Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity

Halaban, R; Moellmann, G

doi:10.1073/pnas.87.12.4809

Title: Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity

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Abstract

Melanogenesis is regulated in large part by tyrosinase, and defective tyrosinase leads to albinism. The mechanisms for other pigmentation determinants (e.g., those operative in tyrosinase-positive albinism and in murine coat-color mutants) are not yet known. One murine pigmentation gene, the brown (b) locus, when mutated leads to a brown (b/b) or hypopigmentated (B{sup lt}/B{sup lt}) coat versus the wild-type black (B/B). The authors show that the b locus codes for a glycoprotein with the activity of a catalase (catalase B). Only the c locus protein is a tyrosinase. Because peroxides may be by-products of melanogenic activity and hydrogen peroxide in particular is known to destroy melanin precursors and melanin, they conclude that pigmentation is controlled not only by tyrosinase but also by a hydroperoxidase. The studies indicate that catalase B is identical with gp75, a known human melanosomal glycoprotein; that the b mutation is in a heme-associated domain; and that the B{sup lt} mutation renders the protein susceptible to rapid proteolytic degradation.

Authors:

Halaban, R; Moellmann, G ^[1]

Yale Univ. School of Medicine, New Haven, CT (USA)

Publication Date:: Fri Jun 01 00:00:00 EDT 1990

OSTI Identifier:: 6249964

Resource Type:: Journal Article

Journal Name:: Proceedings of the National Academy of Sciences of the United States of America; (USA)

Additional Journal Information:: Journal Volume: 87:12; Journal ID: ISSN 0027-8424

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; CATALASE; ENZYME ACTIVITY; MELANIN; HEREDITARY DISEASES; TYROSINASE; GENE MUTATIONS; ANTIBODIES; GENES; MAN; MICE; PIGMENTS; ANIMALS; DISEASES; ENZYMES; HYDROXY COMPOUNDS; HYDROXYLASES; MAMMALS; MUTATIONS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; OXIDOREDUCTASES; PEROXIDASES; PRIMATES; RODENTS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats


                    Halaban, R, and Moellmann, G. Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity.  United States: N. p., 1990. 
        Web.  doi:10.1073/pnas.87.12.4809.

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                    Halaban, R, & Moellmann, G. Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity.  United States.  https://doi.org/10.1073/pnas.87.12.4809

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                    Halaban, R, and Moellmann, G. 1990.  
        "Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity".  United States.  https://doi.org/10.1073/pnas.87.12.4809.

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@article{osti_6249964,

  title        = {Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity},

  author       = {Halaban, R and Moellmann, G},

  abstractNote = {Melanogenesis is regulated in large part by tyrosinase, and defective tyrosinase leads to albinism. The mechanisms for other pigmentation determinants (e.g., those operative in tyrosinase-positive albinism and in murine coat-color mutants) are not yet known. One murine pigmentation gene, the brown (b) locus, when mutated leads to a brown (b/b) or hypopigmentated (B{sup lt}/B{sup lt}) coat versus the wild-type black (B/B). The authors show that the b locus codes for a glycoprotein with the activity of a catalase (catalase B). Only the c locus protein is a tyrosinase. Because peroxides may be by-products of melanogenic activity and hydrogen peroxide in particular is known to destroy melanin precursors and melanin, they conclude that pigmentation is controlled not only by tyrosinase but also by a hydroperoxidase. The studies indicate that catalase B is identical with gp75, a known human melanosomal glycoprotein; that the b mutation is in a heme-associated domain; and that the B{sup lt} mutation renders the protein susceptible to rapid proteolytic degradation.},

  doi          = {10.1073/pnas.87.12.4809},

  url          = {https://www.osti.gov/biblio/6249964},
  journal      = {Proceedings of the National Academy of Sciences of the United States of America; (USA)},

  issn         = {0027-8424},

  number       = ,

  volume       = 87:12,

  place        = {United States},

  year         = {Fri Jun 01 00:00:00 EDT 1990},

  month        = {Fri Jun 01 00:00:00 EDT 1990}

}

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