Insulin-degrading enzyme exists inside of rat liver peroxisomes and degrades oxidized proteins

Masashi Morita; Igor V. Kurochkin; Kiyoto Motojima; Sataro Goto; Tatsuya Takano; Shoji Okamura; Ryuichiro Sato; Sadaki Yokota; Tsuneo Imanaka

doi:10.1247/csf.25.309

Insulin-degrading enzyme exists inside of rat liver peroxisomes and degrades oxidized proteins

Masashi Morita, Igor V. Kurochkin, Kiyoto Motojima, Sataro Goto, Tatsuya Takano, Shoji Okamura, Ryuichiro Sato, Sadaki Yokota, Tsuneo Imanaka^*

^*Corresponding author for this work

Molecular Cell Biology

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

64 Scopus citations

Abstract

Insulin-degrading enzyme (IDE) was detected by immunoblot analysis in highly purified rat liver peroxisomes. IDE in the peroxisomal fraction was resistant to proteolysis by trypsin and chymotrypsin under conditions where the peroxisomal membranes remained intact. After sonication of the peroxisomal fraction, IDE was recovered in the supernatant fraction. Further, the localization of IDE in the peroxisomes was shown by immunoelectron microscopy. In addition, IDE isolated from peroxisomes degraded insulin as well as oxidized lysozyme as a model substrate for oxidized proteins. These results suggest that IDE exists in an active form in the matrix of rat liver peroxisomes and is involved in elimination of oxidized proteins in peroxisomes.

Original language	English
Pages (from-to)	309-315
Number of pages	7
Journal	Cell Structure and Function
Volume	25
Issue number	5
DOIs	https://doi.org/10.1247/csf.25.309
State	Published - 2000

Keywords

Insulin-degrading enzyme
Oxidized proteins
Peroxisomes
Proteolysis
Subcellular localization

ASJC Scopus subject areas

Physiology
Molecular Biology
Cell Biology

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10.1247/csf.25.309

Cite this

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title = "Insulin-degrading enzyme exists inside of rat liver peroxisomes and degrades oxidized proteins",

abstract = "Insulin-degrading enzyme (IDE) was detected by immunoblot analysis in highly purified rat liver peroxisomes. IDE in the peroxisomal fraction was resistant to proteolysis by trypsin and chymotrypsin under conditions where the peroxisomal membranes remained intact. After sonication of the peroxisomal fraction, IDE was recovered in the supernatant fraction. Further, the localization of IDE in the peroxisomes was shown by immunoelectron microscopy. In addition, IDE isolated from peroxisomes degraded insulin as well as oxidized lysozyme as a model substrate for oxidized proteins. These results suggest that IDE exists in an active form in the matrix of rat liver peroxisomes and is involved in elimination of oxidized proteins in peroxisomes.",

keywords = "Insulin-degrading enzyme, Oxidized proteins, Peroxisomes, Proteolysis, Subcellular localization",

author = "Masashi Morita and Kurochkin, {Igor V.} and Kiyoto Motojima and Sataro Goto and Tatsuya Takano and Shoji Okamura and Ryuichiro Sato and Sadaki Yokota and Tsuneo Imanaka",

year = "2000",

doi = "10.1247/csf.25.309",

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journal = "Cell Structure and Function",

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publisher = "Japan Society for Cell Biology",

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TY - JOUR

T1 - Insulin-degrading enzyme exists inside of rat liver peroxisomes and degrades oxidized proteins

AU - Morita, Masashi

AU - Kurochkin, Igor V.

AU - Motojima, Kiyoto

AU - Goto, Sataro

AU - Takano, Tatsuya

AU - Okamura, Shoji

AU - Sato, Ryuichiro

AU - Yokota, Sadaki

AU - Imanaka, Tsuneo

PY - 2000

Y1 - 2000

N2 - Insulin-degrading enzyme (IDE) was detected by immunoblot analysis in highly purified rat liver peroxisomes. IDE in the peroxisomal fraction was resistant to proteolysis by trypsin and chymotrypsin under conditions where the peroxisomal membranes remained intact. After sonication of the peroxisomal fraction, IDE was recovered in the supernatant fraction. Further, the localization of IDE in the peroxisomes was shown by immunoelectron microscopy. In addition, IDE isolated from peroxisomes degraded insulin as well as oxidized lysozyme as a model substrate for oxidized proteins. These results suggest that IDE exists in an active form in the matrix of rat liver peroxisomes and is involved in elimination of oxidized proteins in peroxisomes.

AB - Insulin-degrading enzyme (IDE) was detected by immunoblot analysis in highly purified rat liver peroxisomes. IDE in the peroxisomal fraction was resistant to proteolysis by trypsin and chymotrypsin under conditions where the peroxisomal membranes remained intact. After sonication of the peroxisomal fraction, IDE was recovered in the supernatant fraction. Further, the localization of IDE in the peroxisomes was shown by immunoelectron microscopy. In addition, IDE isolated from peroxisomes degraded insulin as well as oxidized lysozyme as a model substrate for oxidized proteins. These results suggest that IDE exists in an active form in the matrix of rat liver peroxisomes and is involved in elimination of oxidized proteins in peroxisomes.

KW - Insulin-degrading enzyme

KW - Oxidized proteins

KW - Peroxisomes

KW - Proteolysis

KW - Subcellular localization

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M3 - 学術論文

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SN - 0386-7196

VL - 25

SP - 309

EP - 315

JO - Cell Structure and Function

JF - Cell Structure and Function

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Insulin-degrading enzyme exists inside of rat liver peroxisomes and degrades oxidized proteins

Abstract

Keywords

ASJC Scopus subject areas

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