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Melanocytic galectin-3 is associated with tyrosinase-related protein-1 and pigment biosynthesis.

Authors
  • Chalupa, Allison1
  • Koshoffer, Amy1
  • Galan, Emily1
  • Yu, Lan2
  • Liu, Fu-Tong2
  • Boissy, Raymond E3
  • 1 Department of Dermatology, University of Cincinnati College of Medicine, Cincinnati, Ohio, USA.
  • 2 Department of Dermatology, School of Medicine, University of California, Davis, Sacramento, California, USA.
  • 3 Department of Dermatology, University of Cincinnati College of Medicine, Cincinnati, Ohio, USA. Electronic address: [email protected]
Type
Published Article
Journal
Journal of Investigative Dermatology
Publisher
Elsevier
Publication Date
Jan 01, 2015
Volume
135
Issue
1
Pages
202–211
Identifiers
DOI: 10.1038/jid.2014.315
PMID: 25054620
Source
Medline
Language
English
License
Unknown

Abstract

Galectin-3 is a family member of the carbohydrate-binding proteins widely expressed by many cell types and exhibits multiple cellular functions. We demonstrate that melanocytes express galectin-3, which is predominantly localized to the cell body peripherally along the Golgi zone. Downregulation of galectin-3 in human melanocytes using short hairpin RNA technology resulted in the reduction of both melanin synthesis and expression/activity of tyrosinase-related protein-1 (Tyrp-1). In the cell body, galectin-3 colocalizes with melanosome-destined cargo, specifically tyrosinase and Tyrp-1. We studied melanocytes cultured from patients with forms of Hermansky-Pudlak syndrome (HPS) containing defects in trafficking steps governed by biogenesis of lysosome-related organelle complex-2 (BLOC-2) (HPS-5), BLOC-3 (HPS-1), and adaptin-3 (HPS-2). We found that galectin-3 expression mimicked the defective expression of the tyrosinase cargo in dendrites of HPS-5 melanocytes, but it was not altered in HPS-1 or HPS-2 melanocytes. In addition, galectin-3 colocalized predominantly with the HPS-5 component of BLOC-2 in normal human melanocytes. These data indicate that galectin-3 is a regulatory component in melanin synthesis affecting the expression of Tyrp-1.

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