphosphate binding protein similar to phospholipase C (PLC)-δ1, but lacking any PLC activity. It was recently renamed PLC-related catalytically inactive protein-1 (PRIP-1). In the present study, PRIP-1 gene-targeted mice were analyzed for glycogen metabolism based on the previous finding that PRIP-1 interacts with protein phosphatase-1 (26). Compared to the control mice, mutant mice exhibited lower phosphorylase activity and higher levels of glycogen in the liver, which appeared to be consistent with the inhibition of protein phosphatase-1 by PRIP-1. These observation could also be attributed to the increased levels of plasma insulin. Hyperinsulinemia, observed even in the young mice, was progressive with aging, and was accompanied by the accumulation of fat tissues, increased body weight and decreased sensitivity to insulin in the mutant mice at the age of 12 months. These results suggest that PRIP-1 is a molecule involved in the control of plasma insulin.

Original languageEnglish
Pages (from-to)157-165
Number of pages9
JournalBiomedical Research
Volume22
Issue number3
DOIs
Publication statusPublished - Jan 1 2001

Fingerprint

Hyperinsulinism
Programmable logic controllers
Genes
Type C Phospholipases
Protein Phosphatase 1
Proteins
Insulin
Glycogen
Plasmas
Phosphorylases
Liver Glycogen
Inositol 1,4,5-Trisphosphate
Metabolism
Liver
Insulin Resistance
Carrier Proteins
Aging of materials
Fats
Body Weight
Observation

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Doira, N., Kanematsu, T., Matsuda, M., Takeuchi, H., Nakano, H. O., Ito, Y., ... Hirata, M. (2001). Hyperinsulinemia in PRIP-1 gene deleted mice. Biomedical Research, 22(3), 157-165. https://doi.org/10.2220/biomedres.22.157

Hyperinsulinemia in PRIP-1 gene deleted mice. / Doira, Naoko; Kanematsu, Takashi; Matsuda, Miho; Takeuchi, Hiroshi; Nakano, Hito O.; Ito, Yushi; Nakayama, Keiko; Nakayama, Kei Ichi; Hirata, Masato.

In: Biomedical Research, Vol. 22, No. 3, 01.01.2001, p. 157-165.

Research output: Contribution to journalArticle

Doira, N, Kanematsu, T, Matsuda, M, Takeuchi, H, Nakano, HO, Ito, Y, Nakayama, K, Nakayama, KI & Hirata, M 2001, 'Hyperinsulinemia in PRIP-1 gene deleted mice', Biomedical Research, vol. 22, no. 3, pp. 157-165. https://doi.org/10.2220/biomedres.22.157
Doira, Naoko ; Kanematsu, Takashi ; Matsuda, Miho ; Takeuchi, Hiroshi ; Nakano, Hito O. ; Ito, Yushi ; Nakayama, Keiko ; Nakayama, Kei Ichi ; Hirata, Masato. / Hyperinsulinemia in PRIP-1 gene deleted mice. In: Biomedical Research. 2001 ; Vol. 22, No. 3. pp. 157-165.
@article{521f4f9de6144c9cb8cc0ae05348674d,
title = "Hyperinsulinemia in PRIP-1 gene deleted mice",
abstract = "The protein p130, named from its molecular size, was originally identified as an inositol 1, 4,5-trisphosphate binding protein similar to phospholipase C (PLC)-δ1, but lacking any PLC activity. It was recently renamed PLC-related catalytically inactive protein-1 (PRIP-1). In the present study, PRIP-1 gene-targeted mice were analyzed for glycogen metabolism based on the previous finding that PRIP-1 interacts with protein phosphatase-1 (26). Compared to the control mice, mutant mice exhibited lower phosphorylase activity and higher levels of glycogen in the liver, which appeared to be consistent with the inhibition of protein phosphatase-1 by PRIP-1. These observation could also be attributed to the increased levels of plasma insulin. Hyperinsulinemia, observed even in the young mice, was progressive with aging, and was accompanied by the accumulation of fat tissues, increased body weight and decreased sensitivity to insulin in the mutant mice at the age of 12 months. These results suggest that PRIP-1 is a molecule involved in the control of plasma insulin.",
author = "Naoko Doira and Takashi Kanematsu and Miho Matsuda and Hiroshi Takeuchi and Nakano, {Hito O.} and Yushi Ito and Keiko Nakayama and Nakayama, {Kei Ichi} and Masato Hirata",
year = "2001",
month = "1",
day = "1",
doi = "10.2220/biomedres.22.157",
language = "English",
volume = "22",
pages = "157--165",
journal = "Biomedical Research",
issn = "0388-6107",
publisher = "Biomedical Research Foundation",
number = "3",

}

TY - JOUR

T1 - Hyperinsulinemia in PRIP-1 gene deleted mice

AU - Doira, Naoko

AU - Kanematsu, Takashi

AU - Matsuda, Miho

AU - Takeuchi, Hiroshi

AU - Nakano, Hito O.

AU - Ito, Yushi

AU - Nakayama, Keiko

AU - Nakayama, Kei Ichi

AU - Hirata, Masato

PY - 2001/1/1

Y1 - 2001/1/1

N2 - The protein p130, named from its molecular size, was originally identified as an inositol 1, 4,5-trisphosphate binding protein similar to phospholipase C (PLC)-δ1, but lacking any PLC activity. It was recently renamed PLC-related catalytically inactive protein-1 (PRIP-1). In the present study, PRIP-1 gene-targeted mice were analyzed for glycogen metabolism based on the previous finding that PRIP-1 interacts with protein phosphatase-1 (26). Compared to the control mice, mutant mice exhibited lower phosphorylase activity and higher levels of glycogen in the liver, which appeared to be consistent with the inhibition of protein phosphatase-1 by PRIP-1. These observation could also be attributed to the increased levels of plasma insulin. Hyperinsulinemia, observed even in the young mice, was progressive with aging, and was accompanied by the accumulation of fat tissues, increased body weight and decreased sensitivity to insulin in the mutant mice at the age of 12 months. These results suggest that PRIP-1 is a molecule involved in the control of plasma insulin.

AB - The protein p130, named from its molecular size, was originally identified as an inositol 1, 4,5-trisphosphate binding protein similar to phospholipase C (PLC)-δ1, but lacking any PLC activity. It was recently renamed PLC-related catalytically inactive protein-1 (PRIP-1). In the present study, PRIP-1 gene-targeted mice were analyzed for glycogen metabolism based on the previous finding that PRIP-1 interacts with protein phosphatase-1 (26). Compared to the control mice, mutant mice exhibited lower phosphorylase activity and higher levels of glycogen in the liver, which appeared to be consistent with the inhibition of protein phosphatase-1 by PRIP-1. These observation could also be attributed to the increased levels of plasma insulin. Hyperinsulinemia, observed even in the young mice, was progressive with aging, and was accompanied by the accumulation of fat tissues, increased body weight and decreased sensitivity to insulin in the mutant mice at the age of 12 months. These results suggest that PRIP-1 is a molecule involved in the control of plasma insulin.

UR - http://www.scopus.com/inward/record.url?scp=21544459622&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=21544459622&partnerID=8YFLogxK

U2 - 10.2220/biomedres.22.157

DO - 10.2220/biomedres.22.157

M3 - Article

AN - SCOPUS:21544459622

VL - 22

SP - 157

EP - 165

JO - Biomedical Research

JF - Biomedical Research

SN - 0388-6107

IS - 3

ER -