Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo

Marc Rendell, Julia Nierenberg, Carol Brannan, J. L. Valentine, P. M. Stephen, Steven Dodds, Preston Mercer, Paul K. Smith, Joseph Walder

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Aspirin (acetylsalicylic acid or ASA) is known to inhibit glycosylation (glycation) of albumin in vitro. The mechanism has been presumed to be acetylation, but this has never been validated. The new affinity aminophenylboronic acid procedure for determination of glycosylated albumin was used to demonstrate inhibition of glycosylation by aspirin. ASA, but not salicylic acid, inhibited glycation. The inhibition of glycation by equimolar acetic anhydride was greater than that by ASA. Pretreatment of albumin with ASA in the absence of glucose demonstrated that inhibition was extremely rapid, occurring in a matter of minutes. However, the inhibition by ASA could not be prevented by massive acceleration of glycation induced by borohydride reduction. Glycation of hemoglobin was also inhibited by ASA, but the dose requirement was considerably higher. Various analogues of ASA were evaluated for inhibition of glycation. Only acetyl-5-ethylsalicylic acid was more effective than ASA in inhibiting albumin glycation. None of these agents was more potent than ASA in inhibiting glycation of hemoglobin. ASA was fed to diabetic rats in a long-term experiment. Glycohemoglobin and glycoalbumin levels were decreased by ASA administration. We conclude that ASA inhibits glycation by a very rapid acetylation process. This process is apparently quite selective in terms of the protein involved, presumably because of the local environment of affected lysine groups. The phenomenon can be produced in vivo by administration of ASA.

Original languageEnglish
Pages (from-to)277-285
Number of pages9
JournalThe Journal of Laboratory and Clinical Medicine
Volume108
Issue number4
StatePublished - 1986

Fingerprint

Glycosylation
Acetylation
Albumins
Hemoglobins
Aspirin
In Vitro Techniques
Borohydrides
Salicylic Acid
Lysine
Rats
Glucose

All Science Journal Classification (ASJC) codes

  • Medicine(all)
  • Pathology and Forensic Medicine

Cite this

Rendell, M., Nierenberg, J., Brannan, C., Valentine, J. L., Stephen, P. M., Dodds, S., ... Walder, J. (1986). Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo. The Journal of Laboratory and Clinical Medicine, 108(4), 277-285.

Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo. / Rendell, Marc; Nierenberg, Julia; Brannan, Carol; Valentine, J. L.; Stephen, P. M.; Dodds, Steven; Mercer, Preston; Smith, Paul K.; Walder, Joseph.

In: The Journal of Laboratory and Clinical Medicine, Vol. 108, No. 4, 1986, p. 277-285.

Research output: Contribution to journalArticle

Rendell, M, Nierenberg, J, Brannan, C, Valentine, JL, Stephen, PM, Dodds, S, Mercer, P, Smith, PK & Walder, J 1986, 'Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo', The Journal of Laboratory and Clinical Medicine, vol. 108, no. 4, pp. 277-285.
Rendell M, Nierenberg J, Brannan C, Valentine JL, Stephen PM, Dodds S et al. Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo. The Journal of Laboratory and Clinical Medicine. 1986;108(4):277-285.
Rendell, Marc ; Nierenberg, Julia ; Brannan, Carol ; Valentine, J. L. ; Stephen, P. M. ; Dodds, Steven ; Mercer, Preston ; Smith, Paul K. ; Walder, Joseph. / Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo. In: The Journal of Laboratory and Clinical Medicine. 1986 ; Vol. 108, No. 4. pp. 277-285.
@article{44499819513048bcabfc0844183e9aff,
title = "Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo",
abstract = "Aspirin (acetylsalicylic acid or ASA) is known to inhibit glycosylation (glycation) of albumin in vitro. The mechanism has been presumed to be acetylation, but this has never been validated. The new affinity aminophenylboronic acid procedure for determination of glycosylated albumin was used to demonstrate inhibition of glycosylation by aspirin. ASA, but not salicylic acid, inhibited glycation. The inhibition of glycation by equimolar acetic anhydride was greater than that by ASA. Pretreatment of albumin with ASA in the absence of glucose demonstrated that inhibition was extremely rapid, occurring in a matter of minutes. However, the inhibition by ASA could not be prevented by massive acceleration of glycation induced by borohydride reduction. Glycation of hemoglobin was also inhibited by ASA, but the dose requirement was considerably higher. Various analogues of ASA were evaluated for inhibition of glycation. Only acetyl-5-ethylsalicylic acid was more effective than ASA in inhibiting albumin glycation. None of these agents was more potent than ASA in inhibiting glycation of hemoglobin. ASA was fed to diabetic rats in a long-term experiment. Glycohemoglobin and glycoalbumin levels were decreased by ASA administration. We conclude that ASA inhibits glycation by a very rapid acetylation process. This process is apparently quite selective in terms of the protein involved, presumably because of the local environment of affected lysine groups. The phenomenon can be produced in vivo by administration of ASA.",
author = "Marc Rendell and Julia Nierenberg and Carol Brannan and Valentine, {J. L.} and Stephen, {P. M.} and Steven Dodds and Preston Mercer and Smith, {Paul K.} and Joseph Walder",
year = "1986",
language = "English",
volume = "108",
pages = "277--285",
journal = "Translational Research",
issn = "1931-5244",
publisher = "Mosby Inc.",
number = "4",

}

TY - JOUR

T1 - Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo

AU - Rendell, Marc

AU - Nierenberg, Julia

AU - Brannan, Carol

AU - Valentine, J. L.

AU - Stephen, P. M.

AU - Dodds, Steven

AU - Mercer, Preston

AU - Smith, Paul K.

AU - Walder, Joseph

PY - 1986

Y1 - 1986

N2 - Aspirin (acetylsalicylic acid or ASA) is known to inhibit glycosylation (glycation) of albumin in vitro. The mechanism has been presumed to be acetylation, but this has never been validated. The new affinity aminophenylboronic acid procedure for determination of glycosylated albumin was used to demonstrate inhibition of glycosylation by aspirin. ASA, but not salicylic acid, inhibited glycation. The inhibition of glycation by equimolar acetic anhydride was greater than that by ASA. Pretreatment of albumin with ASA in the absence of glucose demonstrated that inhibition was extremely rapid, occurring in a matter of minutes. However, the inhibition by ASA could not be prevented by massive acceleration of glycation induced by borohydride reduction. Glycation of hemoglobin was also inhibited by ASA, but the dose requirement was considerably higher. Various analogues of ASA were evaluated for inhibition of glycation. Only acetyl-5-ethylsalicylic acid was more effective than ASA in inhibiting albumin glycation. None of these agents was more potent than ASA in inhibiting glycation of hemoglobin. ASA was fed to diabetic rats in a long-term experiment. Glycohemoglobin and glycoalbumin levels were decreased by ASA administration. We conclude that ASA inhibits glycation by a very rapid acetylation process. This process is apparently quite selective in terms of the protein involved, presumably because of the local environment of affected lysine groups. The phenomenon can be produced in vivo by administration of ASA.

AB - Aspirin (acetylsalicylic acid or ASA) is known to inhibit glycosylation (glycation) of albumin in vitro. The mechanism has been presumed to be acetylation, but this has never been validated. The new affinity aminophenylboronic acid procedure for determination of glycosylated albumin was used to demonstrate inhibition of glycosylation by aspirin. ASA, but not salicylic acid, inhibited glycation. The inhibition of glycation by equimolar acetic anhydride was greater than that by ASA. Pretreatment of albumin with ASA in the absence of glucose demonstrated that inhibition was extremely rapid, occurring in a matter of minutes. However, the inhibition by ASA could not be prevented by massive acceleration of glycation induced by borohydride reduction. Glycation of hemoglobin was also inhibited by ASA, but the dose requirement was considerably higher. Various analogues of ASA were evaluated for inhibition of glycation. Only acetyl-5-ethylsalicylic acid was more effective than ASA in inhibiting albumin glycation. None of these agents was more potent than ASA in inhibiting glycation of hemoglobin. ASA was fed to diabetic rats in a long-term experiment. Glycohemoglobin and glycoalbumin levels were decreased by ASA administration. We conclude that ASA inhibits glycation by a very rapid acetylation process. This process is apparently quite selective in terms of the protein involved, presumably because of the local environment of affected lysine groups. The phenomenon can be produced in vivo by administration of ASA.

UR - http://www.scopus.com/inward/record.url?scp=46149132560&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=46149132560&partnerID=8YFLogxK

M3 - Article

VL - 108

SP - 277

EP - 285

JO - Translational Research

JF - Translational Research

SN - 1931-5244

IS - 4

ER -