Cardioprotective kinase signaling to subsarcolemmal and interfibrillar mitochondria is mediated by caveolar structures View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2017-02-03

AUTHORS

Wylly Ramsés García-Niño, Francisco Correa, Julia Isabel Rodríguez-Barrena, Juan Carlos León-Contreras, Mabel Buelna-Chontal, Elizabeth Soria-Castro, Rogelio Hernández-Pando, José Pedraza-Chaverri, Cecilia Zazueta

ABSTRACT

The demonstration that caveolin-3 overexpression reduces myocardial ischemia/reperfusion injury and our own finding that multiprotein signaling complexes increase in mitochondria in association with caveolin-3 levels, led us to investigate the contribution of caveolae-driven extracellular signal-regulated kinases 1/2 (ERK1/2) on maintaining the function of cardiac mitochondrial subpopulations from reperfused hearts subjected to postconditioning (PostC). Rat hearts were isolated and subjected to ischemia/reperfusion and to PostC. Enhanced cardiac function, reduced infarct size and preserved ultrastructure of cardiomyocytes were associated with increased formation of caveolar structures, augmented levels of caveolin-3 and mitochondrial ERK1/2 activation in PostC hearts in both subsarcolemmal (SSM) and interfibrillar (IFM) subpopulations. Disruption of caveolae with methyl-β-cyclodextrin abolished cardioprotection in PostC hearts and diminished pho-ERK1/2 gold-labeling in both mitochondrial subpopulations in correlation with suppression of resistance to permeability transition pore opening. Also, differences between the mitochondrial subpopulations in the setting of PostC were evaluated. Caveolae disruption with methyl-β-cyclodextrin abolished the cardioprotective effect of postconditioning by inhibiting the interaction of ERK1/2 with mitochondria and promoted decline in mitochondrial function. SSM, which are particularly sensitive to reperfusion damage, take advantage of their location in cardiomyocyte boundary and benefit from the cardioprotective signaling driven by caveolae, avoiding injury propagation. More... »

PAGES

15

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00395-017-0607-4

DOI

http://dx.doi.org/10.1007/s00395-017-0607-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1083535017

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28160133


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27 schema:description The demonstration that caveolin-3 overexpression reduces myocardial ischemia/reperfusion injury and our own finding that multiprotein signaling complexes increase in mitochondria in association with caveolin-3 levels, led us to investigate the contribution of caveolae-driven extracellular signal-regulated kinases 1/2 (ERK1/2) on maintaining the function of cardiac mitochondrial subpopulations from reperfused hearts subjected to postconditioning (PostC). Rat hearts were isolated and subjected to ischemia/reperfusion and to PostC. Enhanced cardiac function, reduced infarct size and preserved ultrastructure of cardiomyocytes were associated with increased formation of caveolar structures, augmented levels of caveolin-3 and mitochondrial ERK1/2 activation in PostC hearts in both subsarcolemmal (SSM) and interfibrillar (IFM) subpopulations. Disruption of caveolae with methyl-β-cyclodextrin abolished cardioprotection in PostC hearts and diminished pho-ERK1/2 gold-labeling in both mitochondrial subpopulations in correlation with suppression of resistance to permeability transition pore opening. Also, differences between the mitochondrial subpopulations in the setting of PostC were evaluated. Caveolae disruption with methyl-β-cyclodextrin abolished the cardioprotective effect of postconditioning by inhibiting the interaction of ERK1/2 with mitochondria and promoted decline in mitochondrial function. SSM, which are particularly sensitive to reperfusion damage, take advantage of their location in cardiomyocyte boundary and benefit from the cardioprotective signaling driven by caveolae, avoiding injury propagation.
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35 ERK1/2 activation
36 PostC
37 PostC hearts
38 SSM
39 activation
40 advantages
41 association
42 benefits
43 boundaries
44 cardiac function
45 cardiac mitochondrial subpopulations
46 cardiomyocyte boundary
47 cardiomyocytes
48 cardioprotection
49 cardioprotective effects
50 cardioprotective kinase
51 cardioprotective signaling
52 caveolae
53 caveolae disruption
54 caveolar structures
55 caveolin-3
56 caveolin-3 levels
57 caveolin-3 overexpression
58 complexes
59 contribution
60 contribution of caveolae
61 correlation
62 cyclodextrin
63 damage
64 decline
65 demonstration
66 differences
67 disruption
68 disruption of caveolae
69 effect
70 extracellular signal-regulated kinases 1/2
71 findings
72 formation
73 function
74 heart
75 infarct size
76 injury
77 injury propagation
78 interaction
79 interaction of ERK1/2
80 interfibrillar (IFM) subpopulations
81 interfibrillar mitochondria
82 ischemia/reperfusion
83 ischemia/reperfusion injury
84 kinase
85 kinase 1/2
86 levels
87 levels of caveolin-3
88 location
89 methyl
90 mitochondria
91 mitochondrial ERK1/2 activation
92 mitochondrial function
93 mitochondrial subpopulations
94 multiprotein
95 myocardial ischemia/reperfusion injury
96 opening
97 overexpression
98 own findings
99 permeability transition pore opening
100 pore opening
101 propagation
102 rat heart
103 reperfusion
104 reperfusion damage
105 reperfusion injury
106 resistance
107 setting
108 setting of PostC
109 signal-regulated kinases 1/2
110 signaling
111 size
112 structure
113 subpopulations
114 suppression
115 suppression of resistance
116 transition pore opening
117 ultrastructure
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