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Interferon research abs 1 || Hemoglobin research abs || Stem cell research abs || Nucleic acid research abs || Herpes research abs || Bronchitis research abs || Schizophrenia research abs || Tuberculosis research abs || Pneumonia research abs || Constipation research abs || Laxative research abs || hair research abs || hair related research references || testosterone related research references || melanin related research references







Gene. 2000 Dec 23;259(1-2):159-70.
Pigment cell-specific expression of the tyrosinase gene in ascidians has a different regulatory mechanism from vertebrates.

Toyoda R, Sato S, Ikeo K, Gojobori T, Numakunai T, Goding CR, Yamamoto H.

Biological Institute, Graduate School of Science, Tohoku University, Sendai 980-8578, Japan.

Tyrosinase is the key enzyme required for the synthesis of melanin pigments. Sequence comparison and functional analysis of the 5' upstream regions of vertebrate tyrosinase genes have revealed the importance of conserved E-box motifs in regulating their specific expression in pigment cells, optic cup-derived retinal pigment epithelium (RPE) and neural crest-derived melanocytes. In ascidians (more basal protochordates), two pigment cells that resemble vertebrate RPE cells are formed and specifically express the orthologous tyrosinase gene (HrTyr) in the cerebral vesicle located at the anterior end of the neural tube. To define regulatory sequences required for pigment cell-lineage-specific expression of HrTyr during embryogenesis, a series of mutations of the 5' upstream region of HrTyr were fused to the lacZ reporter gene and were microinjected into fertilized eggs. We found that the -152bp upstream of the translational start site is essential for expression in pigment cell precursors of tailbud-stage embryos. Further, additional positive and unique restriction elements were identified in the region up to -1.8kb. Surprisingly, in the -152bp minimal promoter or in other regions with regulatory activities, there are no E-box motifs or sequences correlating with other conserved elements regulating vertebrate tyrosinase promoters. The possibility that Pax proteins regulate HrTyr expression is also discussed.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11163973&dopt=Abstract



Cancer Lett. 2001 Jan;162 Suppl:S49-S55.
Migration and metalloproteinases determine the invasive potential of mouse melanoma cells, but not melanin and telomerase.

Zhao W, Liu H, Xu S, Entschladen F, Niggemann B, Zanker KS, Han R.

Department of Pharmacology I, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, No. 1 Xiannong Tan Street, Beijing 100050, P.R. China.

The biological characteristic cell locomotion and invasion, melanin content, metalloproteinases and telomerase activity were studied in a parental mouse melanoma cell line B16 and two descendents B16BL6 and B16F10. The invasive potential of melanoma cells was assayed in a transwell cell culture chamber. Melanin content was determined by the absorbance value at 470 nm per 10(6) cells. Tumor cells migration within the 3-D collagen matrix was microscopically recorded with a time-lapse video recorder and analyzed by computer-assisted cell tracking. Gelatin zymography was adopted to assay the metalloproteinases secretion. A polymerase chain reaction-based telomeric repeat amplification protocol (TRAP) was used for measuring telomerase activity. The results demonstrated that B16BL6 and B16F10 cells were highly invasive compared to B16 cells, but the melanin content of B16F10 was very low. B16F10 and B16BL6 were hypermotile and secreted much more metalloproteinases than B16. No differences were observed in telomerase activity among the three melanoma cell lines. Invasion of mouse melanoma was closely correlated to tumor cell migration and secretion of metalloproteinases. Melanin content and telomerase activity were phenotypically not related to invasiveness in these three mouse melanoma cell lines.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11164190&dopt=Abstract



FEMS Microbiol Lett. 2003 Mar 14;220(1):99-104.
Electron transfer from Shewanella algae BrY to hydrous ferric oxide is mediated by cell-associated melanin.

Turick CE, Caccavo F Jr, Tisa LS.

Department of Microbiology, University of New Hampshire, Durham, NH 03824-2617, USA. charles.turicrs.gov

Shewanella algae BrY uses insoluble mineral oxides as terminal electron acceptors, but the mechanism of electron transfer from cell surface to mineral surface is not well understood. We tested the hypothesis that cell-associated melanin produced by S. algae BrY serves as an electron conduit for bacterial-mineral reduction. Results from Fourier transform infrared spectroscopy and cell surface hydrophobicity assays indicated that extracellular melanin was associated with the cell surface. With H(2) as electron donor, washed cell suspensions of melanin-coated S. algae BrY reduced hydrous ferric oxide (HFO) 10 times faster than cells without melanin. The addition of melanin (20 microg ml(-1)) to these melanin-free cells increased their HFO reduction rate two-fold. These results suggest that cell-associated melanin acts as an electron conduit for iron mineral reduction by S. algae BrY.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12644234&dopt=Abstract








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