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Activation of calpain-1 in human carotid artery atherosclerotic lesions

Goncalves, Isabel LU orcid ; Nitulescu, Mihaela LU ; Saido, Takaomi C. ; Dias, Nuno LU orcid ; Pedro, Luis M. ; Fernandes e Fernandes, Jose ; Ares, Mikko LU and Ares, Isabella LU (2009) In BMC Cardiovascular Disorders 9(26).
Abstract
Background: In a previous study, we observed that oxidized low-density lipoprotein-induced death of endothelial cells was calpain-1-dependent. The purpose of the present paper was to study the possible activation of calpain in human carotid plaques, and to compare calpain activity in the plaques from symptomatic patients with those obtained from patients without symptoms. Methods: Human atherosclerotic carotid plaques (n = 29, 12 associated with symptoms) were removed by endarterectomy. Calpain activity and apoptosis were detected by performing immunohistochemical analysis and TUNEL assay on human carotid plaque sections. An antibody specific for calpain-proteolyzed alpha-fodrin was used on western blots. Results: We found that calpain was... (More)
Background: In a previous study, we observed that oxidized low-density lipoprotein-induced death of endothelial cells was calpain-1-dependent. The purpose of the present paper was to study the possible activation of calpain in human carotid plaques, and to compare calpain activity in the plaques from symptomatic patients with those obtained from patients without symptoms. Methods: Human atherosclerotic carotid plaques (n = 29, 12 associated with symptoms) were removed by endarterectomy. Calpain activity and apoptosis were detected by performing immunohistochemical analysis and TUNEL assay on human carotid plaque sections. An antibody specific for calpain-proteolyzed alpha-fodrin was used on western blots. Results: We found that calpain was activated in all the plaques and calpain activity colocalized with apoptotic cell death. Our observation of autoproteolytic cleavage of the 80 kDa subunit of calpain-1 provided further evidence for enzyme activity in the plaque samples. When calpain activity was quantified, we found that plaques from symptomatic patients displayed significantly lower calpain activity compared with asymptomatic plaques. Conclusion: These novel results suggest that calpain-1 is commonly active in carotid artery atherosclerotic plaques, and that calpain activity is colocalized with cell death and inversely associated with symptoms. (Less)
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author
; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
BMC Cardiovascular Disorders
volume
9
issue
26
publisher
BioMed Central (BMC)
external identifiers
  • wos:000267829600001
  • scopus:67651053140
  • pmid:19538725
ISSN
1471-2261
DOI
10.1186/1471-2261-9-26
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Pathology (013031100), Emergency medicine/Medicine/Surgery (013240200), Experimental Cardiovascular Research Unit (013242110)
id
deebbc7d-884a-4473-831c-0376e64efd9e (old id 1462817)
date added to LUP
2016-04-01 13:43:16
date last changed
2021-03-24 05:50:44
@article{deebbc7d-884a-4473-831c-0376e64efd9e,
  abstract     = {Background: In a previous study, we observed that oxidized low-density lipoprotein-induced death of endothelial cells was calpain-1-dependent. The purpose of the present paper was to study the possible activation of calpain in human carotid plaques, and to compare calpain activity in the plaques from symptomatic patients with those obtained from patients without symptoms. Methods: Human atherosclerotic carotid plaques (n = 29, 12 associated with symptoms) were removed by endarterectomy. Calpain activity and apoptosis were detected by performing immunohistochemical analysis and TUNEL assay on human carotid plaque sections. An antibody specific for calpain-proteolyzed alpha-fodrin was used on western blots. Results: We found that calpain was activated in all the plaques and calpain activity colocalized with apoptotic cell death. Our observation of autoproteolytic cleavage of the 80 kDa subunit of calpain-1 provided further evidence for enzyme activity in the plaque samples. When calpain activity was quantified, we found that plaques from symptomatic patients displayed significantly lower calpain activity compared with asymptomatic plaques. Conclusion: These novel results suggest that calpain-1 is commonly active in carotid artery atherosclerotic plaques, and that calpain activity is colocalized with cell death and inversely associated with symptoms.},
  author       = {Goncalves, Isabel and Nitulescu, Mihaela and Saido, Takaomi C. and Dias, Nuno and Pedro, Luis M. and Fernandes e Fernandes, Jose and Ares, Mikko and Ares, Isabella},
  issn         = {1471-2261},
  language     = {eng},
  number       = {26},
  publisher    = {BioMed Central (BMC)},
  series       = {BMC Cardiovascular Disorders},
  title        = {Activation of calpain-1 in human carotid artery atherosclerotic lesions},
  url          = {http://dx.doi.org/10.1186/1471-2261-9-26},
  doi          = {10.1186/1471-2261-9-26},
  volume       = {9},
  year         = {2009},
}