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Kinetin is Sufficient to Accelerate Mitophagy Flux in H9c2 Cardiac Myoblast Cells
Author(s) -
Nagaria Omar,
Singh Suprit,
Kabir Rizowana,
Kobayashi Satoru,
Kobayashi Tamayo,
Liang Qiangrong
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.833.8
Subject(s) - mitophagy , microbiology and biotechnology , autophagy , mitochondrion , biology , apoptosis , biochemistry
The lysosomal degradation of dysfunctional mitochondria is vital for cellular health. Although widely known for their role in oxidative phosphorylation, mitochondria also generate reactive oxygen species (ROS) that are cytotoxic. Mitochondria themselves are susceptible to ROS damage, which can render them dysfunctional and eventually lead to various modes of cell death. Therefore, to maintain a healthy population of mitochondria, it is crucial for cells to eliminate injured mitochondria through the autophagy‐lysosomal pathway, a process termed mitophagy. Previous studies have identified Kinetin (KTN) as an activator of PTEN‐induced kinase (PINK‐1), a mitochondrial kinase that is activated in response to mitochondrial damage and orchestrates downstream mitophagy processes. While KTN has been shown to induce mitophagy in human‐derived neural cells, its role in cardiomyocytes remains unknown. In the present study, we tested the ability of KTN to induce mitophagy in H9c2 cardiac myoblast cells. The cells were treated with KTN, and a subset of cells was additionally treated with lysosomal protease inhibitors: pepstatin A (pepA) and E64d. Mitochondrial fractions were isolated and the expression levels of LC3‐II (Microtubule‐associated protein 1A/1B‐light chain 3), an established marker of autophagic vesicles, were analyzed using Western blotting. Our results showed that pepA/ E64d treatment led to a much larger increase in LC3‐II levels among KTN‐treated cells relative to the vehicle‐treated cells, suggesting that KTN was sufficient to accelerate mitophagy flux in cardiomyocytes. This result was confirmed by a novel dual fluorescent mitophagy reporter. Our lab is currently investigating whether KTN can protect cardiomyocytes against stress‐induced cellular injury through upregulation of mitophagy. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .