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Abnormal cytoskeletal protein expression in cultured skin fibroblasts form type 1 diabetes mellitus patiens with nephropathy: A proteomic approach

Millioni, R.; Lori, E.; Puricelli, L.; Arrigoni, Giorgio LU ; Vedovato, M.; Trevisan, R.; James, Peter LU ; Tiengo, A. and Tessari, P. (2008) In Proteomics Clinical Applications 2(4). p.492-503
Abstract
Diabetic nephropathy (DN) develops in about 40% of insulin-dependent type 1 diabetes mellitus (TlDM) patients, and is associated not only with diabetes duration and metabolic control, but also with a genetic predisposition. Constitutive alterations of cytoskeletal proteins may play a role in the development of DN. We investigated the expression of these proteins in cultured skin fibroblasts, obtained from long-term TlDM patients with and without DN but comparable metabolic control, and from matched healthy subjects, by means of 2-DE electrophoresis and MS-MALDI analyses. In T1DM with DN, compared to the other two groups, quantitative analyses revealed an altered expression of 17 spots (p < 0.05-p < 0.01), corresponding to 12 unique... (More)
Diabetic nephropathy (DN) develops in about 40% of insulin-dependent type 1 diabetes mellitus (TlDM) patients, and is associated not only with diabetes duration and metabolic control, but also with a genetic predisposition. Constitutive alterations of cytoskeletal proteins may play a role in the development of DN. We investigated the expression of these proteins in cultured skin fibroblasts, obtained from long-term TlDM patients with and without DN but comparable metabolic control, and from matched healthy subjects, by means of 2-DE electrophoresis and MS-MALDI analyses. In T1DM with DN, compared to the other two groups, quantitative analyses revealed an altered expression of 17 spots (p < 0.05-p < 0.01), corresponding to 12 unique proteins. In T1DM with DN, beta-actin and three isoforms of tubulin beta-2 chain, tropomodulin-3, and LASP-1 were decreased, whereas two tubulin beta-4 chain isoforms, one alpha actinin4 isoform, membrane-organizing extension spike protein (MOESIN), FLJ00279 (corresponding to a fragment of myosin heavy chain, non-muscle type A), vinculin, a tropomyosin isoform, and the macrophage capping protein were increased. A shift in caldesmon isoforms was also detected. These results demonstrate an association between DN and the constitutive expression of cytoskeleton proteins in cultured skin fibroblasts from TlDM with DN, which may retain pathophysiologycal implications. (Less)
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author
organization
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Contribution to journal
publication status
published
subject
keywords
IDDM PATIENTS, ACTIN POLYMERIZATION, ANTIPORT ACTIVITY, cytoskeletal proteins, PHENOTYPE, ASSIGNMENT, MICROALBUMINURIA, INSULIN, ERM PROTEINS, MESANGIAL CELLS, GENE-EXPRESSION, diabetic nephropathy, fibroblasts
in
Proteomics Clinical Applications
volume
2
issue
4
pages
492 - 503
publisher
John Wiley & Sons
external identifiers
  • wos:000255153400004
  • scopus:42449085888
ISSN
1862-8354
DOI
10.1002/prca.200780112
language
English
LU publication?
yes
id
1dbf1900-e929-4248-875f-456c7eee0ebb (old id 1417355)
date added to LUP
2009-06-15 10:13:44
date last changed
2017-04-09 03:35:39
@article{1dbf1900-e929-4248-875f-456c7eee0ebb,
  abstract     = {Diabetic nephropathy (DN) develops in about 40% of insulin-dependent type 1 diabetes mellitus (TlDM) patients, and is associated not only with diabetes duration and metabolic control, but also with a genetic predisposition. Constitutive alterations of cytoskeletal proteins may play a role in the development of DN. We investigated the expression of these proteins in cultured skin fibroblasts, obtained from long-term TlDM patients with and without DN but comparable metabolic control, and from matched healthy subjects, by means of 2-DE electrophoresis and MS-MALDI analyses. In T1DM with DN, compared to the other two groups, quantitative analyses revealed an altered expression of 17 spots (p &lt; 0.05-p &lt; 0.01), corresponding to 12 unique proteins. In T1DM with DN, beta-actin and three isoforms of tubulin beta-2 chain, tropomodulin-3, and LASP-1 were decreased, whereas two tubulin beta-4 chain isoforms, one alpha actinin4 isoform, membrane-organizing extension spike protein (MOESIN), FLJ00279 (corresponding to a fragment of myosin heavy chain, non-muscle type A), vinculin, a tropomyosin isoform, and the macrophage capping protein were increased. A shift in caldesmon isoforms was also detected. These results demonstrate an association between DN and the constitutive expression of cytoskeleton proteins in cultured skin fibroblasts from TlDM with DN, which may retain pathophysiologycal implications.},
  author       = {Millioni, R. and Lori, E. and Puricelli, L. and Arrigoni, Giorgio and Vedovato, M. and Trevisan, R. and James, Peter and Tiengo, A. and Tessari, P.},
  issn         = {1862-8354},
  keyword      = {IDDM PATIENTS,ACTIN POLYMERIZATION,ANTIPORT ACTIVITY,cytoskeletal proteins,PHENOTYPE,ASSIGNMENT,MICROALBUMINURIA,INSULIN,ERM PROTEINS,MESANGIAL CELLS,GENE-EXPRESSION,diabetic nephropathy,fibroblasts},
  language     = {eng},
  number       = {4},
  pages        = {492--503},
  publisher    = {John Wiley & Sons},
  series       = {Proteomics Clinical Applications},
  title        = {Abnormal cytoskeletal protein expression in cultured skin fibroblasts form type 1 diabetes mellitus patiens with nephropathy: A proteomic approach},
  url          = {http://dx.doi.org/10.1002/prca.200780112},
  volume       = {2},
  year         = {2008},
}