Nonenzymatic glycosylation of peripheral nerve protein in diabetes mellitus

H. Vlassara, M. Brownlee, A. Cerami

Research output: Contribution to journalArticle

183 Citations (Scopus)

Abstract

A new affinity chromatography system that selectively retains glycosylated amino acids has been utilized to determine the amount of nonenzymatic glycosylation present in peripheral nerve from diabetic and control rats and dogs. The mean value for glycosylated amino acids in diabetic rats was 2.8 times greater than the mean value in normal rats (P<0.001). In diabetic dogs, mean values were 2.15 times greater than normal values (P<0.05). Amino acid analysis of reduced, glycosylated amino acids previously isolated by affinity chromatography showed that glycosylated lysine and its hydrolysis rearrangement products were the major borohydride-reducible adduct present. In addition, another glycosylated product was noted to be present in major proportions. This radioactive product did not chromatograph with any of the available glycosylated amino acid standards. The finding that diabetes results in a nearly 3-fold increase of peripheral nerve glycosylation is consistent with a number of previous investigations in which glycosylation was measured in hemoglobin, serum albumin, and urinary amino acids and peptides from diabetics and normals. The results reported here provide evidence that increased nonenzymatic glycosylation is occurring in a tissue where physiological, morphological, and clinical degeneration characteristically develop as a result of diabetes mellitus.

Original languageEnglish (US)
Pages (from-to)5190-5192
Number of pages3
JournalProceedings of the National Academy of Sciences of the United States of America
Volume78
Issue number8 I
StatePublished - 1981
Externally publishedYes

Fingerprint

Glycosylation
Peripheral Nerves
Diabetes Mellitus
Amino Acids
Proteins
Affinity Chromatography
Reference Values
Dogs
Borohydrides
Serum Albumin
Hemoglobins
Hydrolysis
Peptides

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Nonenzymatic glycosylation of peripheral nerve protein in diabetes mellitus. / Vlassara, H.; Brownlee, M.; Cerami, A.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 78, No. 8 I, 1981, p. 5190-5192.

Research output: Contribution to journalArticle

@article{d6f177a013fa454a8808095e49cfbe50,
title = "Nonenzymatic glycosylation of peripheral nerve protein in diabetes mellitus",
abstract = "A new affinity chromatography system that selectively retains glycosylated amino acids has been utilized to determine the amount of nonenzymatic glycosylation present in peripheral nerve from diabetic and control rats and dogs. The mean value for glycosylated amino acids in diabetic rats was 2.8 times greater than the mean value in normal rats (P<0.001). In diabetic dogs, mean values were 2.15 times greater than normal values (P<0.05). Amino acid analysis of reduced, glycosylated amino acids previously isolated by affinity chromatography showed that glycosylated lysine and its hydrolysis rearrangement products were the major borohydride-reducible adduct present. In addition, another glycosylated product was noted to be present in major proportions. This radioactive product did not chromatograph with any of the available glycosylated amino acid standards. The finding that diabetes results in a nearly 3-fold increase of peripheral nerve glycosylation is consistent with a number of previous investigations in which glycosylation was measured in hemoglobin, serum albumin, and urinary amino acids and peptides from diabetics and normals. The results reported here provide evidence that increased nonenzymatic glycosylation is occurring in a tissue where physiological, morphological, and clinical degeneration characteristically develop as a result of diabetes mellitus.",
author = "H. Vlassara and M. Brownlee and A. Cerami",
year = "1981",
language = "English (US)",
volume = "78",
pages = "5190--5192",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "8 I",

}

TY - JOUR

T1 - Nonenzymatic glycosylation of peripheral nerve protein in diabetes mellitus

AU - Vlassara, H.

AU - Brownlee, M.

AU - Cerami, A.

PY - 1981

Y1 - 1981

N2 - A new affinity chromatography system that selectively retains glycosylated amino acids has been utilized to determine the amount of nonenzymatic glycosylation present in peripheral nerve from diabetic and control rats and dogs. The mean value for glycosylated amino acids in diabetic rats was 2.8 times greater than the mean value in normal rats (P<0.001). In diabetic dogs, mean values were 2.15 times greater than normal values (P<0.05). Amino acid analysis of reduced, glycosylated amino acids previously isolated by affinity chromatography showed that glycosylated lysine and its hydrolysis rearrangement products were the major borohydride-reducible adduct present. In addition, another glycosylated product was noted to be present in major proportions. This radioactive product did not chromatograph with any of the available glycosylated amino acid standards. The finding that diabetes results in a nearly 3-fold increase of peripheral nerve glycosylation is consistent with a number of previous investigations in which glycosylation was measured in hemoglobin, serum albumin, and urinary amino acids and peptides from diabetics and normals. The results reported here provide evidence that increased nonenzymatic glycosylation is occurring in a tissue where physiological, morphological, and clinical degeneration characteristically develop as a result of diabetes mellitus.

AB - A new affinity chromatography system that selectively retains glycosylated amino acids has been utilized to determine the amount of nonenzymatic glycosylation present in peripheral nerve from diabetic and control rats and dogs. The mean value for glycosylated amino acids in diabetic rats was 2.8 times greater than the mean value in normal rats (P<0.001). In diabetic dogs, mean values were 2.15 times greater than normal values (P<0.05). Amino acid analysis of reduced, glycosylated amino acids previously isolated by affinity chromatography showed that glycosylated lysine and its hydrolysis rearrangement products were the major borohydride-reducible adduct present. In addition, another glycosylated product was noted to be present in major proportions. This radioactive product did not chromatograph with any of the available glycosylated amino acid standards. The finding that diabetes results in a nearly 3-fold increase of peripheral nerve glycosylation is consistent with a number of previous investigations in which glycosylation was measured in hemoglobin, serum albumin, and urinary amino acids and peptides from diabetics and normals. The results reported here provide evidence that increased nonenzymatic glycosylation is occurring in a tissue where physiological, morphological, and clinical degeneration characteristically develop as a result of diabetes mellitus.

UR - http://www.scopus.com/inward/record.url?scp=0042043570&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0042043570&partnerID=8YFLogxK

M3 - Article

C2 - 6946466

AN - SCOPUS:0042043570

VL - 78

SP - 5190

EP - 5192

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 - 8 I

ER -