Tyrosinase Inhibition Due to Interaction of Homocysteine with Copper: Mechanism for Reversible Hypopigmentation in Homocystinuria Due to Cystathionine Beta-Synthase Deficiency

July 1995 in “ PubMed ”

Orit Reish, Danyelle M. Townsend, Susan A. Berry, Michael Y. Tsai, Richard A. King

tyrosinase homocystinuria cystathionine beta-synthase deficiency hypopigmentation homocysteine copper sulfate L-cystine betaine

TLDR Lowering homocyst(e)ine levels can reverse skin and hair lightening by restoring enzyme activity needed for pigmentation.

The study explored the mechanism behind reversible hypopigmentation in patients with homocystinuria due to cystathionine beta-synthase deficiency. It was observed that two patients experienced darkening of their hypopigmented hair after treatment reduced plasma homocyst(e)ine levels. The researchers hypothesized that homocyst(e)ine inhibits tyrosinase, a key enzyme in pigmentation. Experiments showed that tyrosinase activity was reduced in cells exposed to homocysteine, but this inhibition was reversed by adding copper sulfate. The study concluded that the interaction of homocyst(e)ine with copper at the active site of tyrosinase likely caused the reversible hypopigmentation.

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research Tyrosinase Inhibition Due to Interaction of Homocysteine with Copper: Mechanism for Reversible Hypopigmentation in Homocystinuria Due to Cystathionine Beta-Synthase Deficiency

74 citations , July 1995 in “PubMed”

Lowering homocyst(e)ine levels can reverse skin and hair lightening by restoring enzyme activity needed for pigmentation.