Aldose reductase and ϱ-crystallin belong to the same protein superfamily as aldehyde reductase

Deborah Carper; Chihiro Nishimura; Toshimichi Shinohara; Bernard Dietzchold; Graeme Wistow; Cheryl Craft; Peter Kador; Jin H. Kinoshita

doi:10.1016/0014-5793(87)80905-5

Aldose reductase and ϱ-crystallin belong to the same protein superfamily as aldehyde reductase

Deborah Carper, Chihiro Nishimura, Toshimichi Shinohara, Bernard Dietzchold, Graeme Wistow, Cheryl Craft, Peter Kador, Jin H. Kinoshita

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

155 Scopus citations

Abstract

Aldose reductase (EC 1.1.1.21) has been implicated in a variety of diabetic complications. Here we present the first primary sequence data for the rat lens enzyme, obtained by amino acid and cDNA analysis. We have found structural similarities with another NADPH-dependent oxidoreductase: human liver aldehyde reductase (EC 1.1.1.2). The identity between these two enzymes is 50%. Both enzymes share approx. 40-50% homology with ρ{variant}-crystallin, a major lens protein present only in the frog, Rana pipiens. We propose that aldose reductase, aldehyde reductase and ρ{variant}-crystallin are members of a superfamily of related proteins.

Original language	English (US)
Pages (from-to)	209-213
Number of pages	5
Journal	FEBS Letters
Volume	220
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(87)80905-5
State	Published - Aug 10 1987
Externally published	Yes

Keywords

Aldehyde reductase
Aldose reductase
Structural homology
cDNA sequence
ρ{variant}-Crystallin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(87)80905-5

Cite this

@article{165b67f8f9f540018c666b7bd095e0ed,

title = "Aldose reductase and ϱ-crystallin belong to the same protein superfamily as aldehyde reductase",

abstract = "Aldose reductase (EC 1.1.1.21) has been implicated in a variety of diabetic complications. Here we present the first primary sequence data for the rat lens enzyme, obtained by amino acid and cDNA analysis. We have found structural similarities with another NADPH-dependent oxidoreductase: human liver aldehyde reductase (EC 1.1.1.2). The identity between these two enzymes is 50%. Both enzymes share approx. 40-50% homology with ρ{variant}-crystallin, a major lens protein present only in the frog, Rana pipiens. We propose that aldose reductase, aldehyde reductase and ρ{variant}-crystallin are members of a superfamily of related proteins.",

keywords = "Aldehyde reductase, Aldose reductase, Structural homology, cDNA sequence, ρ{variant}-Crystallin",

author = "Deborah Carper and Chihiro Nishimura and Toshimichi Shinohara and Bernard Dietzchold and Graeme Wistow and Cheryl Craft and Peter Kador and Kinoshita, {Jin H.}",

year = "1987",

month = aug,

day = "10",

doi = "10.1016/0014-5793(87)80905-5",

language = "English (US)",

volume = "220",

pages = "209--213",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "1",

}

TY - JOUR

T1 - Aldose reductase and ϱ-crystallin belong to the same protein superfamily as aldehyde reductase

AU - Carper, Deborah

AU - Nishimura, Chihiro

AU - Shinohara, Toshimichi

AU - Dietzchold, Bernard

AU - Wistow, Graeme

AU - Craft, Cheryl

AU - Kador, Peter

AU - Kinoshita, Jin H.

PY - 1987/8/10

Y1 - 1987/8/10

N2 - Aldose reductase (EC 1.1.1.21) has been implicated in a variety of diabetic complications. Here we present the first primary sequence data for the rat lens enzyme, obtained by amino acid and cDNA analysis. We have found structural similarities with another NADPH-dependent oxidoreductase: human liver aldehyde reductase (EC 1.1.1.2). The identity between these two enzymes is 50%. Both enzymes share approx. 40-50% homology with ρ{variant}-crystallin, a major lens protein present only in the frog, Rana pipiens. We propose that aldose reductase, aldehyde reductase and ρ{variant}-crystallin are members of a superfamily of related proteins.

AB - Aldose reductase (EC 1.1.1.21) has been implicated in a variety of diabetic complications. Here we present the first primary sequence data for the rat lens enzyme, obtained by amino acid and cDNA analysis. We have found structural similarities with another NADPH-dependent oxidoreductase: human liver aldehyde reductase (EC 1.1.1.2). The identity between these two enzymes is 50%. Both enzymes share approx. 40-50% homology with ρ{variant}-crystallin, a major lens protein present only in the frog, Rana pipiens. We propose that aldose reductase, aldehyde reductase and ρ{variant}-crystallin are members of a superfamily of related proteins.

KW - Aldehyde reductase

KW - Aldose reductase

KW - Structural homology

KW - cDNA sequence

KW - ρ{variant}-Crystallin

UR - http://www.scopus.com/inward/record.url?scp=0023650008&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023650008&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(87)80905-5

DO - 10.1016/0014-5793(87)80905-5

M3 - Article

C2 - 3111886

AN - SCOPUS:0023650008

SN - 0014-5793

VL - 220

SP - 209

EP - 213

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Aldose reductase and ϱ-crystallin belong to the same protein superfamily as aldehyde reductase

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this