Activation of calpain-1 in human carotid artery atherosclerotic lesions
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1462817
- author
- Goncalves, Isabel LU ; Nitulescu, Mihaela LU ; Saido, Takaomi C. ; Dias, Nuno LU ; Pedro, Luis M. ; Fernandes e Fernandes, Jose ; Ares, Mikko LU and Ares, Isabella LU
- organization
- publishing date
- 2009
- 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
- 2022-02-07 11:25:45
@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}}, }