Aquaporin 8 Regulates Mitochondrial Glycogen Phosphorylase Expression in C57BL6 Mice | ||||
Suez Canal Veterinary Medical Journal. SCVMJ | ||||
Article 3, Volume 23, Issue 1, June 2018, Page 27-39 PDF (833.06 K) | ||||
Document Type: Original Article | ||||
DOI: 10.21608/scvmj.2018.60750 | ||||
View on SCiNiTO | ||||
Authors | ||||
S. Magdeldin1; Masaaki Nameta2; Tadashi Yamamoto2 | ||||
11Department of Physiology, Faculty of Veterinary Medicine, Suez Canal University, Ismailia 41522, Egypt. | ||||
2Biofluid Biomarker Center, Institute of Social innovation and Co-operation, Niigata University, Niigata 951-2181, Japan; | ||||
Abstract | ||||
Aquaporins (AQPs) are group of membranous water channel proteins that regulates water and small molecule movements through cell membrane. Among this group, aquaporin 8 which express in high abundance in colon, liver and kidneys. With the generation of aquaporin 8 knockout model, C57BL6 mice hepatic tissues were fractionated to purify mitochondrial fractions in both wild and AQP8 knockout model. Tandem mass spectrometric analysis revealed a significant downregulation of glycogen phosphorylase in AQP8 knockout mice. This finding was supported by western blotting. Immune-gold electron microscopy showed mitochondrial cisternae localization of glycogen phosphorylase in higher abundance than in knockout model. Present findings suggest a novel strong association between aquaporin 8 and mitochondrial glycogen phosphorylase which pinpoints indirect involvement of AQP8 in glycogen metabolism. | ||||
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