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. 2024 Aug 7;35(11):687-691.
doi: 10.1097/WNR.0000000000002055. Epub 2024 May 30.

Tyrosinase deficiency impairs social novelty preference in mice

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Tyrosinase deficiency impairs social novelty preference in mice

Shu Aizawa et al. Neuroreport. .

Abstract

Objective: Tyrosinase is a rate-limiting enzyme for the biosynthesis of melanin pigment in peripheral tissues, such as skin and the retina. We recently reported the expression and enzymatic activity of tyrosinase as well as its protective effects against oxidative stress-induced protein damage in the mouse brain. The functional role of tyrosinase in the central nervous system, however, remains largely unknown. In the present study, we investigated the involvement of tyrosinase in social behavior in mice.

Methods: Pigmented C57BL/10JMsHir (B10) and tyrosinase-deficient albino B10.C- Tyr c /Hir (B10-c) mice were subjected to the three-chamber sociability test to assess sociability and social novelty preference. In addition, we measured the mRNA expression of genes involved in catecholamine metabolism in the hippocampus by real-time quantitative PCR analysis.

Results: The results obtained showed that tyrosinase deficiency impaired social novelty preference, but not sociability in mice. We also found that the hippocampal expression of genes involved in catecholamine metabolism, such as monoamine oxidase A and catechol-O-methyltransferase , were significantly decreased in tyrosinase-deficient B10-c mice.

Conclusion: These results suggest that tyrosinase activity is functionally involved in the phenotypic expression of social behavior, particularly social novelty preference, in mice. The present study will advance our understanding of the functional role of tyrosinase in the central nervous system.

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References

    1. Sánchez-Ferrer A, Rodríguez-López JN, García-Cánovas F, García-Carmona F. Tyrosinase: a comprehensive review of its mechanism. Biochim Biophys Acta 1995; 1247:1–11.
    1. Körner A, Pawelek J. Mammalian tyrosinase catalyzes three reactions in the biosynthesis of melanin. Science 1982; 217:1163–1165.
    1. Yokoyama T, Silversides DW, Waymire KG, Kwon BS, Takeuchi T, Overbeek PA. Conserved cysteine to serine mutation in tyrosinase is responsible for the classical albino mutation in laboratory mice. Nucleic Acids Res 1990; 18:7293–7298.
    1. Shibahara S, Okinaga S, Tomita Y, Takeda A, Yamamoto H, Sato M, et al. A point mutation in the tyrosinase gene of BALB/c albino mouse causing the cysteine----serine substitution at position 85. Eur J Biochem 1990; 189:455–461.
    1. Beermann F, Orlow SJ, Lamoreux ML. The Tyr (albino) locus of the laboratory mouse. Mamm Genome 2004; 15:749–758.

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