A proteomic study of calpain-3 and its involvement in limb girdle muscular dystrophy type 2A.
Bertipaglia, I ; Richard, I ; Påhlman, Anna-Karin LU ; Andersson, Liselotte LU ; James, Peter LU
and Carafoli, E
(2009)
In Cell Calcium
46(5-6).
p.356-363
- Abstract
- Abstract in Undetermined
Limb-girdle muscular dystrophy type 2A is an autosomal recessive disorder generated by inactivating mutations in the gene coding for the muscle specific protease calpain-3. It is mainly expressed in skeletal muscle as a monomeric multidomain protein characterized by three unique insertion sequences (NS, IS1, IS2). It is unstable, and undergoes very rapid autolysis in solution, therefore, its heterologous expression and purification have been difficult. So far, calpain-3 substrates have been only identified in vitro and with indirect approaches. We have therefore decided to perform a comprehensive study of the substrates of the protease by comparing the 2D electrophoretic profile of myotubes from obtained from... (More) - Abstract in Undetermined
Limb-girdle muscular dystrophy type 2A is an autosomal recessive disorder generated by inactivating mutations in the gene coding for the muscle specific protease calpain-3. It is mainly expressed in skeletal muscle as a monomeric multidomain protein characterized by three unique insertion sequences (NS, IS1, IS2). It is unstable, and undergoes very rapid autolysis in solution, therefore, its heterologous expression and purification have been difficult. So far, calpain-3 substrates have been only identified in vitro and with indirect approaches. We have therefore decided to perform a comprehensive study of the substrates of the protease by comparing the 2D electrophoretic profile of myotubes from obtained from calpain-3 knockout and wild type mice. Digestion of differentially expressed spots was followed by mass spectrometry analysis. We could identify 16 proteins which differed in knockout and wild type mice. Among them: desmin, nestin, spectrin and PDLIM1 were of particular interest. In vitro experiments have then revealed that only PDLIM1 is cleaved directly by the protease, and that a fragment of about 8 kDa is released from the C-terminal portion of the protein. (C) 2009 Elsevier Ltd. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1394514
- author
- Bertipaglia, I
; Richard, I
; Påhlman, Anna-Karin
LU
; Andersson, Liselotte
LU
; James, Peter
LU
and Carafoli, E
- organization
- publishing date
- 2009
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Calpain, Muscular dystrophy, Proteomics, PDLIM 1
- in
- Cell Calcium
- volume
- 46
- issue
- 5-6
- pages
- 356 - 363
- publisher
- Elsevier
- external identifiers
-
- wos:000273411200006
- scopus:70649088773
- pmid:19926129
- ISSN
- 0143-4160
- DOI
- 10.1016/j.ceca.2009.10.003
- language
- English
- LU publication?
- yes
- id
- f08088b5-be87-4902-a15b-d81e5b35937e (old id 1394514)
- date added to LUP
- 2016-04-01 15:04:59
- date last changed
- 2023-09-03 23:21:54
@article{f08088b5-be87-4902-a15b-d81e5b35937e,
abstract = {{Abstract in Undetermined<br/>Limb-girdle muscular dystrophy type 2A is an autosomal recessive disorder generated by inactivating mutations in the gene coding for the muscle specific protease calpain-3. It is mainly expressed in skeletal muscle as a monomeric multidomain protein characterized by three unique insertion sequences (NS, IS1, IS2). It is unstable, and undergoes very rapid autolysis in solution, therefore, its heterologous expression and purification have been difficult. So far, calpain-3 substrates have been only identified in vitro and with indirect approaches. We have therefore decided to perform a comprehensive study of the substrates of the protease by comparing the 2D electrophoretic profile of myotubes from obtained from calpain-3 knockout and wild type mice. Digestion of differentially expressed spots was followed by mass spectrometry analysis. We could identify 16 proteins which differed in knockout and wild type mice. Among them: desmin, nestin, spectrin and PDLIM1 were of particular interest. In vitro experiments have then revealed that only PDLIM1 is cleaved directly by the protease, and that a fragment of about 8 kDa is released from the C-terminal portion of the protein. (C) 2009 Elsevier Ltd. All rights reserved.}},
author = {{Bertipaglia, I and Richard, I and Påhlman, Anna-Karin and Andersson, Liselotte and James, Peter and Carafoli, E}},
issn = {{0143-4160}},
keywords = {{Calpain; Muscular dystrophy; Proteomics; PDLIM 1}},
language = {{eng}},
number = {{5-6}},
pages = {{356--363}},
publisher = {{Elsevier}},
series = {{Cell Calcium}},
title = {{A proteomic study of calpain-3 and its involvement in limb girdle muscular dystrophy type 2A.}},
url = {{http://dx.doi.org/10.1016/j.ceca.2009.10.003}},
doi = {{10.1016/j.ceca.2009.10.003}},
volume = {{46}},
year = {{2009}},
}