DHICA Oxidase Activity of TRP1 and Interactions With Other Melanogenic Enzymes

Kobayashi, Takashi; Urabe, Kazunori; Winder, Alison J.; Tsukamoto, Katsuhiko; Brewington, Timothy; Imokawa, Genji; Potterf, B.; Hearing, Vincent J.

doi:10.1111/j.1600-0749.1994.tb00054.x

Cited by 58 publications

(48 citation statements)

References 23 publications

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“…The detection of the absence of a single melanosomal protein by this organelle scanning approach in melan-si-1 cells that was present in wild-type cells suggested that this protein might represent the product of the si locus, which is mutated in the si cells. To confirm the validity of this prediction, the same extracts were analyzed with aPEP13, an antiserum directed against a synthetic peptide corresponding to the predicted carboxyl terminus ofthe murine si locus gene product (8). As expected, aPEP13 also recognized an antigen of 85 kDa in melan-a cells that was absent from melan-si-1 cells (Fig.…”

Section: Resultssupporting

confidence: 63%

“…Briefly, a 15-amino-acid sequence representing the predicted carboxyl terminus ofthe cloned murine si-encoded protein (8) was synthesized (BioSynthesis, Denton, TX) and conjugated to bovine serum albumin SuperCarrier (Pierce). Immunization and sera collection from the rabbit and the titration and specificity of antibody production, as determined by ELISA, was as reported (3).…”

Section: Methodsmentioning

confidence: 99%

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Identification of a melanosomal matrix protein encoded by the murine si (silver) locus using "organelle scanning".

Zhou

Kobayashi

Donatien

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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To Identify a broad sperm of melanosomal proteins, antisera were raised In rabbits against melanosomal protein fractions separated on the basi oftheir soubilit in the onic detergent Triton X-114. Antisera METHODS Subceflular Fractionation and Prparation of Antisera. Melanosomes were purified as described (7) from B16 cells grown as tumors subcutaneously in C57BL/6J mice. Stage III-IV melanosomes made up >90%6 ofthe organelles in the purified fraction as assessed by electron microscopy (7). To further fractionate melanosomes, they were solubilized in 0.1 M sodium phosphate buffer (pH 6.8) containing 1% (vol/vol) Triton X-114 at 40C for 10 min. Detergent-insoluble material was then removed by centrifugation at 10,000 x g for 10 min. The Triton X-114-soluble proteins were subjected to separation into aqueous and detergent phases [adapted from the method of Bordier (6)] as described (7). The protein content ofeach fraction was determined, and rabbits were immunized monthly with 0.2 mg of protein emulsified with complete Freund's adjuvant initially and subsequently in incomplete adjuvant as described (5). Rabbits were bled from the ear vein, the blood was allowed to coagulate at room temperature, and sera were isolated by centrifugation at 10,000 x g for 30 min. Final bleeds were obtained at 6 months. The production of antiserum to the Triton-insoluble melanosomal matrix has been described (5).The polyclonal antibody aPEP13 was produced in rabbits (8) using procedures as detailed (3). Briefly, a 15-amino-acid sequence representing the predicted carboxyl terminus ofthe cloned murine si-encoded protein (8) was synthesized (BioSynthesis, Denton, TX) and conjugated to bovine serum albumin SuperCarrier (Pierce). Immunization and sera collection from the rabbit and the titration and specificity of antibody production, as determined by ELISA, was as reported (3).Immunoblotting. Melanocyte lines were established from C57BL/6J mice, either wild type ("melan-a" cells), homozygous for the silver (si) mutation ("melan-si-l" cells), or homozygous for the albino (c) mutation ("melan-c" cells),

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Section: Resultssupporting

confidence: 63%

Section: Methodsmentioning

confidence: 99%

Identification of a melanosomal matrix protein encoded by the murine si (silver) locus using "organelle scanning".

Zhou

Kobayashi

Donatien

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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“…Interestingly, Dct also seems able to stabilize the activity of Tyr in vitro as does Tyrp1 (Hearing et al, 1992;Winder et al, 1994;Kobayashi et al, 1994c) and Dct forms a molecular complex with Tyr and Tyrp1 in vitro (Orlow et al, 1994). This suggested the possibility that Dct interacts with Tyr in vivo, a hypothesis not supported by our results.…”

Section: Fig 2 Interaction Of Tyr and Tyrp1 In Melanocytescontrasting

confidence: 55%

“…Tyrp1 and Dct, in addition to having enzymatic functions, stabilize Tyr (Hearing et al, 1992;Winder et al, 1994;Kobayashi et al, 1994c), and coexpression of Tyr with Tyrp1 or Dct in melanocytes increases pigmentation (Zhao et al, 1996;Manga et al, 2000;Hirosaki et al, 2002). These results suggest that TRP family proteins associate and form multienzyme complexes on the internal surface of the melanosomal membrane.…”

Section: Introductionmentioning

confidence: 99%

Direct interaction of tyrosinase with Tyrp1 to form heterodimeric complexes in vivo

Kobayashi

Hearing

2007

Journal of Cell Science

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“…GTP cyclohydrase-1 and mast cell proteases are probably involved in melanocyte and mast cell functions. PMEL17 is also known as an MITFinducible pigment cell-specific gene and a melanosomal matrix protein, which may function as a structural protein in melanogenesis (Kobayashi et al, 1994). JE and A7 are chemokines that are induced by immunoglobulin (Ig) E plus antigen stimulation in mast cells.…”

Section: Discussionmentioning

confidence: 99%

STAT3 and MITF cooperatively induce cellular transformation through upregulation of c-fos expression

et al. 2004

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The signal transducer and activator of transcription (STAT) family proteins are transcription factors critical in mediating cytokine signaling. Among them, STAT3 is frequently activated in a number of human cancers and transformed cell lines and is implicated in tumorigenesis. However, although constitutively activated STAT3 mutant (STAT3C) leads to cellular transformation, its transformation potential such as colony-forming activity in soft-agar is much weaker than that of v-src. To identify tumorigenic factors that cooperatively induce cellular transformation with STAT3C, we screened the retroviral cDNA library. We found that the microphthalmiaassociated transcription factor (MITF), an essential transcription factor for melanocyte development and pigmentation, induces anchorage-independent growth of NIH-3T3 cells in cooperation with STAT3C. Microarray analysis revealed that c-fos is highly expressed in transformants expressing STAT3C and MITF. Promoter analysis and chromatin immunoprecipitation assay suggested that both STAT3 and MITF can cooperatively upregulate the c-fos gene. In addition, the transformation of NIH-3T3 cells by both MITF and STAT3C was significantly suppressed by a dominant-negative AP-1 retrovirus. These data indicate that MITF and STAT3 cooperatively induce c-fos, resulting in cellular transformation.

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DHICA Oxidase Activity of TRP1 and Interactions With Other Melanogenic Enzymes

Cited by 58 publications

References 23 publications

Identification of a melanosomal matrix protein encoded by the murine si (silver) locus using "organelle scanning".

Identification of a melanosomal matrix protein encoded by the murine si (silver) locus using "organelle scanning".

Direct interaction of tyrosinase with Tyrp1 to form heterodimeric complexes in vivo

STAT3 and MITF cooperatively induce cellular transformation through upregulation of c-fos expression

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