Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Proteome analysis of cultured fibroblasts from type 1 diabetic patients and normal subjects

Puricelli, Lucia ; Iori, Elisabetta ; Millioni, Renato ; Arrigoni, Giorgio LU ; James, Peter LU ; Vedovato, Monica and Tessari, Paolo (2006) In Journal of Clinical Endocrinology and Metabolism 91(9). p.3507-3514
Abstract
Context: Protein profiling of diabetic tissues could provide useful biomarkers for early diagnosis, therapeutic targets, and disease response markers. Cultured fibroblasts are a useful in vitro model for proteome analysis and study of the molecular mechanisms involved in diabetes. Objective: The objective of the study was to isolate and characterize the proteins of cultured fibroblasts, obtained by skin biopsy, from long-term type 1 diabetic patients without complications and age- and sex-matched normal subjects as controls. Design: Proteins were separated by two-dimensional electrophoresis (2-DE), and the gel images were qualitatively and quantitatively analyzed. Protein identification was performed by matrix-assisted laser... (More)
Context: Protein profiling of diabetic tissues could provide useful biomarkers for early diagnosis, therapeutic targets, and disease response markers. Cultured fibroblasts are a useful in vitro model for proteome analysis and study of the molecular mechanisms involved in diabetes. Objective: The objective of the study was to isolate and characterize the proteins of cultured fibroblasts, obtained by skin biopsy, from long-term type 1 diabetic patients without complications and age- and sex-matched normal subjects as controls. Design: Proteins were separated by two-dimensional electrophoresis (2-DE), and the gel images were qualitatively and quantitatively analyzed. Protein identification was performed by matrix-assisted laser desorption/ionization mass spectrometry. Results: Reproducible protein maps of fibroblasts from diabetic and healthy subjects were obtained. A total of 125 protein spots were isolated and identified, among them 27 proteins not previously reported in published human fibroblast 2-DE maps, including 20 proteins never reported previously in the literature in human skin fibroblasts. Quantitative analyses revealed six protein spots differentially expressed in the fibroblasts from the diabetic vs. the control subjects (P < 0.05), representing glycolytic enzymes and structural proteins. An increase of triosephosphate I isomerase of two splice isoforms of pyruvate kinase and alpha-actinin 4 and a decrease of tubulin-beta 2 and splice isoform 2 of tropomyosin beta-chain were detected. Conclusions: We generated 2-DE reference maps of the proteome of human skin fibroblasts from both normal and uncomplicated type 1 diabetic patients. Differences in glycolytic enzymes and structural proteins were found. The functional implications of the identified proteins are discussed. (Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Clinical Endocrinology and Metabolism
volume
91
issue
9
pages
3507 - 3514
publisher
Oxford University Press
external identifiers
  • wos:000240358600043
  • pmid:16822825
  • scopus:33748755546
ISSN
1945-7197
DOI
10.1210/jc.2006-0274
language
English
LU publication?
yes
id
e6c42391-89dc-4940-8b19-fa235b8281bd (old id 394103)
date added to LUP
2016-04-01 16:44:56
date last changed
2021-08-04 03:54:31
@article{e6c42391-89dc-4940-8b19-fa235b8281bd,
  abstract     = {Context: Protein profiling of diabetic tissues could provide useful biomarkers for early diagnosis, therapeutic targets, and disease response markers. Cultured fibroblasts are a useful in vitro model for proteome analysis and study of the molecular mechanisms involved in diabetes. Objective: The objective of the study was to isolate and characterize the proteins of cultured fibroblasts, obtained by skin biopsy, from long-term type 1 diabetic patients without complications and age- and sex-matched normal subjects as controls. Design: Proteins were separated by two-dimensional electrophoresis (2-DE), and the gel images were qualitatively and quantitatively analyzed. Protein identification was performed by matrix-assisted laser desorption/ionization mass spectrometry. Results: Reproducible protein maps of fibroblasts from diabetic and healthy subjects were obtained. A total of 125 protein spots were isolated and identified, among them 27 proteins not previously reported in published human fibroblast 2-DE maps, including 20 proteins never reported previously in the literature in human skin fibroblasts. Quantitative analyses revealed six protein spots differentially expressed in the fibroblasts from the diabetic vs. the control subjects (P &lt; 0.05), representing glycolytic enzymes and structural proteins. An increase of triosephosphate I isomerase of two splice isoforms of pyruvate kinase and alpha-actinin 4 and a decrease of tubulin-beta 2 and splice isoform 2 of tropomyosin beta-chain were detected. Conclusions: We generated 2-DE reference maps of the proteome of human skin fibroblasts from both normal and uncomplicated type 1 diabetic patients. Differences in glycolytic enzymes and structural proteins were found. The functional implications of the identified proteins are discussed.},
  author       = {Puricelli, Lucia and Iori, Elisabetta and Millioni, Renato and Arrigoni, Giorgio and James, Peter and Vedovato, Monica and Tessari, Paolo},
  issn         = {1945-7197},
  language     = {eng},
  number       = {9},
  pages        = {3507--3514},
  publisher    = {Oxford University Press},
  series       = {Journal of Clinical Endocrinology and Metabolism},
  title        = {Proteome analysis of cultured fibroblasts from type 1 diabetic patients and normal subjects},
  url          = {http://dx.doi.org/10.1210/jc.2006-0274},
  doi          = {10.1210/jc.2006-0274},
  volume       = {91},
  year         = {2006},
}