The mouse brown (b) locus protein has dopachrome tautomerase activity and is located in lysosomes in transfected fibroblasts

QUICK SEARCH:

[advanced]

	Author:		Keyword(s):

Home Help Feedback Subscriptions Archive Search Table of Contents

This Article

	Summary
	Full Text (PDF)
	Alert me when this article is cited
	Alert me if a correction is posted

Services

	Email this article to a friend
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new issues of the journal
	Download to citation manager


Citing Articles

	Citing Articles via HighWire
	Citing Articles via Google Scholar

Google Scholar

	Articles by Winder, A. J.
	Articles by Rorsman, H.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Winder, A. J.
	Articles by Rorsman, H.

Aroca, P., Garc\222a-Borron, J. C., Solano, F. and Lozano, J. A (1990). Regulation of mammalian melanogenesis I: partial purification and characterization of a dopachrome converting factor: dopachrome tautomerase. Biochim. Biophys. Acta 1035, 266-.[Medline]

Aroca, P., Martinez-Liarte, J. H., Solano, F., Garc\222a-Borron, J. C. and Lozano, J. A (1992). The action of glycosylases on dopachrome (2-carboxy-2,3-dihydroindole-5,6-quinone) tautomerase. Biochem J 284, 109-.

Aroca, P., Solano, F., Salinas, C., Garc\222a-Borron, J. C. and Lozano, J. A (1992). Regulation of the final phase of mammalian melanogenesis: theA. J. Winder and othersTable 3. Putative Golgi sorting signalsMouse CD3- Mouse CD3-Mouse b-protein Human b-proteinMouse tyrosinase Human tyrosinaseMouse TRP-2 Human LAPMouse LAMP-1 Comparison of the amino acid sequences of the carboxy-terminal cytoplasmic tails of the b-protein, tyrosinase and TRP-2 with proteins targeted tolysosomes. Amino acids thought to be important for Golgi sorting are underlined. LAP, lysosomal acid phosphatase.165Expression of mouse b-proteinrole of dopachrome tautomerase and the ratio between 5,6-dihydroxyindole-2-carboxylic acid and 5,6-dihydroxyindole. Eur. J. Biochem 208, 155-.[Medline]

Andrews, P. C. and Krinsky, N. I (1986). Human myeloperoxidase and hemi-myeloperoxidase. Methods Enzymol 132, 369-.[Medline]

Barber, J. L., Townsend, D., Olds, D. P. and King, R. A (1984). Dopachrome oxidoreductase: a new enzyme in the pigment pathway. J. Invest. Dermatol 83, 145-.[Medline]

Baudhuin, P., Beaufay, H., Rahman-Li, Y., Sellinger, O. Z., Wattiaux, R., Jacques, P. and de Duve, C (1964). Tissue fractionation studies 17. Intracellular distribution of monoamine oxidase, aspartate aminotransferase, alanine aminotransferase, D-amino acid oxidase and catalase in rat-liver tissue. Biochem. J 92, 179-.[Medline]

Bennett, D. C., Huszar, D., Laipis, P. J., Jaenisch, R. and Jackson, I. J (1990). Phenotypic rescue of mutant brown melanocytes by a retrovirus carrying a wild-type tyrosinase-related protein gene. Development 110, 471-.[Abstract/Free Full Text]

Bodnar, A. G. and Rachubinski, R. A (1990). Cloning and sequence determination of cDNA encoding a second rat liver peroxisomal 3-ketoacyl-CoA thiolase. Gene 91, 193-.[Medline]

Bradford, M. M (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem 72, 248-.[Medline]

Chakraborty, A. K., Orlow, S. J. and Pawelek, J. M (1992). Evidence that dopachrome tautomerase is a ferrous iron-binding glycoprotein. FEBS Lett 302, 126-.[Medline]

Chen, J. W., Murphy, T. L., Willingham, M. C., Pastan, I. and August, J. T (1985). Identification of two lysosomal membrane glycoproteins. J. Cell Biol 101, 85-.[Abstract/Free Full Text]

Chintamaneni, C. D., Halaban, R., Kobayashi, Y., Witkop, C. J. and Kwon, B. S (1991). A single base insertion in the putative transmembrane domain of the tyrosinase gene as a cause for tyrosinase-negative oculocutaneous albinism. Proc. Nat. Acad. Sci. USA 88, 5272-.[Abstract/Free Full Text]

Cohen, T., Muller, R. M., Tomita, Y. and Shibahara, S (1990). Nucleotide sequence of the cDNA encoding human tyrosinase-related protein. Nucl. Acids Res 18, 2807-.[Free Full Text]

d'Ischia, M., Napolitano, A. and Prota, G (1991). Peroxidase as an alternative to tyrosinase in the oxidative polymerisation of 5,6-dihydroxyindoles to melanin(s). Biochim. Biophys. Acta 1073, 423-.[Medline]

Fukuda, M (1991). Lysosomal membrane glycoproteins: structure, biosynthesis and intracellular trafficking. J. Biol. Chem 266, 21327-.[Free Full Text]

Giacomini, P., Fraioli, R., Cuomo, M. and Natali, P. G (1992). Membrane compartmentalization of melanosomal gp75. J. Invest. Dermatol 98, 340-.[Medline]

Gould, S. J., Keller, G.-A. and Subramani, S (1988). Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins. J. Cell Biol 107, 897-.[Abstract/Free Full Text]

Halaban, R. and Moellmann, G (1990). Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity. Proc. Nat. Acad. Sci. USA 87, 4809-.[Abstract/Free Full Text]

Halaban, R., Pomerantz, S. H., Marshall, S., Lambert, D. T. and Lerner, A. B (1983). Regulation of tyrosinase in human melanocytes grown in culture. J. Cell Biol 97, 480-.[Abstract/Free Full Text]

Hearing, V. J. and Jimenez, M (1987). Mammalian tyrosinase \321 the critical regulatory control point in melanocyte pigmentation. Int. J. Biochem 19, 1141-.[Medline]

Hearing, V. J. and Jimenez, M (1989). Analysis of mammalian pigmentation at the molecular level. Pigment Cell Res 2, 75-.[Medline]

Hearing, V. J. and Tsukamoto, K (1991). Enzymatic control of pigmentation in mammals. FASEB J 5, 2902-.[Abstract]

Jackson, I. J (1988). A cDNA encoding tyrosinase-related protein maps to the brown locus in mouse. Proc. Nat. Acad. Sci. USA 85, 4392-.[Abstract/Free Full Text]

Jackson, I. J., Chambers, D., Rinchik, E. M. and Bennett, D. C (1990). Characterization of TRP-1 mRNA levels in dominant and recessive mutations at the mouse brown ( b ) locus. Genetics 126, 451-.[Abstract]

Jackson, I. J., Chambers, D. M., Tsukamoto, K., Copeland, N. G., Gilbert, D. J., Jenkins, N. A. and Hearing, V. J (1992). A second tyrosinase-related protein, TRP-2, maps to and is mutated at the mouse slaty locus. EMBO J 11, 527-.[Medline]

Jara, J. R., Solano, F., Garc\222a-Borron, J. C., Aroca, P. and Lozano, J. A (1990). Regulation of mammalian melanogenesis II: the role of metal cations. Biochim. Biophys. Acta 1035, 276-.[Medline]

Jimenez, M., Kameyama, K., Maloy, W. L., Tomita, Y. and Hearing, V. J (1988). Mammalian tyrosinase: biosynthesis, processing and modulation by melanocyte-stimulating hormone. Proc. Nat. Acad. Sci. USA 85, 3830-.[Abstract/Free Full Text]

Jimenez, M., Maloy, W. L. and Hearing, V. J (1989). Specific identification of an authentic clone for mammalian tyrosinase. J. Biol. Chem 264, 3397-.[Abstract/Free Full Text]

Jimenez, M., Tsukamoto, K. and Hearing, V. J (1991). Tyrosinases from two different loci are expressed by normal and by transformed melanocytes. J. Biol. Chem 266, 1147-.[Abstract/Free Full Text]

Johnson, K. F. and Kornfeld, S (1992). The cytoplasmic tail of the mannose 6-phosphate/Insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi. J. Cell Biol 119, 249-.[Abstract/Free Full Text]

Johnson, L. V., Walsh, M. L. and Chen, L. B (1980). Localization of mitochondria in living cells with rhodamine 123. Proc. Nat. Acad. Sci. USA 77, 990-.[Abstract/Free Full Text]

Johnson, R. and Jackson, I. J (1992). Light is a dominant mouse mutation resulting in premature cell death. Nature Genet 1, 226-.[Medline]

Jonasson, J., Povey, S. and Harris, H (1977). The analysis of malignancy by cell fusion. VII. Cytogenetic analysis of hybrids between malignant and diploid cells and of tumours derived from them. J. Cell Sci 24, 217-.[Medline]

Kaetzel, C. S., Rao, C. K. and Lamm, M. E (1987). Protein disulphide-isomerase from human placenta and rat liver. Biochem. J 241, 39-.[Medline]

Korner, A. M. and Gettins, P (1985). Synthesis in vitro of 5,6-dihydroxyindole-2-carboxylic acid by dopachrome conversion factor from Cloudman S91 melanoma cells. J. Invest. Dermatol 85, 229-.[Medline]

Korner, A. M. and Pawelek, J (1980). Dopachrome conversion: a possible control point in melanin biosynthesis. J. Invest. Dermatol 75, 192-.[Medline]

Korner, A. M. and Pawelek, J (1982). Mammalian tyrosinase catalyses three reactions in the biosynthesis of melanin. Nature 217, 1163-.

Kornfeld, S. and Mellman, I (1989). The biogenesis of lysosomes. Annu. Rev. Cell Biol 5, 483-.

Kwon, B. S., Chintamaneni, C., Kozak, C. A., Copeland, N. G., Gilbert, D. J., Jenkins, N., Barton, D., Francke, U., Kobayashi, Y. and Kim, K. K (1991). A melanocyte-specific gene, Pmel 17, maps near the silver coat color locus on mouse chromosome 10 and is in a syntenic region on human chromosome 12. Proc. Nat. Acad. Sci. USA 88, 9228-.[Abstract/Free Full Text]

Kwon, B. S., Haq, A. K., Pomerantz, S. H. and Halaban, R (1987). Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proc. Nat. Acad. Sci. USA 84, 7473-.[Abstract/Free Full Text]

Lazarow, P. B. and Fujiki, Y (1985). Biogenesis of peroxisomes. Annu. Rev. Cell Biol 1, 489-.

Laemmli, U. K (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-.[Medline]

Leonard, L. J., Townsend, D. and King, R. A (1988). Function of dopachrome oxidoreductase and metal ions in dopachrome conversion in the eumelanin pathway. Biochemistry 27, 6156-.[Medline]

Letourneur, F. and Klausner, R. D (1992). A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains. Cell 69, 1143-.[Medline]

Logan, A. and Weatherhead, B (1978). Pelage color cycles and hair follicle tyrosinase activity in the Siberian hamster. J. Invest. Dermatol 71, 295-.[Medline]

Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J (1951). Protein measurement with the Folin phenol reagent. J. Biol. Chem 193, 265-.[Free Full Text]

Meisler, M. and Paigen, K (1972). Coordinated development of-glucuronidase and -galactosidase in mouse organs. Science 177, 894-.[Abstract/Free Full Text]

Mishima, Y. and Imokawa, G (1983). Selective aberration and pigment loss in melanosomes of malignant melanoma cells in vitro by glycosylation inhibitors: premelanosomes as glycoprotein. J. Invest. Dermatol 81, 106-.[Medline]

Muller, G., Ruppert, S., Schmid, E. and Schutz, G (1988). Functional analysis of alternatively spliced tyrosinase gene transcripts. EMBO J 7, 2723-.[Medline]

Novikoff, A. B., Albala, A. and Biempica, L (1968). Ultrastructural and cytochemical observations on B-16 and Harding-Passey mouse melanomas: the origin of premelanosomes and compound melanosomes. J. Histochem. Cytochem 16, 299-.[Abstract]

Ohkuma, S. and Poole, B (1978). Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc. Nat. Acad. Sci. USA 75, 3327-.[Abstract/Free Full Text]

Olsen, I., Oliver, T., Muir, H., Smith, R. and Partridge, T (1986). Role of cell adhesion in contact-dependent transfer of a lysosomal enzyme from lymphocytes to fibroblasts. J. Cell Sci 85, 231-.[Abstract]

Orlow, S. J., Boissy, R. E., Moran, D. J. and Pifko-Hirst, S (1993). Subcellular distribution of tyrosinase and tyrosinase-related protein-1: implications for melanosomal biogenesis. J. Invest. Dermatol 100, 55-.[Medline]

Palumbo, A., d'Ischia, M., Misuraca, G. and Prota, G (1987). Effect of metal ions on the rearrangement of dopachrome. Biochim. Biophys. Acta 925, 203-.[Medline]

Pawelek, J. M (1990). Dopachrome conversion factor functions as an isomerase. Biochem. Biophys. Res. Commun 166, 1328-.[Medline]

Pawelek, J. M (1991). After dopachrome?. Pigment Cell Res 4, 53-.[Medline]

Pawelek, J. M., Korner, A., Bergstrom, A. and Bologna, J (1980). New regulators of melanin biosynthesis and the autodestruction of melanoma cells. Nature 286, 617-.[Medline]

Peters, C., Braun, M., Weber, B., Wendland, M., Schmidt, B., Pohlmann, R., Waheed, A. and von Figura, K (1990). Targeting of a lysosomal membrane protein: a tyrosine-containing endocytosis signal in the cytoplasmic tail of lysosomal acid phosphatase is necessary and sufficient for targeting to lysosomes. EMBO J 9, 3497-.[Medline]

Roux, L. and Lloyd, K. O (1986). Glycosylation characteristics of pigmentation-associated antigen (GP75): an intracellular glycoprotein of human melanocytes and malignant melanomas. Arch. Biochem. Biophys 251, 87-.[Medline]

Ruppert, S., Muller, G., Kwon, B. and Schutz, G (1988). Multiple transcripts of the mouse tyrosinase gene are generated by alternative splicing. EMBO J 7, 2715-.[Medline]

Saeki, H. and Oikawa, A (1983). Stimulation of tyrosinase activity of cultured melanoma cells by lysosomotropic agents. J. Cell. Physiol 116, 93-.[Medline]

Seiji, M. and Kikuchi, A (1969). Acid phosphatase activity in melanosomes. J. Invest. Dermatol 52, 212-.[Medline]

Shibahara, S., Taguchi, H., Muller, R. M., Shibata, K., Cohen, T., Tomita, Y. and Tagami, H (1991). Structural organization of the pigment cell-specific gene located at the brown locus in mouse. Its promoter activity and alternatively spliced transcripts. J. Biol. Chem 266, 15895-.[Abstract/Free Full Text]

Shibahara, S., Tomita, Y., Sakakura, T., Nager, C., Chaudhuri, B. and Muller, R (1986). Cloning and expression of cDNA encoding mouse tyrosinase. Nucl. Acids Res 14, 2413-.[Abstract/Free Full Text]

Slominski, A., Moellmann, G., Kuklinska, E., Bomirski, A. and Pawelek, J (1988). Positive regulation of melanin pigmentation by two key substrates of the melanogenic pathway, L-tyrosine and L-dopa. J. Cell Sci 89, 287-.[Abstract/Free Full Text]

Steel, D. M. and Harris, H (1989). The effect of antisense RNA tofibronectin on the malignancy of hybrids between melanoma cells and normal fibroblasts. J. Cell Sci 93, 515-.[Abstract/Free Full Text]

Sugumaran, M (1992). Letter to the editor. Pigment Cell Res 5, 203-.[Medline]

Sugumaran, M., Dali, H. and Semensi, V (1990). Formation of a stable quinone methide during tyrosinase-catalysed oxidation of-methyl dopa methyl ester and its implication in melanin biosynthesis. Bioorg. Chem 18, 144-.

Sugumaran, M. and Semensi, V (1991). Quinone methide as a new intermediate in eumelanin biosynthesis. J. Biol. Chem 266, 6073-.[Abstract/Free Full Text]

Thomson, T. M., Mattes, M. J., Roux, L., Old, L. J. and Lloyd, K. O (1985). Pigmentation-associated glycoprotein of human melanomas and melanocytes: definition with a mouse monoclonal antibody. J. Invest. Dermatol 85, 169-.[Medline]

Thomson, T. M., Real, F. X., Murakami, S., Cordon-Cardo, C., Old, L. J. and Houghton, A. N (1988). Differentiation antigens of melanocytes and melanoma: analysis of melanosome and cell surface markers of human pigmented cells with monoclonal antibodies. J. Invest. Dermatol 90, 459-.[Medline]

Tomita, Y., Montague, P. M. and Hearing, V. J (1985). Anti-T4 -tyrosinase monoclonal antibodies \321 specific markers for pigmented melanocytes. J. Invest. Dermatol 85, 426-.[Medline]

Tripathi, R. K., Hearing, V. J., Urabe, K., Aroca, P. and Spritz, R. A (1992). Mutational mapping of the catalytic activities of human tyrosinase. J. Biol. Chem 267, 23707-.[Abstract/Free Full Text]

Tsukamoto, K., Jackson, I. J., Urabe, K., Montague, P. M. and Hearing, V. J (1992). A second tyrosinase-related protein, TRP-2, is a melanogenic enzyme termed DOPAchrome tautomerase. EMBO J 11, 519-.[Medline]

van den Bosch, H., Schutgens, R. B. H., Wanders, R. J. A. and Tager, J. M (1992). Biochemistry of peroxisomes. Annu. Rev. Biochem 61, 157-.[Medline]

Vijayasaradhi, S., Bouchard, B. and Houghton, A. N (1990). The melanoma antigen gp75 is the human homologue of the mouse b ( brown ) locus gene product. J. Exp. Med 171, 1375-.[Abstract/Free Full Text]

Vijayasaradhi, S., Doskoch, P. M. and Houghton, A. N (1991). Biosynthesis and intracellular movement of the melanosomal membrane glycoprotein gp75, the human b (brown) locus product. Exp. Cell Res 196, 233-.[Medline]

Vijayasaradhi, S. and Houghton, A. N (1991). Purification of an autoantigenic 75-kDa human melanosomal glycoprotein. Int. J. Cancer 47, 298-.[Medline]

Williams, M. A. and Fukuda, M (1990). Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail. J. Cell Biol 111, 955-.[Abstract/Free Full Text]

Winder, A. J (1991). Expression of a mouse tyrosinase cDNA in 3T3 Swiss mouse fibroblasts. Biochem. Biophys. Res. Commun 178, 739-.[Medline]

Winder, A. J. and Harris, H (1991). New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase. Eur. J. Biochem 198, 317-.[Medline]

Winder, A. J. and Harris, H (1992). Induction of tyrosinase in human melanoma cells by L-tyrosine phosphate and cytochalasin D. Exp. Cell Res 199, 248-.[Medline]

Winder, A. J., Wittbjer, A., Rosengren, E. and Rorsman, H (1993). Fibroblasts expressing mouse c locus tyrosinase produce an authentic enzyme and synthesise phaeomelanin. J. Cell Sci 104, 467-.[Abstract]

This article has been cited by other articles:

R. Piccirillo, I. Palmisano, G. Innamorati, P. Bagnato, D. Altimare, and M. V. Schiaffino
An unconventional dileucine-based motif and a novel cytosolic motif are required for the lysosomal and melanosomal targeting of OA1
J. Cell Sci., May 15, 2006; 119(10): 2003 - 2014.
[Abstract] [Full Text] [PDF]

M. d'Addio, A. Pizzigoni, M. T. Bassi, C. Baschirotto, C. Valetti, B. Incerti, M. Clementi, M. De Luca, A. Ballabio, and M. V. Schiaffino
Defective intracellular transport and processing of OA1 is a major cause of ocular albinism type 1
Hum. Mol. Genet., December 1, 2000; 9(20): 3011 - 3018.
[Abstract] [Full Text] [PDF]

T Simmen, A Schmidt, W Hunziker, and F Beermann
The tyrosinase tail mediates sorting to the lysosomal compartment in MDCK cells via a di-leucine and a tyrosine-based signal
J. Cell Sci., January 1, 1999; 112(1): 45 - 53.
[Abstract] [PDF]

T. Kobayashi, G. Imokawa, D. C. Bennett, and V. J. Hearing
Tyrosinase Stabilization by Tyrp1 (the brown Locus Protein)
J. Biol. Chem., November 27, 1998; 273(48): 31801 - 31805.
[Abstract] [Full Text] [PDF]

S. Diment, M. Eidelman, G. M. Rodriguez, and S. J. Orlow
Lysosomal Hydrolases Are Present in Melanosomes and Are Elevated in Melanizing Cells
J. Biol. Chem., March 3, 1995; 270(9): 4213 - 4215.
[Abstract] [Full Text] [PDF]

This Article

Summary

Full Text (PDF)

Alert me when this article is cited

Alert me if a correction is posted

Services

Email this article to a friend

Similar articles in this journal

Similar articles in PubMed

Alert me to new issues of the journal

Download to citation manager

Citing Articles

Citing Articles via HighWire

Citing Articles via Google Scholar

Google Scholar

Articles by Winder, A. J.

Articles by Rorsman, H.

Search for Related Content

PubMed

PubMed Citation

Articles by Winder, A. J.

Articles by Rorsman, H.

				M. d'Addio, A. Pizzigoni, M. T. Bassi, C. Baschirotto, C. Valetti, B. Incerti, M. Clementi, M. De Luca, A. Ballabio, and M. V. Schiaffino Defective intracellular transport and processing of OA1 is a major cause of ocular albinism type 1 Hum. Mol. Genet., December 1, 2000; 9(20): 3011 - 3018. [Abstract] [Full Text] [PDF]

				T Simmen, A Schmidt, W Hunziker, and F Beermann The tyrosinase tail mediates sorting to the lysosomal compartment in MDCK cells via a di-leucine and a tyrosine-based signal J. Cell Sci., January 1, 1999; 112(1): 45 - 53. [Abstract] [PDF]

				T. Kobayashi, G. Imokawa, D. C. Bennett, and V. J. Hearing Tyrosinase Stabilization by Tyrp1 (the brown Locus Protein) J. Biol. Chem., November 27, 1998; 273(48): 31801 - 31805. [Abstract] [Full Text] [PDF]

				S. Diment, M. Eidelman, G. M. Rodriguez, and S. J. Orlow Lysosomal Hydrolases Are Present in Melanosomes and Are Elevated in Melanizing Cells J. Biol. Chem., March 3, 1995; 270(9): 4213 - 4215. [Abstract] [Full Text] [PDF]