Genetic and Epigenetic Control of the Proliferation and Differentiation of Mouse Epidermal Melanocytes in Culture

Hirobe, Tomohisa; Abé, Hiroyuki

doi:10.1111/j.1600-0749.1999.tb00508.x

Cited by 50 publications

(41 citation statements)

References 114 publications

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“…The spontaneous regression of melanocytes in hair follicles of the Light (Tyrp1 B-lt ) mice at the end of hair cycle was speculated to be a consequence of leakage of toxic metabolites of melanin synthesis due to disruption of the melanosomal ultrastructure associated with mutation of Tyrp1 (85). Moreover, the mutation in the Tyrp1 b was also associated with the presence of a disordered internal structure in stage III melanosomes (86). Since the mutation in the murine Typr1 b affected melanosome structure, we investigated the effect of a similar mutation in human TRYP1.…”

Section: Tyrp1 Its Functionmentioning

confidence: 99%

“…This is the first observation demonstrating that Tyrp1 is involved, perhaps to a limited extent, in the maintenance of the integrity of melanosome ultrastructure. The C86Y mutation associated with murine Tyrp1 b does not result in significant alteration in melanosome structure in the C57B/6J background (73), but does affect Tyrp1 b mice in the C57BL/10Hir background (86); this suggests subtle differences in Tyrp1 structure can influence its role in the maintenance of melanocyte function.…”

Section: Tyrp1 Its Functionmentioning

confidence: 99%

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Tyrp1 and Oculocutaneous Albinism Type 3

Sarangarajan

Boissy

2001

Pigment Cell Research

111

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addition to its role in eumelanin synthesis, Tyrp1 is involved in Tyrosinase-related protein 1 (Tyrp1) is a melanocyte-specific maintaining stability of tyrosinase protein and modulating its gene product involved in eumelanin synthesis. Mutations in the catalytic activity. Tyrp1 is also involved in maintenance of mouse Tyrp1 gene are associated with brown pelage, and in the human TYRP1 gene with oculocutaneous albinism type 3 melanosome ultrastructure and affects melanocyte prolifera-(OCA3). In the murine system, Tyrp1 expresses significant tion and melanocyte cell death. The current review is an dihydroxyindole carboxylic acid oxidase (i.e. DHICA oxattempt to consolidate our understanding of the role of Tyrp1 idase) activity. However, in humans, TYRP1 is enigmatic in in the melanocyte. that despite extensive efforts focused on the study of its Key words: Pigmentation, Tyrosine hydroxylase, Brown/Rufunction, its actual role in the human melanocyte is still fous Albinism, Brown locus, Protein trafficking unclear. There is mounting evidence demonstrating that in Mutations in the genes encoding some of the enzymes and regulatory proteins involved in melanin synthesis result in various forms of oculocutaneous albinism (OCA). OCA1 correlates with mutations in the tyrosinase (TYR) gene (7). Most individuals with OCA1 have completely amelanotic skin, hair and eyes with the inability to tan (i.e. OCA1A). However, some nucleotide lesions of the TYR gene result in a partially functional enzyme so that individuals with this subtype of OCA1 can exhibit moderate levels of skin and hair pigmentation and the ability to tan (i.e. OCA1B). OCA2 correlates with mutations in the P gene (8). Individuals with OCA2 present with minimal to moderate amounts of pigment remaining in the skin, hair and eyes, many of whom can develop pigmented freckles, lentigines and/or nevi with age. OCA3 correlates with mutations in the TYRP1 gene (9). Individuals with OCA3 present with minimal pigment reduction in the skin, hair and eyes. This form of albinism was previously referred to as Rufous and possibly some forms of Brown albinism.

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Section: Tyrp1 Its Functionmentioning

confidence: 99%

Section: Tyrp1 Its Functionmentioning

confidence: 99%

Tyrp1 and Oculocutaneous Albinism Type 3

Sarangarajan

Boissy

2001

Pigment Cell Research

111

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“…After centrifugation, cell pellets were resuspended in the culture medium. 7) Melanoblast-defined medium (MDM) consisted of Ham's F-10 plus insulin (bovine) 10 µg/ml, bovine serum albumin 0.5 mg/ml (fraction V), ethanolamine 1 µM, phosphoethanolamine 1 µM, sodium selenite 10 nM, penicillin G 100 U/ml, streptomycin sulfate 100 µg/ml, gentamycin sulfate 50 µg/ml, and amphotericin B 0.25 µg/ml. Melanocyte-differentiation medium (MDMM) consisted of MDM supplemented with α-melanocytestimulating hormone (MSH) 100 nM.…”

Section: Methodsmentioning

confidence: 99%

“…Since α-MSH is known to stimulate melanocyte differentiation in vivo and in vitro, 7) this medium can be used to determine whether Pairogen or Pairogen Gold stimulates differentiation-stimulating activity toward melanoblasts in cooperation with α-MSH. When epidermal cell suspensions were cultured in MDMM, pigment-producing differentiated melanocytes appeared around keratinocyte colonies within 2-3 days and then increased in number.…”

Section: Effects Of Pairogen and Pairogen Gold On Proliferation And Dmentioning

confidence: 99%

“…Since MDM does not contain melanogens such as α-MSH or DBcAMP, [5][6][7] this medium can be used to determine whether FFC, Pairogen, or Pairogen Gold possesses differentiation-stimulating activity for melanoblasts. Bipolar, tripolar, or dendritic melanoblasts were in contact with adjacent keratinocyte colonies through a dendritic process within a day or two after initiation of the primary culture.…”

Section: Effects Of Ffc Pairogen and Pairogen Gold On Proliferationmentioning

confidence: 99%

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Ferrous Ferric Chloride Induces the Differentiation of Cultured Mouse Epidermal Melanocytes Additionally with Herbal Medicines

Hirobe¹

2009

JOURNAL OF HEALTH SCIENCE

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Ferrous ferric chloride (FFC) is a special form of aqueous iron that is a complex of ferrous chloride and ferric chloride and participates in oxidation and reduction reactions. My previous study showed that FFC stimulated the proliferation and differentiation of cultured epidermal melanoblasts or melanocytes derived from newborn mice. However, it is not known whether FFC stimulates the proliferation and differentiation of melanocytes in cooperation with natural factors, such as vinegars, vitamins, and herbal medicines. The drink Pairogen R (Akatsuka Co., Tsu, Japan) consists of FFC, vinegars, and vitamins, while Pairogen Gold R (Akatsuka Co.) contains herbal medicines in addition to FFC, vinegar, and vitamins. To clarify whether these natural factors supplemented to Pairogen or Pairogen Gold elicit stimulative effects on skin function, Pairogen and Pairogen Gold were added to the culture medium and tested for their proliferation-and differentiation-stimulating activity on melanocytes. Although Pairogen Gold failed to increase melanocyte proliferation beyond that elicited by FFC alone, it markedly increased melanocyte differentiation. In contrast, Pairogen possessed no such effect. The extracts of Chinese wolfberry (Lycium chinense) and Siberian ginseng (Eleutherococcus senticosus) that are included in Pairogen Gold stimulated melanocyte differentiation additionally with FFC. Therefore, these results suggest that FFC is involved in regulating the differentiation of melanocytes additionally with extracts of Chinese wolfberry and Siberian ginseng.

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ACTH4-12 is the minimal message sequence required to induce the differentiation of mouse epidermal melanocytes in serum-free primary culture

Hirobe¹,

Abé

2000

J. Exp. Zool.

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It is well known that α‐melanocyte stimulating hormone (MSH) induces the differentiation of mouse epidermal melanocytes in vivo and in vitro. Although adrenocorticotropic hormone (ACTH) possesses the same amino acid sequence as MSH does, it is not clear whether the peptide and its fragments induce the differentiation of mouse epidermal melanocytes. In this study, the differentiation‐inducing potencies of human ACTH and its fragments were investigated by adding them into a culture medium (0.001–1,000 nM) from the initiation of primary culture of epidermal cell suspensions. Their potencies were compared with the potency of α‐MSH. After 2–4 days of primary cultures with ACTH1–13, ACTH1–17, ACTH1–24, ACTH1–39, ACTH4–12, ACTH4–13, and α‐MSH, pigment granules appeared in the cytoplasms and dendrites of melanoblasts that were in contact with the adjacent keratinocyte colonies. By 14 days, cultures contained mostly pigmented melanocytes. The order of potencies of ACTH fragments and α‐MSH shown by the ED50 value was as follows: α‐MSH = ACTH1–13 = ACTH1–17 = ACTH4–12 = ACTH4–13 > ACTH1–24 > ACTH1–39. The length of their peptide chains was inversely proportional to the potency. On the contrary, ACTH1–4, ACTH11–24, and ACTH18–39 failed to induce the differentiation of melanocytes. In contrast, ACTH1–10, ACTH4–10, ACTH4–11, and ACTH5–12 possessed a weak potency at high doses only (100 and 1,000 nM). These results suggest that ACTH4–12 is the minimal message sequence required to induce the differentiation of mouse epidermal melanocytes in culture completely. The amino acids of Met4 and Pro12 are suggested to be important for its potency. J. Exp. Zool. 286:632–640, 2000. © 2000 Wiley‐Liss, Inc.

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Genetic and Epigenetic Control of the Proliferation and Differentiation of Mouse Epidermal Melanocytes in Culture

Cited by 50 publications

References 114 publications

Tyrp1 and Oculocutaneous Albinism Type 3

Tyrp1 and Oculocutaneous Albinism Type 3

Ferrous Ferric Chloride Induces the Differentiation of Cultured Mouse Epidermal Melanocytes Additionally with Herbal Medicines

ACTH4-12 is the minimal message sequence required to induce the differentiation of mouse epidermal melanocytes in serum-free primary culture

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