title: The expression of Cox17p in rodent tissues and cells.
abstract: Previous works have reported the isolation of a novel polypeptide from porcine heart. Structural analysis has shown that it is a mammalian homologue of Cox17p, believed essential for the assembly of functional cytochrome c oxidase and delivery of copper ions to the mitochondrion for insertion into the enzyme in yeast. Although the human, mouse and porcine homologs of this small protein have already been cloned or purified, the function of Cox17p in the mammalian system has not yet been elucidated. To investigate the physiological function of Cox17p in mammals, we performed Northern blot analysis using probes containing the mouse and rat sequences obtained by RT-PCR. The hybridization signals were detected in all mouse tissues, but notably intense signals were observed in heart, brain and kidney RNA samples. Some of the neuroendocrine and endocrine cell lines showed higher expression levels than fibroblasts. The highest expression level of Cox17p mRNA in mouse brain was observed in the pituitary sample. While in rat heart, Cox17p mRNA expression was detected from early development, in rat brain, embryonic and postnatal changes in the expression were observed. Immunocytochemical analysis showed that Cox17p immunoreactivity was strong in the pituitary cell line, AtT-20. These findings suggested that Cox17p is not only part of the respiratory chain but also involved in brain and endocrine functions.
authors.affiliation: Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Kako
authors.forename: K
authors.initials: K
authors.lastname: Tsumori
authors.forename: Y
authors.initials: Y
authors.lastname: Ohmasa
authors.forename: Y
authors.initials: Y
authors.lastname: Takahashi
authors.forename: E
authors.initials: E
authors.lastname: Munekata
mesh_terms: D016475:3T3 Cells; D000375:Aging; D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology; D002352:Carrier Proteins; D027682:Cation Transport Proteins; D002460:Cell Line; D000079922:Copper Transport Proteins; D003576:Electron Transport Complex IV / Q000235:genetics*; D005314:Embryonic and Fetal Development; D018507:Gene Expression Regulation, Developmental; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D007668:Kidney / Q000201:enzymology; D007739:L Cells; D008297:Male; D051379:Mice; D008813:Mice, Inbred ICR; D018832:Molecular Chaperones; D008969:Molecular Sequence Data; D009206:Myocardium / Q000201:enzymology; D016716:PC12 Cells; D011506:Proteins / Q000235:genetics*; D051381:Rats; D017208:Rats, Wistar; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid; D013552:Swine; D014407:Tumor Cells, Cultured
chemical_list: C100359:COX17 protein, S cerevisiae; C491006:COX17 protein, human; D002352:Carrier Proteins; D027682:Cation Transport Proteins; D000079922:Copper Transport Proteins; C491005:Cox17 protein, mouse; C491004:Cox17 protein, rat; D018832:Molecular Chaperones; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins; D003576:Electron Transport Complex IV