Activation of aldose reductase from human tissues

B. Das, Satish Srivastava

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

Human aorta, brain, and muscle aldose reductase, partially purified by DEAE-cellulose (DE-52) column chromatography, is activated 2-2.5-fold on incubation with 10 μM each of glucose-6-phosphate, NADPH, and glucose for 20 min at 25°C. The activation of the enzyme was established by following the NADPH oxidation as well as the sorbitol formation using glucose as substrate. The activated form of aldose reductase exhibited monophasic kinetics with glucose and glyceraldehyde, whereas the unactivated or native enzyme exhibited a biphasic kinetics with both the substrates. The activated enzyme was less susceptible to inhibition by aldose reductase inhibitors such as sorbinil, alrestatin, and quercetrin as compared with the unactivated enzyme. Similarly, the native enzyme was strongly inhibited by some of the phosphorylated intermediates of glycolytic pathway, such as 3-phosphoglycerate, 1,3-diphosphoglycerate, 2,3-diphosphoglycerate, and ADP, whereas the activated enzyme was either not inhibited or inhibition was 20-30% only. Partially purified aldose reductase from the normal human lens exhibited properties similar to the native enzyme of other tissues, whereas the enzyme from clear lens obtained from diabetic subjects with severe hyperglycemia expressed properties similar to the in vitro activated enzyme of aorta, brain, and muscle.

Original languageEnglish (US)
Pages (from-to)1145-1151
Number of pages7
JournalDiabetes
Volume34
Issue number11
StatePublished - 1985

Fingerprint

Aldehyde Reductase
Enzymes
NADP
Glucose
Lenses
Aorta
Glyceraldehyde
2,3-Diphosphoglycerate
Muscles
DEAE-Cellulose
Glucose-6-Phosphate
Enzyme Activation
Sorbitol
Brain
Hyperglycemia
Adenosine Diphosphate
Chromatography

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Internal Medicine

Cite this

Das, B., & Srivastava, S. (1985). Activation of aldose reductase from human tissues. Diabetes, 34(11), 1145-1151.

Activation of aldose reductase from human tissues. / Das, B.; Srivastava, Satish.

In: Diabetes, Vol. 34, No. 11, 1985, p. 1145-1151.

Research output: Contribution to journalArticle

Das, B & Srivastava, S 1985, 'Activation of aldose reductase from human tissues', Diabetes, vol. 34, no. 11, pp. 1145-1151.
Das B, Srivastava S. Activation of aldose reductase from human tissues. Diabetes. 1985;34(11):1145-1151.
Das, B. ; Srivastava, Satish. / Activation of aldose reductase from human tissues. In: Diabetes. 1985 ; Vol. 34, No. 11. pp. 1145-1151.
@article{b19551210d654222ac4956dccf454333,
title = "Activation of aldose reductase from human tissues",
abstract = "Human aorta, brain, and muscle aldose reductase, partially purified by DEAE-cellulose (DE-52) column chromatography, is activated 2-2.5-fold on incubation with 10 μM each of glucose-6-phosphate, NADPH, and glucose for 20 min at 25°C. The activation of the enzyme was established by following the NADPH oxidation as well as the sorbitol formation using glucose as substrate. The activated form of aldose reductase exhibited monophasic kinetics with glucose and glyceraldehyde, whereas the unactivated or native enzyme exhibited a biphasic kinetics with both the substrates. The activated enzyme was less susceptible to inhibition by aldose reductase inhibitors such as sorbinil, alrestatin, and quercetrin as compared with the unactivated enzyme. Similarly, the native enzyme was strongly inhibited by some of the phosphorylated intermediates of glycolytic pathway, such as 3-phosphoglycerate, 1,3-diphosphoglycerate, 2,3-diphosphoglycerate, and ADP, whereas the activated enzyme was either not inhibited or inhibition was 20-30{\%} only. Partially purified aldose reductase from the normal human lens exhibited properties similar to the native enzyme of other tissues, whereas the enzyme from clear lens obtained from diabetic subjects with severe hyperglycemia expressed properties similar to the in vitro activated enzyme of aorta, brain, and muscle.",
author = "B. Das and Satish Srivastava",
year = "1985",
language = "English (US)",
volume = "34",
pages = "1145--1151",
journal = "Diabetes",
issn = "0012-1797",
publisher = "American Diabetes Association Inc.",
number = "11",

}

TY - JOUR

T1 - Activation of aldose reductase from human tissues

AU - Das, B.

AU - Srivastava, Satish

PY - 1985

Y1 - 1985

N2 - Human aorta, brain, and muscle aldose reductase, partially purified by DEAE-cellulose (DE-52) column chromatography, is activated 2-2.5-fold on incubation with 10 μM each of glucose-6-phosphate, NADPH, and glucose for 20 min at 25°C. The activation of the enzyme was established by following the NADPH oxidation as well as the sorbitol formation using glucose as substrate. The activated form of aldose reductase exhibited monophasic kinetics with glucose and glyceraldehyde, whereas the unactivated or native enzyme exhibited a biphasic kinetics with both the substrates. The activated enzyme was less susceptible to inhibition by aldose reductase inhibitors such as sorbinil, alrestatin, and quercetrin as compared with the unactivated enzyme. Similarly, the native enzyme was strongly inhibited by some of the phosphorylated intermediates of glycolytic pathway, such as 3-phosphoglycerate, 1,3-diphosphoglycerate, 2,3-diphosphoglycerate, and ADP, whereas the activated enzyme was either not inhibited or inhibition was 20-30% only. Partially purified aldose reductase from the normal human lens exhibited properties similar to the native enzyme of other tissues, whereas the enzyme from clear lens obtained from diabetic subjects with severe hyperglycemia expressed properties similar to the in vitro activated enzyme of aorta, brain, and muscle.

AB - Human aorta, brain, and muscle aldose reductase, partially purified by DEAE-cellulose (DE-52) column chromatography, is activated 2-2.5-fold on incubation with 10 μM each of glucose-6-phosphate, NADPH, and glucose for 20 min at 25°C. The activation of the enzyme was established by following the NADPH oxidation as well as the sorbitol formation using glucose as substrate. The activated form of aldose reductase exhibited monophasic kinetics with glucose and glyceraldehyde, whereas the unactivated or native enzyme exhibited a biphasic kinetics with both the substrates. The activated enzyme was less susceptible to inhibition by aldose reductase inhibitors such as sorbinil, alrestatin, and quercetrin as compared with the unactivated enzyme. Similarly, the native enzyme was strongly inhibited by some of the phosphorylated intermediates of glycolytic pathway, such as 3-phosphoglycerate, 1,3-diphosphoglycerate, 2,3-diphosphoglycerate, and ADP, whereas the activated enzyme was either not inhibited or inhibition was 20-30% only. Partially purified aldose reductase from the normal human lens exhibited properties similar to the native enzyme of other tissues, whereas the enzyme from clear lens obtained from diabetic subjects with severe hyperglycemia expressed properties similar to the in vitro activated enzyme of aorta, brain, and muscle.

UR - http://www.scopus.com/inward/record.url?scp=0022359247&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022359247&partnerID=8YFLogxK

M3 - Article

C2 - 3930326

AN - SCOPUS:0022359247

VL - 34

SP - 1145

EP - 1151

JO - Diabetes

JF - Diabetes

SN - 0012-1797

IS - 11

ER -