Defective Intercellular Adhesion Complex in Myocardium Predisposes to Infarct Rupture in Humans

Borne, Susanne W.M. van den; Narula, Jagat; Voncken, Jan Willem; Lijnen, Peter; Vervoort-Peters, H.T.M.; Dahlmans, V.E.H.; Smits, J. F. M.; Daemen, Mat J.A.P.; Blankesteijn, W. Matthijs

doi:10.1016/j.jacc.2008.02.056

Cited by 28 publications

(12 citation statements)

References 24 publications

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“…The relatively late onset of cardiomyopathy (>8 months of age) suggests αT-catenin may compensate, at least to some degree, for loss of αE-catenin. In another study, significant mortality was observed in αE-catenin heterozygous null mice post-MI (van den Borne et al, 2008). …”

Section: α-Catenin Function In the Heartmentioning

confidence: 97%

N-Cadherin/Catenin Complex as a Master Regulator of Intercalated Disc Function

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Radice

2014

Cell Communication & Adhesion

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Intercellular adhesive junctions are essential for maintaining the physical integrity of tissues; this is particularly true for the heart that is under constant mechanical load. The correct functionality of the heart is dependent on the electrical and mechanical coordination of its constituent cardiomyocytes. The intercalated disc (ID) structure located at the termini of the rod shaped adult cardiomyocyte contains various junctional proteins responsible for the integration of structural information and cell-cell communication. According to the classical description, the ID consists of three distinct junctional complexes: adherens junction (AJ), desmosome (Des), and gap junction (GJ) that work together to mediate mechanical and electrical coupling of cardiomyocytes. However, recent morphological and molecular studies indicate that AJ and Des components are capable of mixing together resulting in a ‘hybrid adhering junction’ or ‘area composita’. This review summarizes recent progress in understanding the in vivo function(s) of AJ components in cardiac homeostasis and disease.

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Section: α-Catenin Function In the Heartmentioning

confidence: 97%

N-Cadherin/Catenin Complex as a Master Regulator of Intercalated Disc Function

Vite

Radice

2014

Cell Communication & Adhesion

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“…In fact ICAM-1 knock-out mice do not develop inflammation and have less inflammatory cell infiltration [20,21]. Mutations of ICAM-1 are associated with different diseases as infarct, biliary atresia, multiple sclerosis, obesity [21][22][23][24]. When the sICAM-1 levels are compared to sHLA-G, a soluble molecule involved in embryo implantation [3], sICAM-1 showed higher levels in oocyte supernatants than sHLA-G.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional Proling Reveals Barcode-Like Toxicogenomic Responses in the Zebrash Embryo

2011

Current Research in Embryology

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Background: During the last years, several studies have reported the significant relationship between the production of soluble HLA-G molecules (sHLA-G) by 48-72 hours early embryos and an increased implantation rate in IVF protocols. As consequence, the detection of HLA-G modulation was suggested as a marker to identify the best embryos to be transferred. On the opposite, no suitable markers are available for the oocyte selection.

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“…However, vinculin, a binding partner of αE-catenin, was decreased in the αE-catenin CKO heart. Another group reported significant mortality in αE-catenin heterozygous null mice following myocardial infarction (van den Borne et al, 2008) further supporting the importance of αE-catenin following ischemic injury.…”

Section: α-Catenins and Mechanical Coupling In The Heartmentioning

confidence: 91%

“…In another study, αE-catenin was reported to be preferentially downregulated in both the remote and infarct area of human hearts (van den Borne et al, 2008). Interestingly, inactivation of α-catenins in mice subjected to myocardial infarction induced cardiomyocyte regeneration and improved heart function (Li et al, 2014).…”

Section: α-Catenins and Cardiac Regenerationmentioning

confidence: 99%

New functions for alpha-catenins in health and disease: from cancer to heart regeneration

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Radice

2015

Cell Tissue Res

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Strong cell-cell adhesion mediated by adherens junctions is dependent on anchoring the transmembrane cadherin molecule to the underlying actin cytoskeleton. To do this, cadherin cytoplasmic domain interacts with catenin proteins, which include α-catenin that binds directly to filamentous actin. Originally thought to be a static structure, the connection between the cadherin/catenin adhesion complex and the actin cytoskeleton is now considered to be dynamic and responsive to both intercellular and intracellular signals. Alpha-catenins are mechanosensing proteins that undergo conformational change in response to cytoskeletal tension thus modifying the linkage between the cadherin and the actin cytoskeleton. There are three α-catenin isoforms expressed in mouse and human: αE-catenin (CTNNA1), αN-catenin (CTNNA2), and αT-catenin (CTNNA3). This review summarizes recent progress in understanding the in vivo function(s) of α-catenins in tissue morphogenesis, homeostasis, and disease. The role of α-catenin in the regulation of cellular proliferation will be discussed in the context of cancer and regeneration.

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Defective Intercellular Adhesion Complex in Myocardium Predisposes to Infarct Rupture in Humans

Abstract: The data show a reduced expression and defective localization of alphaE-catenin in the intercalated disc region in patients dying of infarct rupture. The mechanism of lower expression of alphaE-catenin remains to be elucidated.

Cited by 28 publications

References 24 publications

N-Cadherin/Catenin Complex as a Master Regulator of Intercalated Disc Function

N-Cadherin/Catenin Complex as a Master Regulator of Intercalated Disc Function

Transcriptional Proling Reveals Barcode-Like Toxicogenomic Responses in the Zebrash Embryo

New functions for alpha-catenins in health and disease: from cancer to heart regeneration

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