3-hydroxy-3-methylglutaryl-coenzyme A reductase is present in peroxisomes in normal rat liver cells

G. A. Keller, M. C. Barton, D. J. Shapiro, S. J. Singer

Research output: Contribution to journalArticle

Abstract

The location inside rat liver parenchymal cells of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase; EC 1.1.1.34), the key regulatory enzyme in cholesterol biosynthesis, has been examined by immunoelectron microscopy and by subcellular fractionation. Although HMG-CoA reductase is generally thought to be exclusively a microsomal enzyme, we find that a substantial portion of cellular HMG-CoA reductase is localized in peroxisomes. Immunoelectron microscopic labeling of ultrathin frozen sections of normal rat liver, using two monoclonal antibodies to purified HMG-CoA reductase, showed that the enzyme is present in the peroxisomes at a higher concentration than at any other site inside the hepatocytes. Subcellular fractionation studies using Percoll and metrizamide gradients demonstrated a close correspondence of peaks of HMG-CoA reductase activity and of catalase activity, again revealing the presence of the reductase enzyme in peroxisomes. HMG-CoA reductase is therefore localized in peroxisomes in addition to being in the microsomal fraction.

Original languageEnglish (US)
Pages (from-to)770-774
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume82
Issue number3
DOIs
StatePublished - Jan 1 1985
Externally publishedYes

Fingerprint

Hydroxymethylglutaryl CoA Reductases
Peroxisomes
Oxidoreductases
Liver
Enzymes
Metrizamide
Immunoelectron Microscopy
Frozen Sections
Catalase
3-hydroxy-3-methylglutaryl-coenzyme A
Hepatocytes
Cholesterol
Monoclonal Antibodies

ASJC Scopus subject areas

  • General

Cite this

3-hydroxy-3-methylglutaryl-coenzyme A reductase is present in peroxisomes in normal rat liver cells. / Keller, G. A.; Barton, M. C.; Shapiro, D. J.; Singer, S. J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 82, No. 3, 01.01.1985, p. 770-774.

Research output: Contribution to journalArticle

@article{96ee3420211b492b8d28b5dac2765733,
title = "3-hydroxy-3-methylglutaryl-coenzyme A reductase is present in peroxisomes in normal rat liver cells",
abstract = "The location inside rat liver parenchymal cells of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase; EC 1.1.1.34), the key regulatory enzyme in cholesterol biosynthesis, has been examined by immunoelectron microscopy and by subcellular fractionation. Although HMG-CoA reductase is generally thought to be exclusively a microsomal enzyme, we find that a substantial portion of cellular HMG-CoA reductase is localized in peroxisomes. Immunoelectron microscopic labeling of ultrathin frozen sections of normal rat liver, using two monoclonal antibodies to purified HMG-CoA reductase, showed that the enzyme is present in the peroxisomes at a higher concentration than at any other site inside the hepatocytes. Subcellular fractionation studies using Percoll and metrizamide gradients demonstrated a close correspondence of peaks of HMG-CoA reductase activity and of catalase activity, again revealing the presence of the reductase enzyme in peroxisomes. HMG-CoA reductase is therefore localized in peroxisomes in addition to being in the microsomal fraction.",
author = "Keller, {G. A.} and Barton, {M. C.} and Shapiro, {D. J.} and Singer, {S. J.}",
year = "1985",
month = "1",
day = "1",
doi = "10.1073/pnas.82.3.770",
language = "English (US)",
volume = "82",
pages = "770--774",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "3",

}

TY - JOUR

T1 - 3-hydroxy-3-methylglutaryl-coenzyme A reductase is present in peroxisomes in normal rat liver cells

AU - Keller, G. A.

AU - Barton, M. C.

AU - Shapiro, D. J.

AU - Singer, S. J.

PY - 1985/1/1

Y1 - 1985/1/1

N2 - The location inside rat liver parenchymal cells of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase; EC 1.1.1.34), the key regulatory enzyme in cholesterol biosynthesis, has been examined by immunoelectron microscopy and by subcellular fractionation. Although HMG-CoA reductase is generally thought to be exclusively a microsomal enzyme, we find that a substantial portion of cellular HMG-CoA reductase is localized in peroxisomes. Immunoelectron microscopic labeling of ultrathin frozen sections of normal rat liver, using two monoclonal antibodies to purified HMG-CoA reductase, showed that the enzyme is present in the peroxisomes at a higher concentration than at any other site inside the hepatocytes. Subcellular fractionation studies using Percoll and metrizamide gradients demonstrated a close correspondence of peaks of HMG-CoA reductase activity and of catalase activity, again revealing the presence of the reductase enzyme in peroxisomes. HMG-CoA reductase is therefore localized in peroxisomes in addition to being in the microsomal fraction.

AB - The location inside rat liver parenchymal cells of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase; EC 1.1.1.34), the key regulatory enzyme in cholesterol biosynthesis, has been examined by immunoelectron microscopy and by subcellular fractionation. Although HMG-CoA reductase is generally thought to be exclusively a microsomal enzyme, we find that a substantial portion of cellular HMG-CoA reductase is localized in peroxisomes. Immunoelectron microscopic labeling of ultrathin frozen sections of normal rat liver, using two monoclonal antibodies to purified HMG-CoA reductase, showed that the enzyme is present in the peroxisomes at a higher concentration than at any other site inside the hepatocytes. Subcellular fractionation studies using Percoll and metrizamide gradients demonstrated a close correspondence of peaks of HMG-CoA reductase activity and of catalase activity, again revealing the presence of the reductase enzyme in peroxisomes. HMG-CoA reductase is therefore localized in peroxisomes in addition to being in the microsomal fraction.

UR - http://www.scopus.com/inward/record.url?scp=0021961770&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021961770&partnerID=8YFLogxK

U2 - 10.1073/pnas.82.3.770

DO - 10.1073/pnas.82.3.770

M3 - Article

C2 - 3883347

AN - SCOPUS:0021961770

VL - 82

SP - 770

EP - 774

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 3

ER -