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Diabetic cardiomyopathy is associated with increased risk of heart failure in type 1 diabetic patients. Mitochondrial dysfunction is suggested as an underlying contributor to diabetic cardiomyopathy. Cardiac mitochondria are characterized by subcellular spatial locale, including mitochondria located beneath the sarcolemma, subsarcolemmal mitochondria (SSM), and mitochondria situated between the myofibrils, interfibrillar mitochondria (IFM). The goal of this study was to determine whether type 1 diabetic insult in the heart influences proteomic make-up of spatially distinct mitochondrial subpopulations and to evaluate the role of nuclear encoded mitochondrial protein import. Utilizing multiple proteomic approaches (iTRAQ and two-dimensional-differential in-gel electrophoresis), IFM proteomic make-up was impacted by type 1 diabetes mellitus to a greater extent than SSM, as evidenced by decreased abundance of fatty acid oxidation and electron transport chain proteins. Mitochondrial phosphate carrier and adenine nucleotide translocator, as well as inner membrane translocases, were decreased in the diabetic IFM (P < 0.05 for both). Mitofilin, a protein involved in cristae morphology, was diminished in the diabetic IFM (P < 0.05). Posttranslational modifications, including oxidations and deamidations, were most prevalent in the diabetic IFM. Mitochondrial heat shock protein 70 (mtHsp70) was significantly decreased in diabetic IFM (P < 0.05). Mitochondrial protein import was decreased in the diabetic IFM with no change in the diabetic SSM (P < 0.05). Taken together, these results indicate that mitochondrial proteomic alterations in the type 1 diabetic heart are more pronounced in the IFM. Further, proteomic alterations are associated with nuclear encoded mitochondrial protein import dysfunction and loss of an essential mitochondrial protein import constituent, mtHsp70, implicating this process in the pathogenesis of the diabetic heart.
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http://dx.doi.org/10.1152/ajpregu.00423.2010 | DOI Listing |
Life Sci Alliance
December 2025
Department of Medicine, University of Wisconsin-Madison, Madison, WI, USA
Nε-lysine acetylation in the lumen of the ER requires two acetyltransferases, ATase1/NAT8B and ATase2/NAT8. They are type II membrane proteins and belong to the larger GNAT superfamily of acetyltransferases. Their enzymatic activity is tightly coupled to the import of acetyl-CoA in the lumen of the ER by AT-1/SLC33A1.
View Article and Find Full Text PDFJ Mol Biol
September 2025
University of South Alabama, Department of Physiology and Cell Biology, 5851 USA Dr. North, Mobile, AL 36688, USA. Electronic address:
In sexually reproducing eukaryotes-particularly mammals-mitochondrial DNA (mtDNA) is typically inherited from a single parent, making uniparental mtDNA inheritance a fundamental feature of eukaryotic biology. Recently, it has been suggested that spermatozoa contain no mtDNA because the matrix targeting sequence (MTS) of the mitochondrial transcription factor A (TFAM) becomes phosphorylated, which prevents the mitochondrial import of this protein essential for mtDNA replication. In this study, we used a combination of the GeneSwap technique and phosphomimetic mutations to investigate the impact of TFAM MTS phosphorylation on mtDNA maintenance in cultured cells.
View Article and Find Full Text PDFOncol Res
September 2025
Department of Thoracic Surgery, Xuanwu Hospital, Capital Medical University, Beijing, 100053, China.
Objectives: Lung cancer represents a major global healthcare challenge, characterized by high annual incidence and mortality rates worldwide. Although targeted therapies for lung cancer have advanced, treatment outcomes for advanced-stage patients remain suboptimal. This investigation examines the role of the translocase of the inner mitochondrial membrane (TIMM)8A-TIMM13 complex in lung cancer and evaluates its potential as a novel therapeutic target.
View Article and Find Full Text PDFACS Omega
September 2025
Department of Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701, United States.
Ipomoeassin F (Ipom-F) is a natural compound that exhibits a potent cytotoxic effect on triple-negative breast cancer (TNBC) cells. The mechanism underlying this selective potency remains unclear. To elucidate this mechanism, we analyzed the proteome profiles of the TNBC MDA-MB-231 cells after exposure to Ipom-F at different time points and increasing doses using a quantitative proteomic method.
View Article and Find Full Text PDFBiochim Biophys Acta Mol Cell Res
September 2025
University of Warsaw, Faculty of Biology, Institute of Experimental Plant Biology and Biotechnology, Department of Plant Metal Homeostasis, 1 Miecznikowa Str., 02-096, Warszawa, Poland. Electronic address:
The Natural Resistance Associated Macrophage Proteins (NRAMPs) are membrane-targeted transporters with low substrate specificity, that mediate the import (translocation to the cytoplasm) of metals, mainly essential nutrients, e.g. iron (Fe), manganese (Mn), zinc (Zn), cobalt (Co), copper (Cu) or nickel (Ni).
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