A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-β4, from the particulate fraction of bovine cerebellum

Do Sik Min; Yong Kim; Young Han Lee; Pann Ghill Suh; Sung Ho Ryu

doi:10.1016/0014-5793(93)80293-4

A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-β4, from the particulate fraction of bovine cerebellum

Do Sik Min, Yong Kim, Young Han Lee, Pann Ghill Suh, Sung Ho Ryu

Department of Pharmacy

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

Abstract

A 130 kDa PLC isozyme was purified from the particulate fraction of bovine cerebellum. This PLC was recognized by a polyclonal antiserum generated against the purified 97 kDa PLC-β4. Reconstitution of the purified 130 kDa PLC with the membranes of C₆ Bu-1 cells in the presence of GTPγS or Alp₄^- resulted in PLC activation as well as the association of PLC with the membranes. Both the association and activation were revoked when the membrane was washed with 2 M KC1. The 97 kDa PLC-β4 did not associate with membranes. These data suggest that the 130 kDa PLC is the intact form of PLC-β4 the activity of which is likely to be regulated by a G-protein on the membrane.

Original language	English
Pages (from-to)	38-42
Number of pages	5
Journal	FEBS Letters
Volume	331
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(93)80293-4
Publication status	Published - 1993 Sep 27

Bibliographical note

Funding Information:
Acknowledgements. This work was supported m part by grants from the Korea Science and Engineermg Foundation (KOSEF 89-07-02-04) and from Pohang University of Science and Technology. We would like to thank Dr. Sung Ki Jang for critical reading of the manuscript.

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-β4, from the particulate fraction of bovine cerebellum",

abstract = "A 130 kDa PLC isozyme was purified from the particulate fraction of bovine cerebellum. This PLC was recognized by a polyclonal antiserum generated against the purified 97 kDa PLC-β4. Reconstitution of the purified 130 kDa PLC with the membranes of C6 Bu-1 cells in the presence of GTPγS or Alp4- resulted in PLC activation as well as the association of PLC with the membranes. Both the association and activation were revoked when the membrane was washed with 2 M KC1. The 97 kDa PLC-β4 did not associate with membranes. These data suggest that the 130 kDa PLC is the intact form of PLC-β4 the activity of which is likely to be regulated by a G-protein on the membrane.",

author = "Min, {Do Sik} and Yong Kim and Lee, {Young Han} and Suh, {Pann Ghill} and Ryu, {Sung Ho}",

note = "Funding Information: Acknowledgements. This work was supported m part by grants from the Korea Science and Engineermg Foundation (KOSEF 89-07-02-04) and from Pohang University of Science and Technology. We would like to thank Dr. Sung Ki Jang for critical reading of the manuscript.",

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T1 - A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-β4, from the particulate fraction of bovine cerebellum

AU - Min, Do Sik

AU - Kim, Yong

AU - Lee, Young Han

AU - Suh, Pann Ghill

AU - Ryu, Sung Ho

N1 - Funding Information: Acknowledgements. This work was supported m part by grants from the Korea Science and Engineermg Foundation (KOSEF 89-07-02-04) and from Pohang University of Science and Technology. We would like to thank Dr. Sung Ki Jang for critical reading of the manuscript.

PY - 1993/9/27

Y1 - 1993/9/27

N2 - A 130 kDa PLC isozyme was purified from the particulate fraction of bovine cerebellum. This PLC was recognized by a polyclonal antiserum generated against the purified 97 kDa PLC-β4. Reconstitution of the purified 130 kDa PLC with the membranes of C6 Bu-1 cells in the presence of GTPγS or Alp4- resulted in PLC activation as well as the association of PLC with the membranes. Both the association and activation were revoked when the membrane was washed with 2 M KC1. The 97 kDa PLC-β4 did not associate with membranes. These data suggest that the 130 kDa PLC is the intact form of PLC-β4 the activity of which is likely to be regulated by a G-protein on the membrane.

AB - A 130 kDa PLC isozyme was purified from the particulate fraction of bovine cerebellum. This PLC was recognized by a polyclonal antiserum generated against the purified 97 kDa PLC-β4. Reconstitution of the purified 130 kDa PLC with the membranes of C6 Bu-1 cells in the presence of GTPγS or Alp4- resulted in PLC activation as well as the association of PLC with the membranes. Both the association and activation were revoked when the membrane was washed with 2 M KC1. The 97 kDa PLC-β4 did not associate with membranes. These data suggest that the 130 kDa PLC is the intact form of PLC-β4 the activity of which is likely to be regulated by a G-protein on the membrane.

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SP - 38

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JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1-2

ER -

A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-β4, from the particulate fraction of bovine cerebellum

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

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