Massive glycation of protein HC, a low molecular weight lipocalin, in non-diabetic individuals

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P Bonay1, J Solís, H de la Calle

  • 1Unidad de Análisis Estructural de Proteínas, Centro Nacional de Biotecnología, Madrid, Spain.

FEBS Letters
|December 31, 1997
PubMed

Insights

Human protein HC, a lipocalin, naturally binds IgA and exhibits advanced glycosylation end products (AGEs). In vitro studies show glycation forms fibrils, with 35% glycation in healthy individuals, a high level for plasma proteins.

Area of Science:

  • Biochemistry
  • Proteomics
  • Glycobiology

Background:

  • Human protein HC (also known as HEPC) is a lipocalin superfamily member.
  • It uniquely binds plasma proteins, predominantly IgA, via a fluorescent chromophore.
  • Native protein HC exhibits spectral properties resembling advanced glycosylation end products (AGEs).

Purpose of the Study:

  • To investigate the glycation status of human protein HC.
  • To characterize the effects of in vitro glycation on protein HC structure and properties.
  • To quantify the glycation level in plasma-derived protein HC from healthy individuals.

Main Methods:

  • Spectroscopic analysis (absorption and fluorescence) of native and glycated protein HC.
  • In vitro glycation experiments to induce fibril formation.
  • Boronate-affinity chromatography to assess glycated protein HC.
  • Galactosyltransferase assay to quantify glucose residues.

Main Results:

  • In vitro glycation of protein HC led to fibril aggregate formation and increased visible light absorption.
  • Boronate-affinity chromatography and galactosyltransferase assay confirmed glucose modification in a terminal non-reducing position.
  • Human protein HC demonstrated a significant glycation level of approximately 35%.

Conclusions:

  • Human protein HC is naturally glycated, exhibiting spectral characteristics of AGEs.
  • The observed glycation level of 35% is notably high for plasma proteins from healthy individuals.
  • These findings suggest protein HC as a potential biomarker or player in glycation-related processes.

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