2002
DOI: 10.2108/zsj.19.275
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Biochemical and Immunohistochemical Studies on Tropomyosin and Glutamate Dehydrogenase in the Chicken Liver

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Cited by 10 publications
(5 citation statements)
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“…Similarly, in this study, Sc-GDH protein distributions altered after ammonia stress, which were mostly expressed in the cytoplasm endothelial cells of hepatocytes. Identical conclusions were found in the livers of chicken and mouse (Akutsu and Miyazaki, 2002;Vázquez-Martínez et al, 2017). Collectively, these findings indicate that Sc-GDH in the hepatopancreas of razor clam plays a key role in response to external ammonia entering the bodies.…”
Section: Discussionsupporting
confidence: 70%
“…Similarly, in this study, Sc-GDH protein distributions altered after ammonia stress, which were mostly expressed in the cytoplasm endothelial cells of hepatocytes. Identical conclusions were found in the livers of chicken and mouse (Akutsu and Miyazaki, 2002;Vázquez-Martínez et al, 2017). Collectively, these findings indicate that Sc-GDH in the hepatopancreas of razor clam plays a key role in response to external ammonia entering the bodies.…”
Section: Discussionsupporting
confidence: 70%
“…Several metabolic enzymes identified here have already been known to associate with actin fibers: glutamate dehydrogenase [33], glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [34], pyruvate kinase [35], and enolase [36].…”
Section: Cytosolic Skeleton Fractionmentioning
confidence: 90%
“…The majority of the proteins that were not previously implicated to associate with the skeleton were metabolic enzymes (Table 1A): phosphoglycerate mutase (glycolysis), transketolase, phosphogluconate dehydrogenase (pentose phosphate pathway), n-acetylglucosamine kinase (glutamate and aminosugar metabolism), glucosidase (glycoprotein processing), and aldehyde dehydrogenase (oxidation of aldehydes). Several metabolic enzymes identified here have already been known to associate with actin fibers: glutamate dehydrogenase [33], glyceraldehyde-3-phosphate dehydrogenase (GAPDH) [34], pyruvate kinase [35], and enolase [36].…”
Section: Cytosolic Skeleton Fractionmentioning
confidence: 90%
“…In muscle cells, Tm interacts with troponin T, caldesmon, and tropomodulin as part of the contractile apparatus (Perry, 2001). In non‐muscle cells, various Tm isoforms bind to calponin (Takahashi et al , 1986), pEL98 (Takenaga et al , 1994), and glutamic dehydrogenase (Akutsu and Miyazaki, 2002) although the physiological significance of these interactions is largely unknown. By linking Tm directly to RhoA signalling, we establish a new paradigm in which structurally unrelated actin‐binding proteins such as Tm and synaptopodin not only serve as passive structural components of actin filaments, but also can actively regulate stress fibre dynamics (Figure 7E).…”
Section: Discussionmentioning
confidence: 99%