Remote ischemic preconditioning prevents sarcolemmal-associated proteolysis by MMP-2 inhibition.

Autor: Bin EP; Universidad de Buenos Aires, Facultad de Ciencias Médicas, Instituto de Fisiopatología Cardiovascular, 950 J. E. Uriburu, 2nd floor, C1114AAD, Buenos Aires, Argentina.; Universidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina., Zaobornyj T; Universidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina.; Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Departamento de Físico-Química, Buenos Aires, Argentina., Garces M; Universidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina., D'Annunzio V; Universidad de Buenos Aires, Facultad de Ciencias Médicas, Instituto de Fisiopatología Cardiovascular, 950 J. E. Uriburu, 2nd floor, C1114AAD, Buenos Aires, Argentina.; Universidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina., Buchholz B; Universidad de Buenos Aires, Facultad de Ciencias Médicas, Instituto de Fisiopatología Cardiovascular, 950 J. E. Uriburu, 2nd floor, C1114AAD, Buenos Aires, Argentina.; Universidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina., Marchini T; Universidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina., Evelson P; Universidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina., Gelpi RJ; Universidad de Buenos Aires, Facultad de Ciencias Médicas, Instituto de Fisiopatología Cardiovascular, 950 J. E. Uriburu, 2nd floor, C1114AAD, Buenos Aires, Argentina.; Universidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina., Donato M; Universidad de Buenos Aires, Facultad de Ciencias Médicas, Instituto de Fisiopatología Cardiovascular, 950 J. E. Uriburu, 2nd floor, C1114AAD, Buenos Aires, Argentina. mdonato@fmed.uba.ar.; Universidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina. mdonato@fmed.uba.ar.
Jazyk: angličtina
Zdroj: Molecular and cellular biochemistry [Mol Cell Biochem] 2024 Sep; Vol. 479 (9), pp. 2351-2363. Date of Electronic Publication: 2023 Sep 20.
DOI: 10.1007/s11010-023-04849-2
Abstrakt: The death of myocytes occurs through different pathways, but the rupture of the plasma membrane is the key point in the transition from reversible to irreversible injury. In the myocytes, three major groups of structural proteins that link the extracellular and intracellular milieus and confer structural stability to the cell membrane: the dystrophin-associated protein complex, the vinculin-integrin link, and the spectrin-based submembranous cytoskeleton. The objective was to determine if remote ischemic preconditioning (rIPC) preserves membrane-associated cytoskeletal proteins (dystrophin and β-dystroglycan) through the inhibition of metalloproteinase type 2 (MMP-2) activity. A second objective was to describe some of the intracellular signals of the rIPC, that modify mitochondrial function at the early reperfusion. Isolated rat hearts were subjected to 30 min of global ischemia and 120 min of reperfusion (I/R). rIPC was performed by 3 cycles of ischemia/reperfusion in the lower limb (rIPC). rIPC significantly decreased the infarct size, induced Akt/GSK-3 β phosphorylation and inhibition of the MPTP opening. rIPC improved mitochondrial function, increasing membrane potential, ATP production and respiratory control. I/R increased ONOO - production, which activates MMP-2. This enzyme degrades β-dystroglycan and dystrophin and collaborates to sarcolemmal disruption. rIPC attenuates the breakdown of β-dystroglycan and dystrophin through the inhibition of MMP-2 activity. Furthermore, we confirm that rIPC activates different intracellular pathway that involves the an Akt/Gsk3β and MPTP pore with preservation of mitochondrial function.
(© 2023. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
Databáze: MEDLINE
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