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. 1998 Aug;7(4):198-204.
doi: 10.1111/j.1600-0625.1998.tb00324.x.

Human Tyrosinase Related protein-1 (TRP-1) Does Not Function as a DHICA Oxidase Activity in Contrast to Murine TRP-1

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Human Tyrosinase Related protein-1 (TRP-1) Does Not Function as a DHICA Oxidase Activity in Contrast to Murine TRP-1

R E Boissy et al. Exp Dermatol. .

Abstract

Tyrosinase related protein-1 is a melanocyte specific protein and a member of the tyrosinase gene family which also includes tyrosinase and TRP 2 (DOPAchrome tautomerase). In murine melanocytes, TRP-1 functions as a 5,6-dihydroxyindole-2-carboxylic acid [DHICA] oxidase during the biosynthetic conversion of tyrosine to eumelanin and mutations affecting TRP-1 result in the synthesis of brown rather than black pelage coloration. In this study, we examined the putative DHICA oxidase activity of TRP-1 in human melanocytes using several approaches. We first utilized a line of cultured melanocytes established from a patient with a form of oculocutaneous albinism completely lacking expression of TRP-1 (OCA3). This line of melanocytes endogenously exhibited the same amount of DHICA oxidase activity as control melanocytes expressing TRP-1. In other experiments, cultured human fibroblasts were transfected with a cDNA for TRP-1, in either the sense or antisense direction, or with the retroviral vector alone. TRP-1 expression was induced in fibroblasts transfected with the TRP-1 cDNA in the sense direction only. Although TRP-1 was expressed by sense-transfected cells, there was no significant DHICA oxidase activity above controls. These results demonstrate that human TRP-1 does not use DHICA as a substrate for oxidation.

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