Purification of hamster melanoma tyrosinases and structural studies of their asparagine-linked sugar chains☆
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2016, Journal of Photochemistry and Photobiology B: BiologyCitation Excerpt :For all assays the lysates were corrected by total protein concentration. The enzymatic activity of tyrosinase (EC:1.14.18.1) as DOPA oxidase was measured at 475 nm with an ELISA plate reader (Tecan) [30,33]. Mushroom tyrosinase (Sigma) was used as positive control.
Biphasic pro-melanogenic and pro-apoptotic effects of all-trans-retinoic acid (ATRA) on human melanocytes: Time-course study
2013, Journal of Dermatological ScienceCitation Excerpt :Protein concentrations were determined using the Bradford method according to the manufacturer's specifications and using bovine serum albumin as standard. Tyrosinase enzymatic activity (DOPA oxidase) was measured as described previously [13]. Briefly, 100 μL of each cell lysate were incubated with 1 mL DOPA (2.5 mg/mL prepared in 10 mM phosphate buffer, pH 7.2.)
Conformation-dependent post-translational glycosylation of tyrosinase: Requirement of a specific interaction involving the CuB metal binding site
2003, Journal of Biological ChemistryCitation Excerpt :Indeed, using several mutants where specific N-glycosylation sequons were abolished, it was shown that wild type Tyr expressed in Chinese hamster ovary cells bears four glycosylated and two unglycosylated sequons (16). Four occupied sequons were also found in hamster tyrosinase (44), and it has been shown for TYR that, when the rate of protein synthesis is high, a partially processed protein with an unoccupiedN-glycosylation site is present (17). However, it is also possible that the different heterologous cellular systems employed for transient expression of tyrosinase might yield a slightly different processing, and therefore, a higher degree ofN-glycosylation in our experimental system cannot be ruled out.
Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control
2000, Journal of Biological ChemistryCitation Excerpt :Expression in CHO cells of tyrosinase mutants lacking single N-glycosylation sites shows that sites 1, 4, 5, and 6 (at Asn residues 86, 230, 337, and 371) are fully occupied, whereas sites 2 and 3 (at Asn residues 111 and 161) are unoccupied. Although the exact locations have not been identified, four asparagine-linked oligosaccharides chains/molecule have been found on hamster tyrosinase (16), and both hamster (16) and mouse (17) tyrosinase show a similar range of oligomannosidic and sialilated complex antennary structures. These data, together with the observation that mouse and human tyrosinase have 85% sequence identity and identical potential N-glycosylation sites, indicate an interesting and possibly functionally relevant conservation ofN-glycosylation between tyrosinases from different mammalian species.
Inhibition of N-glycan processing in B16 melanoma cells results in inactivation of tyrosinase but does not prevent its transport to the melanosome
1997, Journal of Biological Chemistry
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This study was supported in part by a Grant-in-Aid for Cooperative Research and for Cancer Research of the Ministry of Education, Science, and Culture of Japan. This paper is a part of the dissertation submitted by T.O. to Kobe University School of Medicine for the degree requirement of Doctor of Medical Sciences.