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Altered chaperone and protein turnover regulators expression in cultured skin fibroblasts from type 1 diabetes mellitus with nephropathy

Tessari, P; Puricelli, L; Iori, E; Arrigoni, Giorgio LU ; Vedovato, M; James, Peter LU ; Coracina, C and Millioni, R (2007) In Journal of Proteome Research 6(3). p.976-986
Abstract
In type-1 diabetes mellitus (T1DM) with diabetic nephropathy (DN), accumulation of abnormal proteins in the kidney and other tissues may derive from constitutive alterations of intracellular protein recognition, assembly, and turnover. We characterized the proteins involved in these functions in cultured skin fibroblasts from long-term T1DM patients with [DN+] or without [DN-] nephropathy but similar metabolic control, and from matched healthy subjects. 2-D gel electrophoresis and MS-MALDI analysis were employed. The [DN+] T1DM patients, compared with the two other groups, exhibited increased abundance of a high-molecular weight isoform of protein disulphide-isomerase A3 and a decrease of two low-molecular weight isoforms. They also had... (More)
In type-1 diabetes mellitus (T1DM) with diabetic nephropathy (DN), accumulation of abnormal proteins in the kidney and other tissues may derive from constitutive alterations of intracellular protein recognition, assembly, and turnover. We characterized the proteins involved in these functions in cultured skin fibroblasts from long-term T1DM patients with [DN+] or without [DN-] nephropathy but similar metabolic control, and from matched healthy subjects. 2-D gel electrophoresis and MS-MALDI analysis were employed. The [DN+] T1DM patients, compared with the two other groups, exhibited increased abundance of a high-molecular weight isoform of protein disulphide-isomerase A3 and a decrease of two low-molecular weight isoforms. They also had increased levels of heat shock protein (HSP) 60 kDa isoform #A4, of HSP71 kDa isoform #A30, and of HSP27 kDa isoform #6, whereas the HSP27 kDa isoforms #A90 and #A71 were decreased. Cathepsin beta-2 (#40), the cation-independent mannose 6-phosphate receptor binding protein 1 (CIMPR) (#A27), and annexin 2 (#A9) were also decreased in the [DN+] T1DM patients, whereas the RNA-binding protein regulatory subunity (#38) and the translationally-controlled tumor protein (TCTP) (#A45) were increased. These changes of chaperone-like proteins in fibroblasts may highlight those of the kidney and be patho-physiologically related to the development of nephropathy in T1DM. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
proteomics, fibroblasts, diabetic nephropathy, protein folding, chaperones
in
Journal of Proteome Research
volume
6
issue
3
pages
976 - 986
publisher
The American Chemical Society
external identifiers
  • wos:000244638400006
  • scopus:33947574508
ISSN
1535-3893
DOI
10.1021/pr060443n
language
English
LU publication?
yes
id
d36100a1-1339-4bab-ab68-9834ccc585c0 (old id 600025)
date added to LUP
2008-01-10 16:05:51
date last changed
2017-04-16 03:28:55
@article{d36100a1-1339-4bab-ab68-9834ccc585c0,
  abstract     = {In type-1 diabetes mellitus (T1DM) with diabetic nephropathy (DN), accumulation of abnormal proteins in the kidney and other tissues may derive from constitutive alterations of intracellular protein recognition, assembly, and turnover. We characterized the proteins involved in these functions in cultured skin fibroblasts from long-term T1DM patients with [DN+] or without [DN-] nephropathy but similar metabolic control, and from matched healthy subjects. 2-D gel electrophoresis and MS-MALDI analysis were employed. The [DN+] T1DM patients, compared with the two other groups, exhibited increased abundance of a high-molecular weight isoform of protein disulphide-isomerase A3 and a decrease of two low-molecular weight isoforms. They also had increased levels of heat shock protein (HSP) 60 kDa isoform #A4, of HSP71 kDa isoform #A30, and of HSP27 kDa isoform #6, whereas the HSP27 kDa isoforms #A90 and #A71 were decreased. Cathepsin beta-2 (#40), the cation-independent mannose 6-phosphate receptor binding protein 1 (CIMPR) (#A27), and annexin 2 (#A9) were also decreased in the [DN+] T1DM patients, whereas the RNA-binding protein regulatory subunity (#38) and the translationally-controlled tumor protein (TCTP) (#A45) were increased. These changes of chaperone-like proteins in fibroblasts may highlight those of the kidney and be patho-physiologically related to the development of nephropathy in T1DM.},
  author       = {Tessari, P and Puricelli, L and Iori, E and Arrigoni, Giorgio and Vedovato, M and James, Peter and Coracina, C and Millioni, R},
  issn         = {1535-3893},
  keyword      = {proteomics,fibroblasts,diabetic nephropathy,protein folding,chaperones},
  language     = {eng},
  number       = {3},
  pages        = {976--986},
  publisher    = {The American Chemical Society},
  series       = {Journal of Proteome Research},
  title        = {Altered chaperone and protein turnover regulators expression in cultured skin fibroblasts from type 1 diabetes mellitus with nephropathy},
  url          = {http://dx.doi.org/10.1021/pr060443n},
  volume       = {6},
  year         = {2007},
}