Molecules interacting with PRIP-2, a novel Ins(1,4,5)P3 binding protein type 2: Comparison with PRIP-1

Ayako Uji, Miho Matsuda, Toshio Kukita, Katsumasa Maeda, Takashi Kanematsu, Masato Hirata

Research output: Contribution to journalArticle

56 Citations (Scopus)

Abstract

A family of phospholipase C-related, catalytically inactive proteins (designated PRIP) have been identified as a group of novel inositol 1,4,5-trisphosphate binding proteins with a domain organization similar to phospholipase C-δ but lacking the enzymatic activity. The PRIP family consists of at least two types of proteins (PRIP-1 and PRIP-2 subfamilies). In the present study, we examined the tissue distribution of PRIP-2, its expression in rat brain at the mRNA level, and the characteristics of its binding to inositol compounds, protein phosphatase 1, and γ-amino butyric acid receptor associated protein. We also compared these characteristics with those of PRIP-1. Northern blot analysis and reverse-transcription polymerase chain reaction showed that PRIP-1 was present mainly in the brain, whereas PRIP-2 was expressed ubiquitously. In situ hybridization studies using rat brain revealed that the mRNA for both PRIP-1 and PRIP-2 was similarly expressed; it was detected in the granular cell and Purkinje cell layers in the cerebellum, and in the hippocampal pyramidal cells, dentate granule cells, and pyramidal and/or granule cells of the cerebral cortex in the cerebrum. PRIP-2 bound inositol 1,4,5-trisphosphate and its parent lipid, phosphatidylinositol 4,5-bisphosphate, with a similar affinity, while PRIP-1 preferentially bound the former ligand by about 10-fold. PRIP-1 and PRIP-2 interacted with protein phosphatase 1 and γ-amino butyric acid receptor associated protein in a similar manner. These results indicate that, similar to PRIP-1, PRIP-2 may be involved in both inositol 1,4,5-trisphosphate-mediated and γ-amino butyric acid-related signaling.

Original languageEnglish
Pages (from-to)443-453
Number of pages11
JournalLife Sciences
Volume72
Issue number4-5
DOIs
Publication statusPublished - Dec 20 2002

Fingerprint

Inositol 1,4,5-Trisphosphate
Butyric Acid
Carrier Proteins
Amino Acid Receptors
Protein Phosphatase 1
Brain
Molecules
Pyramidal Cells
Type C Phospholipases
Rats
Proteins
Messenger RNA
Purkinje Cells
Polymerase chain reaction
Cerebrum
Inositol
Tissue Distribution
Transcription
Phosphatidylinositols
Northern Blotting

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

Cite this

Molecules interacting with PRIP-2, a novel Ins(1,4,5)P3 binding protein type 2 : Comparison with PRIP-1. / Uji, Ayako; Matsuda, Miho; Kukita, Toshio; Maeda, Katsumasa; Kanematsu, Takashi; Hirata, Masato.

In: Life Sciences, Vol. 72, No. 4-5, 20.12.2002, p. 443-453.

Research output: Contribution to journalArticle

@article{66e9fea9571f443c87ffccdebf4f23c0,
title = "Molecules interacting with PRIP-2, a novel Ins(1,4,5)P3 binding protein type 2: Comparison with PRIP-1",
abstract = "A family of phospholipase C-related, catalytically inactive proteins (designated PRIP) have been identified as a group of novel inositol 1,4,5-trisphosphate binding proteins with a domain organization similar to phospholipase C-δ but lacking the enzymatic activity. The PRIP family consists of at least two types of proteins (PRIP-1 and PRIP-2 subfamilies). In the present study, we examined the tissue distribution of PRIP-2, its expression in rat brain at the mRNA level, and the characteristics of its binding to inositol compounds, protein phosphatase 1, and γ-amino butyric acid receptor associated protein. We also compared these characteristics with those of PRIP-1. Northern blot analysis and reverse-transcription polymerase chain reaction showed that PRIP-1 was present mainly in the brain, whereas PRIP-2 was expressed ubiquitously. In situ hybridization studies using rat brain revealed that the mRNA for both PRIP-1 and PRIP-2 was similarly expressed; it was detected in the granular cell and Purkinje cell layers in the cerebellum, and in the hippocampal pyramidal cells, dentate granule cells, and pyramidal and/or granule cells of the cerebral cortex in the cerebrum. PRIP-2 bound inositol 1,4,5-trisphosphate and its parent lipid, phosphatidylinositol 4,5-bisphosphate, with a similar affinity, while PRIP-1 preferentially bound the former ligand by about 10-fold. PRIP-1 and PRIP-2 interacted with protein phosphatase 1 and γ-amino butyric acid receptor associated protein in a similar manner. These results indicate that, similar to PRIP-1, PRIP-2 may be involved in both inositol 1,4,5-trisphosphate-mediated and γ-amino butyric acid-related signaling.",
author = "Ayako Uji and Miho Matsuda and Toshio Kukita and Katsumasa Maeda and Takashi Kanematsu and Masato Hirata",
year = "2002",
month = "12",
day = "20",
doi = "10.1016/S0024-3205(02)02275-0",
language = "English",
volume = "72",
pages = "443--453",
journal = "Life Sciences",
issn = "0024-3205",
publisher = "Elsevier Inc.",
number = "4-5",

}

TY - JOUR

T1 - Molecules interacting with PRIP-2, a novel Ins(1,4,5)P3 binding protein type 2

T2 - Comparison with PRIP-1

AU - Uji, Ayako

AU - Matsuda, Miho

AU - Kukita, Toshio

AU - Maeda, Katsumasa

AU - Kanematsu, Takashi

AU - Hirata, Masato

PY - 2002/12/20

Y1 - 2002/12/20

N2 - A family of phospholipase C-related, catalytically inactive proteins (designated PRIP) have been identified as a group of novel inositol 1,4,5-trisphosphate binding proteins with a domain organization similar to phospholipase C-δ but lacking the enzymatic activity. The PRIP family consists of at least two types of proteins (PRIP-1 and PRIP-2 subfamilies). In the present study, we examined the tissue distribution of PRIP-2, its expression in rat brain at the mRNA level, and the characteristics of its binding to inositol compounds, protein phosphatase 1, and γ-amino butyric acid receptor associated protein. We also compared these characteristics with those of PRIP-1. Northern blot analysis and reverse-transcription polymerase chain reaction showed that PRIP-1 was present mainly in the brain, whereas PRIP-2 was expressed ubiquitously. In situ hybridization studies using rat brain revealed that the mRNA for both PRIP-1 and PRIP-2 was similarly expressed; it was detected in the granular cell and Purkinje cell layers in the cerebellum, and in the hippocampal pyramidal cells, dentate granule cells, and pyramidal and/or granule cells of the cerebral cortex in the cerebrum. PRIP-2 bound inositol 1,4,5-trisphosphate and its parent lipid, phosphatidylinositol 4,5-bisphosphate, with a similar affinity, while PRIP-1 preferentially bound the former ligand by about 10-fold. PRIP-1 and PRIP-2 interacted with protein phosphatase 1 and γ-amino butyric acid receptor associated protein in a similar manner. These results indicate that, similar to PRIP-1, PRIP-2 may be involved in both inositol 1,4,5-trisphosphate-mediated and γ-amino butyric acid-related signaling.

AB - A family of phospholipase C-related, catalytically inactive proteins (designated PRIP) have been identified as a group of novel inositol 1,4,5-trisphosphate binding proteins with a domain organization similar to phospholipase C-δ but lacking the enzymatic activity. The PRIP family consists of at least two types of proteins (PRIP-1 and PRIP-2 subfamilies). In the present study, we examined the tissue distribution of PRIP-2, its expression in rat brain at the mRNA level, and the characteristics of its binding to inositol compounds, protein phosphatase 1, and γ-amino butyric acid receptor associated protein. We also compared these characteristics with those of PRIP-1. Northern blot analysis and reverse-transcription polymerase chain reaction showed that PRIP-1 was present mainly in the brain, whereas PRIP-2 was expressed ubiquitously. In situ hybridization studies using rat brain revealed that the mRNA for both PRIP-1 and PRIP-2 was similarly expressed; it was detected in the granular cell and Purkinje cell layers in the cerebellum, and in the hippocampal pyramidal cells, dentate granule cells, and pyramidal and/or granule cells of the cerebral cortex in the cerebrum. PRIP-2 bound inositol 1,4,5-trisphosphate and its parent lipid, phosphatidylinositol 4,5-bisphosphate, with a similar affinity, while PRIP-1 preferentially bound the former ligand by about 10-fold. PRIP-1 and PRIP-2 interacted with protein phosphatase 1 and γ-amino butyric acid receptor associated protein in a similar manner. These results indicate that, similar to PRIP-1, PRIP-2 may be involved in both inositol 1,4,5-trisphosphate-mediated and γ-amino butyric acid-related signaling.

UR - http://www.scopus.com/inward/record.url?scp=0037146874&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037146874&partnerID=8YFLogxK

U2 - 10.1016/S0024-3205(02)02275-0

DO - 10.1016/S0024-3205(02)02275-0

M3 - Article

C2 - 12467885

AN - SCOPUS:0037146874

VL - 72

SP - 443

EP - 453

JO - Life Sciences

JF - Life Sciences

SN - 0024-3205

IS - 4-5

ER -