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

Bonay, Pedro ; Solís, Juan ; de la Calle, Hermenegildo ; Fresno, Manuel ; Grubb, Anders LU orcid and Méndez, Enrique (1997) In FEBS Letters 416(3). p.276-280
Abstract

Human protein HC is a member of the lipocalin superfamily with unique properties since it carries a covalently bound fluorescent chromophore mediating the linkage of the major part of protein HC to several plasma proteins, with IgA as the dominating complex partner. Native protein HC displays characteristic absorption and fluorescence spectra similar to those of glycated proteins with advanced glycosylation end products (AGEs). In vitro glycation of protein HC induces the formation of fibril aggregates with a corresponding increase of absorption in the visible region of the spectrum. Boronate-affinity chromatography and a novel galactosyltransferase assay indicate that protein HC is modified with residues of glucose exposed in a... (More)

Human protein HC is a member of the lipocalin superfamily with unique properties since it carries a covalently bound fluorescent chromophore mediating the linkage of the major part of protein HC to several plasma proteins, with IgA as the dominating complex partner. Native protein HC displays characteristic absorption and fluorescence spectra similar to those of glycated proteins with advanced glycosylation end products (AGEs). In vitro glycation of protein HC induces the formation of fibril aggregates with a corresponding increase of absorption in the visible region of the spectrum. Boronate-affinity chromatography and a novel galactosyltransferase assay indicate that protein HC is modified with residues of glucose exposed in a terminal non-reducing position which is typical of glycated proteins. The glycation level of several isolated batches of protein HC as measured by both assays was around 35%, which represents the highest level described for human plasma-derived proteins from healthy individuals.

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author
; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Alpha-Globulins/chemistry, Chromatography, Affinity, Chromatography, High Pressure Liquid, Colorimetry, Diabetes Mellitus, Galactosyltransferases, Glycoside Hydrolases, Glycosylation, Humans, Protease Inhibitors/chemistry, Reference Values
in
FEBS Letters
volume
416
issue
3
pages
276 - 280
publisher
Wiley-Blackwell
external identifiers
  • scopus:0030722201
  • pmid:9373169
ISSN
0014-5793
DOI
10.1016/s0014-5793(97)01220-9
language
English
LU publication?
no
id
b05c39ed-6e23-4b17-bd66-343f5689479e
date added to LUP
2021-10-29 10:05:08
date last changed
2024-01-12 02:55:26
@article{b05c39ed-6e23-4b17-bd66-343f5689479e,
  abstract     = {{<p>Human protein HC is a member of the lipocalin superfamily with unique properties since it carries a covalently bound fluorescent chromophore mediating the linkage of the major part of protein HC to several plasma proteins, with IgA as the dominating complex partner. Native protein HC displays characteristic absorption and fluorescence spectra similar to those of glycated proteins with advanced glycosylation end products (AGEs). In vitro glycation of protein HC induces the formation of fibril aggregates with a corresponding increase of absorption in the visible region of the spectrum. Boronate-affinity chromatography and a novel galactosyltransferase assay indicate that protein HC is modified with residues of glucose exposed in a terminal non-reducing position which is typical of glycated proteins. The glycation level of several isolated batches of protein HC as measured by both assays was around 35%, which represents the highest level described for human plasma-derived proteins from healthy individuals.</p>}},
  author       = {{Bonay, Pedro and Solís, Juan and de la Calle, Hermenegildo and Fresno, Manuel and Grubb, Anders and Méndez, Enrique}},
  issn         = {{0014-5793}},
  keywords     = {{Alpha-Globulins/chemistry; Chromatography, Affinity; Chromatography, High Pressure Liquid; Colorimetry; Diabetes Mellitus; Galactosyltransferases; Glycoside Hydrolases; Glycosylation; Humans; Protease Inhibitors/chemistry; Reference Values}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{276--280}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{FEBS Letters}},
  title        = {{Massive glycation of protein HC, a low molecular weight lipocalin, in non-diabetic individuals}},
  url          = {{http://dx.doi.org/10.1016/s0014-5793(97)01220-9}},
  doi          = {{10.1016/s0014-5793(97)01220-9}},
  volume       = {{416}},
  year         = {{1997}},
}