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Melanocyte‐stimulating Properties of Secretory Phospholipase A 2
Author(s) -
Maeda Kazuhisa,
Naganuma Masako
Publication year - 1997
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1997.tb01890.x
Subject(s) - tyrosinase , melanin , phospholipase a2 , melanocyte , phospholipase , biochemistry , enzyme , chemistry , phospholipase c , phospholipase a , lipoxygenase , biology , microbiology and biotechnology , melanoma , genetics
— Phospholipase A 2 (PLA 2 ) catalyzes the release of free fatty acids from membrane phospholipids, and its products derived from these fatty acids, such as prostaglandins and leukotrienes, significantly up‐regulate the key mela‐nogenic enzyme, tyrosinase, in melanocytes. This has led to suggestions that PLA 2 itself triggers melanin synthesis in melanogenesis following UV irradiation or inflammation. We have examined the effect of secretory PLA 2 (sPLA 2 ) on melanogenesis in cultured human melanocytes. Secretory PLA 2 stimulated DNA synthesis and melanin synthesis, and these phenomena were completely inhibited by treatment with a phospholipase inhibitor, p‐ bromophenacyl bromide, demonstrating that the catalytic activity of sPLA 2 is required for melanogenesis. Secretory PLA 2 also stimulated tyrosinase activity, increased the amount of tyrosinase‐related protein‐1 and up‐regulated the expression of both mRNA. These findings suggest that sPLA 2 is an important mediator of UV‐induced or postinflammatory pigmentation.