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
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.
(Less)
- author
- Bonay, Pedro
; Solís, Juan
; de la Calle, Hermenegildo
; Fresno, Manuel
; Grubb, Anders
LU
and Méndez, Enrique
- publishing date
- 1997
- 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}},
}