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Article: Differential expression of integrin α5β1 in human abdominal aortic aneurysm and healthy aortic tissues and its significance in pathogenesis

TitleDifferential expression of integrin α5β1 in human abdominal aortic aneurysm and healthy aortic tissues and its significance in pathogenesis
Authors
Issue Date2004
PublisherElsevier Inc.. The Journal's web site is located at http://www.elsevier.com/locate/jsre
Citation
Journal Of Surgical Research, 2004, v. 118 n. 2, p. 176-182 How to Cite?
AbstractBackground Abdominal aortic aneurysm (AAA) is a common aged disease of human aorta with increasing incidence. It is characterized by dramatic vascular remodeling via proteolysis and degradation of matrix proteins. Integrins are important cellular receptors for matrix proteins, which may have an association with pathological remodeling. The present study was undertaken to analyze the expression of integrin subunits in human aneurysmal aortas and with healthy aortic tissues as controls. Materials and methods The expression of integrin genes in AAA specimens and healthy human aortic tissues was detected by RT-PCR technique. The correlation of variation and distribution of smooth muscle cells (SMCs) and integrin protein expression in the corresponding tissues were studied immunohistochemically. Results The gene transcripts coding for integrin α4, α5, αV, β1, β3, β5, and β6 subunits were constitutively expressed in the normal aortas. Only gene expressions of integrin α5 and β1 were significantly decreased by 81% and 85%, respectively, in AAA specimens (P < 0.005) when compared with healthy aortic specimens. No age dependence of the expression of integrin α5β1 genes was found. Significant reduction of medial SMC density was confirmed in corresponding AAA compared with control aortas. Immunoreactivity of integrin α5β1 receptor was found to be exclusively localized within the medial layer of the parallel normal aortic sections, whereas this protein was absent in the destructive media of aneurysmal aortic sections. Conclusions The marked decrease in integrin α5β1 expressions was unique to aneurysmal aortic tissues and correlated to a decrease in density of SMCs, which are the major cells in maintaining the structure stability of normal aortas. As integrin α5β1 specifically binds fibronectin and collagen, those results may suggest that the absence of integrin α5β1 activity impair matrix protein attachment and alter the architecture in aortic media thereby lead to the deformity of aorta and aneurysm formation. © 2004 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/169746
ISSN
2015 Impact Factor: 2.198
2015 SCImago Journal Rankings: 0.928
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCheuk, BLYen_US
dc.contributor.authorCheng, SWKen_US
dc.date.accessioned2012-10-25T04:54:49Z-
dc.date.available2012-10-25T04:54:49Z-
dc.date.issued2004en_US
dc.identifier.citationJournal Of Surgical Research, 2004, v. 118 n. 2, p. 176-182en_US
dc.identifier.issn0022-4804en_US
dc.identifier.urihttp://hdl.handle.net/10722/169746-
dc.description.abstractBackground Abdominal aortic aneurysm (AAA) is a common aged disease of human aorta with increasing incidence. It is characterized by dramatic vascular remodeling via proteolysis and degradation of matrix proteins. Integrins are important cellular receptors for matrix proteins, which may have an association with pathological remodeling. The present study was undertaken to analyze the expression of integrin subunits in human aneurysmal aortas and with healthy aortic tissues as controls. Materials and methods The expression of integrin genes in AAA specimens and healthy human aortic tissues was detected by RT-PCR technique. The correlation of variation and distribution of smooth muscle cells (SMCs) and integrin protein expression in the corresponding tissues were studied immunohistochemically. Results The gene transcripts coding for integrin α4, α5, αV, β1, β3, β5, and β6 subunits were constitutively expressed in the normal aortas. Only gene expressions of integrin α5 and β1 were significantly decreased by 81% and 85%, respectively, in AAA specimens (P < 0.005) when compared with healthy aortic specimens. No age dependence of the expression of integrin α5β1 genes was found. Significant reduction of medial SMC density was confirmed in corresponding AAA compared with control aortas. Immunoreactivity of integrin α5β1 receptor was found to be exclusively localized within the medial layer of the parallel normal aortic sections, whereas this protein was absent in the destructive media of aneurysmal aortic sections. Conclusions The marked decrease in integrin α5β1 expressions was unique to aneurysmal aortic tissues and correlated to a decrease in density of SMCs, which are the major cells in maintaining the structure stability of normal aortas. As integrin α5β1 specifically binds fibronectin and collagen, those results may suggest that the absence of integrin α5β1 activity impair matrix protein attachment and alter the architecture in aortic media thereby lead to the deformity of aorta and aneurysm formation. © 2004 Elsevier Inc. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier Inc.. The Journal's web site is located at http://www.elsevier.com/locate/jsreen_US
dc.relation.ispartofJournal of Surgical Researchen_US
dc.subject.meshAdulten_US
dc.subject.meshAgeden_US
dc.subject.meshAged, 80 And Overen_US
dc.subject.meshAorta - Metabolism - Physiologyen_US
dc.subject.meshAortic Aneurysm, Abdominal - Etiology - Metabolism - Physiopathologyen_US
dc.subject.meshExtracellular Matrix - Physiologyen_US
dc.subject.meshGene Expressionen_US
dc.subject.meshHumansen_US
dc.subject.meshImmunohistochemistryen_US
dc.subject.meshIntegrin Alpha5beta1 - Genetics - Metabolismen_US
dc.subject.meshMiddle Ageden_US
dc.subject.meshMuscle, Smooth, Vascular - Physiologyen_US
dc.subject.meshRna, Messenger - Analysisen_US
dc.titleDifferential expression of integrin α5β1 in human abdominal aortic aneurysm and healthy aortic tissues and its significance in pathogenesisen_US
dc.typeArticleen_US
dc.identifier.emailCheuk, BLY: bernice@hku.hken_US
dc.identifier.emailCheng, SWK: wkcheng@hkucc.hku.hken_US
dc.identifier.authorityCheuk, BLY=rp01671en_US
dc.identifier.authorityCheng, SWK=rp00374en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0022-4804(03)00351-2en_US
dc.identifier.pmid15100006-
dc.identifier.scopuseid_2-s2.0-12344338789en_US
dc.identifier.hkuros87625-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-12344338789&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume118en_US
dc.identifier.issue2en_US
dc.identifier.spage176en_US
dc.identifier.epage182en_US
dc.identifier.isiWOS:000221040400008-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridCheuk, BLY=7801343617en_US
dc.identifier.scopusauthoridCheng, SWK=7404684779en_US

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