Activation of calpain-1 in human carotid artery atherosclerotic lesions

Autor: José Fernandes e Fernandes, Isabel Gonçalves, Luís Mendes Pedro, Mikko P.S. Ares, Nuno Dias, Isabella Pörn-Ares, Mihaela Nitulescu, Takaomi C. Saido
Rok vydání: 2008
Předmět:
Zdroj: BMC Cardiovascular Disorders
BMC Cardiovascular Disorders, Vol 9, Iss 1, p 26 (2009)
ISSN: 1471-2261
Popis: 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 α-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.
Databáze: OpenAIRE