Molecular regulation of CPC-induced downregulation of tyrosinase activity in B16F10 murine melanoma cells

• Main Authors: Szu-Yen Yang, 楊思燕
• Other Authors: Li-Chen Wu
• Format: Others
• Language: zh-TW
• Published: 2007
• Online Access: http://ndltd.ncl.edu.tw/handle/20244058785166815432

碩士 === 國立暨南國際大學 === 生物醫學科技研究所 === 95 === The major function of melanogenesis is to prevent cells damage from the attack of UV light. Over-production of melanin may result in hyperpigmentation and melanoma. Tyrosinase is the key enzyme in melanogenesis. It catalyzes the rate-limiting redox reaction of melanogenesis. Consequently, the inhibition of tyrosinase activity or suppression of its expression may lead to reduce melanogenesis. c-Phycocyanin (CPC) is a water-soluble protein with characteristics of anti-oxidant and scavenging of free radicals. In the previous studies, the inhibitory mechanism of CPC on B16F10 melanogenesis was studied. The results indicated that CPC activated the activity of ERK and suppressed the activity of CREB, which led to diminished level of MITF. Moreover, suppression of PKC-beta I by CPC might cause lowered activity of tyrosinase, which further caused reduced level of melanogenesis. In addition, CPC engulfed into B16F10 through endocytosis and then transferred into nucleus was determined by confocal microscopic analysis.