Isolation and characterization of two 20S proteasomes from the endoplasmic reticulum of rat liver microsomes.

Isolation and characterization of two 20S proteasomes from the endoplasmic reticulum of rat liver microsomes. Research Abstract Details 

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Isolation and characterization of two 20S proteasomes from the endoplasmic reticulum of rat liver microsomes. Abstract Text:

H Hori,T Nembai,Y Miyata,T Hayashi,K Ueno,T Koide,

Two new forms of proteasomes, designated as the endoplasmic reticulum (ER) membrane-associated proteasome (ERa proteasome) and ER membrane-bound proteasome (ERb proteasome), were purified to homogeneity from 0.0125 and 2.5% sodium cholate extracts, respectively, of a rat liver microsomal fraction. SDS-PAGE analysis revealed that the purified ERa and ERb proteasomes were composed of multiple subunits similar to the cytosolic 20S proteasome. However, electrophoretic, structural and immunochemical differences between the ERa, ERb and cytosolic 20S proteasomes were observed on native PAGE, two-dimensional (2D) PAGE, and immunoblot analyses. Purification of ERb from a 2.5% sodium cholate extract of the trypsin-treated microsomal fraction yielded a trypsin-modified form of ERb (tERb), which lacked the C2 subunit at least. On the other hand, no ERa proteasome was obtained from the 0.0125% sodium cholate extract of the trypsin-treated microsomes, suggesting that ERa and ERb are ER membrane-associated and -bound proteasomes, respectively. The ERa, ERb, and cytosolic 20S proteasomes exhibited similar specificities as to peptide hydrolyzing activity, although differences in their activities were noted in the presence of SDS and phospholipid. With respect to the proteolysis of protein substrates, only the ERb proteasome cleaved beta-casein, and it also degraded reduced and carboxymethylated lysozyme considerably faster than the cytosolic 20S and ERa proteasomes. Collectively our results suggest that the ERa and ERb proteasomes may play roles in intracellular proteolysis distinct from that of the cytosolic 20S proteasome.

Isolation and characterization of two 20S proteasomes from the endoplasmic reticulum of rat liver microsomes. Publishing Authors By Initials

H Hori,T Nembai,Y Miyata,T Hayashi,K Ueno,T Koide,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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Isolation and characterization of two 20S proteasomes from the endoplasmic reticulum of rat liver microsomes. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 126

Page Numbers: 722-30

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 1999

Isolation and characterization of two 20S proteasomes from the endoplasmic reticulum of rat liver microsomes. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Isolation and characterization of two 20S proteasomes from the endoplasmic reticulum of rat liver microsomes. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Isolation and characterization of two 20S proteasomes from the endoplasmic reticulum of rat liver microsomes. Information

Substance Name: Proteasome Endopeptidase Complex

Registry Number: EC 3.4.25.1

Grant and Affiliation Information for Isolation and characterization of two 20S proteasomes from the endoplasmic reticulum of rat liver microsomes.

AFFILIATION: Department of Life Science, Faculty of Science, Himeji Institute of Technology, Harima Science Garden City, Hyogo, 678-1297, Japan.

Country: JAPAN

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MEDLINETA: J Biochem

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