• Korean Journal of Food Science and Technology
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• v.44 no.6
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• pp.653-657
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• 2012

While it is known that sulfur containing amino acids (SCAA) are very important in regulating hepatocyte growth and preventing liver-diseases, the fundamental molecular mechanisms of how they exert their hepatoprotective functions are not well known. Since it is widely understood that the hepatic concentrations of S-adenosylmethionine (SAMe) in chronic liver disease patients are severely decreased, the pathophysiological importance of SAMe and its downstream antioxidant, glutathione should be discussed in order to see a big picture of relationship between SCAA and liver diseases. Chronic SAMe deficient mice have shown spontaneous hepatocellular carcinoma development due to impaired mitochondria functions with low levels of prohibitin1 protein, and through deficiency in many genes which are known to ameliorate genetic instability, such as APEX1 and DUSP1, the functions of which are recovered by SAMe treatment. In this review, current knowledge of the basic concepts of the mechanisms through which SCAAs protect the liver will be discussed in detail. Also, a possible tumor suppressor in livers, prohibitin1, and its functional relationship with SAMe will be discussed.

• Journal of Life Science
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• v.34 no.10
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• pp.723-729
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• 2024

Kinesin superfamily protein 5A (KIF5A) is the motor protein of kinesin-1 and forms a heterotetrameric complex by binding to KIF5B or KIF5C and kinesin light chains (KLCs), a non-motor protein. Amyotrophic lateral sclerosis (ALS)-associated KIF5A single nucleotide variants are clustered in the near exon 27 and are predicted to have a change in the carboxy (C)-terminal region of KIF5A. In patients with ALS, mitochondria membrane protein prohibitin 1 (Phb1) and Phb2 were found downregulated in the spinal cord. In this study, we confirmed that Phb2 binds to KIF5A. Phb2 bounds to the C-terminal region of KIF5A, which is the KIF5A-specific terminus, and KIF5A bounds to the C-terminal region of Phb2 but not to Phb1 in a two-hybrid assay. In human embryonic kidney-293T cells co-expressing EGFP-Phb2 and myc-KIF5A plasmids, Phb2 was co-immunoprecipitated with the motor proteins of kinesin-1, KIF5A and KIF5B, and the non-motor protein KLC1. In addition, both EGFP-Phb2 and myc-KIF5A were expressed at the same location in the cell. These results suggest that the binding of KIF5A to phb2 plays a role in mediating the association of kinesin-1 with mitochondria.