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Volumn 19, Issue 5-6, 2008, Pages 415-426

The role of activins and follistatins in skin and hair follicle development and function

Author keywords

Activin; Follistatin; Hair follicle; Skin; Wound healing

Indexed keywords

ACTIVIN; ACTIVIN RECEPTOR; FOLLISTATIN;

EID: 56949095483     PISSN: 13596101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2008.08.005     Document Type: Short Survey
Times cited : (44)

References (77)
  • 1
    • 0033549754 scopus 로고    scopus 로고
    • The biology of hair follicles
    • Paus R., and Cotsarelis G. The biology of hair follicles. N Engl J Med 341 (1999) 491-497
    • (1999) N Engl J Med , vol.341 , pp. 491-497
    • Paus, R.1    Cotsarelis, G.2
  • 3
    • 0026571418 scopus 로고
    • The secret life of the hair follicle
    • Hardy M.H. The secret life of the hair follicle. Trends Genet 8 (1992) 55-61
    • (1992) Trends Genet , vol.8 , pp. 55-61
    • Hardy, M.H.1
  • 4
    • 0024100969 scopus 로고
    • Dermal-epidermal interactions
    • Oliver R.F., and Jahoda C.A. Dermal-epidermal interactions. Clinic Derm 6 (1988) 74-82
    • (1988) Clinic Derm , vol.6 , pp. 74-82
    • Oliver, R.F.1    Jahoda, C.A.2
  • 5
    • 0141726876 scopus 로고    scopus 로고
    • Mechanisms of ectodermal organogenesis
    • Pispa J., and Thesleff I. Mechanisms of ectodermal organogenesis. Dev Biol 262 (2003) 195-205
    • (2003) Dev Biol , vol.262 , pp. 195-205
    • Pispa, J.1    Thesleff, I.2
  • 6
    • 0033593404 scopus 로고    scopus 로고
    • Morphogenesis
    • Hogan B.L. Morphogenesis. Cell 96 (1999) 225-233
    • (1999) Cell , vol.96 , pp. 225-233
    • Hogan, B.L.1
  • 7
    • 0031693463 scopus 로고    scopus 로고
    • Epithelial/mesenchymal interactions and branching morphogenesis of the lung
    • Hogan B.L., and Yingling J.M. Epithelial/mesenchymal interactions and branching morphogenesis of the lung. Curr Opin Genet Dev 8 (1998) 481-486
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 481-486
    • Hogan, B.L.1    Yingling, J.M.2
  • 8
    • 0033995537 scopus 로고    scopus 로고
    • Kidney morphogenesis: cellular and molecular regulation
    • Kuure S., Vuolteenaho R., and Vainio S. Kidney morphogenesis: cellular and molecular regulation. Mech Dev 92 (2000) 31-45
    • (2000) Mech Dev , vol.92 , pp. 31-45
    • Kuure, S.1    Vuolteenaho, R.2    Vainio, S.3
  • 9
    • 0032529168 scopus 로고    scopus 로고
    • Activin is an essential early mesenchymal signal in tooth development that is required for patterning of the murine dentition
    • Ferguson C.A., Tucker A.S., Christensen L., Lau A.L., Matzuk M.M., and Sharpe P.T. Activin is an essential early mesenchymal signal in tooth development that is required for patterning of the murine dentition. Genes Dev 12 (1998) 2636-2649
    • (1998) Genes Dev , vol.12 , pp. 2636-2649
    • Ferguson, C.A.1    Tucker, A.S.2    Christensen, L.3    Lau, A.L.4    Matzuk, M.M.5    Sharpe, P.T.6
  • 10
    • 0036264391 scopus 로고    scopus 로고
    • The role of growth factors in tooth development
    • Thesleff I., and Mikkola M. The role of growth factors in tooth development. Int Rev Cytol 217 (2002) 93-135
    • (2002) Int Rev Cytol , vol.217 , pp. 93-135
    • Thesleff, I.1    Mikkola, M.2
  • 11
    • 0036178229 scopus 로고    scopus 로고
    • Molecular mechanisms regulating hair follicle development
    • Millar S.E. Molecular mechanisms regulating hair follicle development. J Invest Dermatol 118 (2002) 216-225
    • (2002) J Invest Dermatol , vol.118 , pp. 216-225
    • Millar, S.E.1
  • 12
    • 0142056038 scopus 로고    scopus 로고
    • Molecular biology of hair morphogenesis: development and cycling
    • Botchkarev V.A., and Paus R. Molecular biology of hair morphogenesis: development and cycling. J Exper Zool B (Mol Dev Evol) 298 (2003) 164-180
    • (2003) J Exper Zool B (Mol Dev Evol) , vol.298 , pp. 164-180
    • Botchkarev, V.A.1    Paus, R.2
  • 13
    • 39449112659 scopus 로고    scopus 로고
    • BMP signaling in dermal papilla cells is required for their hair follicle-inductive properties
    • Rendl M., Polak L., and Fuchs E. BMP signaling in dermal papilla cells is required for their hair follicle-inductive properties. Genes Dev 15 (2008) 543-557
    • (2008) Genes Dev , vol.15 , pp. 543-557
    • Rendl, M.1    Polak, L.2    Fuchs, E.3
  • 15
    • 0031759310 scopus 로고    scopus 로고
    • Defective whisker follicles and altered brainstem patterns in activin and follistatin knockout mice
    • Jhaveri S., Erzurumlu R.S., Chiaia N., Kumar T.R., and Matzuk M.M. Defective whisker follicles and altered brainstem patterns in activin and follistatin knockout mice. Mol Cell Neurosci 12 (1998) 206-219
    • (1998) Mol Cell Neurosci , vol.12 , pp. 206-219
    • Jhaveri, S.1    Erzurumlu, R.S.2    Chiaia, N.3    Kumar, T.R.4    Matzuk, M.M.5
  • 16
    • 0028929864 scopus 로고
    • Different phenotypes for mice deficient in either activins or activin receptor type II
    • Matzuk M.M., Kumar T.R., and Bradley A. Different phenotypes for mice deficient in either activins or activin receptor type II. Nature 374 (1995) 356-360
    • (1995) Nature , vol.374 , pp. 356-360
    • Matzuk, M.M.1    Kumar, T.R.2    Bradley, A.3
  • 18
    • 0037364579 scopus 로고    scopus 로고
    • Control of pelage hair follicle development and cycling by complex interactions between follistatin and activin
    • Nakamura M., Matzuk M.M., Gerstmayer B., Bosio A., Lauster R., Miyachi Y., et al. Control of pelage hair follicle development and cycling by complex interactions between follistatin and activin. FASEB J 17 (2003) 497-499
    • (2003) FASEB J , vol.17 , pp. 497-499
    • Nakamura, M.1    Matzuk, M.M.2    Gerstmayer, B.3    Bosio, A.4    Lauster, R.5    Miyachi, Y.6
  • 19
    • 33744982427 scopus 로고    scopus 로고
    • Activin signaling and its role in regulation of cell proliferation, apoptosis, and carcinogenesis
    • Chen Y.G., Wang Q., Lin S.L., Chang C.D., Chuang J., and Ying S.Y. Activin signaling and its role in regulation of cell proliferation, apoptosis, and carcinogenesis. Exp Biol Med (Maywood) 231 (2006) 534-544
    • (2006) Exp Biol Med (Maywood) , vol.231 , pp. 534-544
    • Chen, Y.G.1    Wang, Q.2    Lin, S.L.3    Chang, C.D.4    Chuang, J.5    Ying, S.Y.6
  • 20
    • 0023617797 scopus 로고
    • Follistatin specifically inhibits pituitary follicle stimulating hormone release in vitro
    • Ying S.Y., Becker A., Swanson G., Tan P., Ling N., Esch F., et al. Follistatin specifically inhibits pituitary follicle stimulating hormone release in vitro. Biochem Biophys Res Commun 149 (1987) 133-139
    • (1987) Biochem Biophys Res Commun , vol.149 , pp. 133-139
    • Ying, S.Y.1    Becker, A.2    Swanson, G.3    Tan, P.4    Ling, N.5    Esch, F.6
  • 21
    • 0023515180 scopus 로고
    • Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone
    • Ueno N., Ling N., Ying S.Y., Esch F., Shimasaki S., and Guillemin R. Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone. Proc Natl Acad Sci USA 84 (1987) 8282-8286
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8282-8286
    • Ueno, N.1    Ling, N.2    Ying, S.Y.3    Esch, F.4    Shimasaki, S.5    Guillemin, R.6
  • 22
    • 0036486076 scopus 로고    scopus 로고
    • Regulation of cell proliferation, apoptosis, and carcinogenesis by activin
    • Chen Y.G., Lui H.M., Lin S.L., Lee J.M., and Ying S.Y. Regulation of cell proliferation, apoptosis, and carcinogenesis by activin. Exp Biol Med (Maywood) 227 (2002) 75-87
    • (2002) Exp Biol Med (Maywood) , vol.227 , pp. 75-87
    • Chen, Y.G.1    Lui, H.M.2    Lin, S.L.3    Lee, J.M.4    Ying, S.Y.5
  • 23
    • 0028942101 scopus 로고
    • Cloning of a new member of the TGF-beta family: a putative new activin beta C chain
    • Hotten G., Neidhardt H., Schneider C., and Pohl J. Cloning of a new member of the TGF-beta family: a putative new activin beta C chain. Biochem Biophys Res Commun 206 (1995) 608-613
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 608-613
    • Hotten, G.1    Neidhardt, H.2    Schneider, C.3    Pohl, J.4
  • 24
    • 0030015295 scopus 로고    scopus 로고
    • Structural analysis of the mouse activin beta C gene
    • Lau A.L., Nishimori K., and Matzuk M.M. Structural analysis of the mouse activin beta C gene. Biochim Biophys Acta 1307 (1996) 145-148
    • (1996) Biochim Biophys Acta , vol.1307 , pp. 145-148
    • Lau, A.L.1    Nishimori, K.2    Matzuk, M.M.3
  • 25
    • 0029003329 scopus 로고
    • Molecular cloning and functional analysis of a new activin beta subunit: a dorsal mesoderm-inducing activity in Xenopus
    • Oda S., Nishimatsu S., Murakami K., and Ueno N. Molecular cloning and functional analysis of a new activin beta subunit: a dorsal mesoderm-inducing activity in Xenopus. Biochem Biophys Res Commun 210 (1995) 581-588
    • (1995) Biochem Biophys Res Commun , vol.210 , pp. 581-588
    • Oda, S.1    Nishimatsu, S.2    Murakami, K.3    Ueno, N.4
  • 26
    • 0031584814 scopus 로고    scopus 로고
    • Genes coding for mouse activin beta C and beta E are closely linked and exhibit a liver-specific expression pattern in adult tissues
    • Fang J., Wang S.Q., Smiley E., and Bonadio J. Genes coding for mouse activin beta C and beta E are closely linked and exhibit a liver-specific expression pattern in adult tissues. Biochem Biophys Res Commun 24 (1997) 655-661
    • (1997) Biochem Biophys Res Commun , vol.24 , pp. 655-661
    • Fang, J.1    Wang, S.Q.2    Smiley, E.3    Bonadio, J.4
  • 28
    • 0025741546 scopus 로고
    • Follistatin binds to both activin and inhibin through the common subunit
    • Shimonaka M., Inouye S., Shimasaki S., and Ling N. Follistatin binds to both activin and inhibin through the common subunit. Endocrinology 128 (1991) 3313-3315
    • (1991) Endocrinology , vol.128 , pp. 3313-3315
    • Shimonaka, M.1    Inouye, S.2    Shimasaki, S.3    Ling N4
  • 30
    • 0034457429 scopus 로고    scopus 로고
    • Analysis of human follistatin structure: identification of two discontinuous N-terminal sequences coding for activin A binding and structural consequences of activin binding to native proteins
    • Wang Q., Keutmann H.T., Schneyer A.L., and Sluss P.M. Analysis of human follistatin structure: identification of two discontinuous N-terminal sequences coding for activin A binding and structural consequences of activin binding to native proteins. Endocrinology 141 (2000) 3183-3193
    • (2000) Endocrinology , vol.141 , pp. 3183-3193
    • Wang, Q.1    Keutmann, H.T.2    Schneyer, A.L.3    Sluss, P.M.4
  • 32
    • 0023772938 scopus 로고
    • Primary structure of the human follistatin precursor and its genomic organization
    • Shimasaki S., Koga M., Esch F., Cooksey K., Mercado M., Koba A., et al. Primary structure of the human follistatin precursor and its genomic organization. Proc Natl Acad Sci USA 85 (1988) 4218-4222
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4218-4222
    • Shimasaki, S.1    Koga, M.2    Esch, F.3    Cooksey, K.4    Mercado, M.5    Koba, A.6
  • 33
    • 0024299381 scopus 로고
    • Porcine follistatin gene structure supports two forms of mature follistatin produced by alternative splicing
    • Shimasaki S., Koga M., Esch F., Mercado M., Cooksey K., Koba A., et al. Porcine follistatin gene structure supports two forms of mature follistatin produced by alternative splicing. Biochem Biophys Res Commun 152 (1988) 717-723
    • (1988) Biochem Biophys Res Commun , vol.152 , pp. 717-723
    • Shimasaki, S.1    Koga, M.2    Esch, F.3    Mercado, M.4    Cooksey, K.5    Koba, A.6
  • 34
    • 0026014287 scopus 로고
    • Recombinant expression of human follistatin with 315 and 288 amino acids: chemical and biological comparison with native porcine follistatin
    • Inouye S., Guo Y., DePaolo L., Shimonaka M., Ling N., and Shimasaki S. Recombinant expression of human follistatin with 315 and 288 amino acids: chemical and biological comparison with native porcine follistatin. Endocrinology 129 (1991) 815-822
    • (1991) Endocrinology , vol.129 , pp. 815-822
    • Inouye, S.1    Guo, Y.2    DePaolo, L.3    Shimonaka, M.4    Ling, N.5    Shimasaki, S.6
  • 35
    • 27844569857 scopus 로고    scopus 로고
    • Too many follistatins: racing inside and getting out of the cell
    • Kumar T.R. Too many follistatins: racing inside and getting out of the cell. Endocrinology 146 (2005) 5048-5051
    • (2005) Endocrinology , vol.146 , pp. 5048-5051
    • Kumar, T.R.1
  • 36
  • 38
    • 0034731508 scopus 로고    scopus 로고
    • Identification and characterization of a novel follistatin-like protein as a binding protein for the TGF-beta family
    • Tsuchida K., Arai K.Y., Kuramoto Y., Yamakawa N., Hasegawa Y., and Sugino H. Identification and characterization of a novel follistatin-like protein as a binding protein for the TGF-beta family. J Biol Chem 275 (2000) 40788-40796
    • (2000) J Biol Chem , vol.275 , pp. 40788-40796
    • Tsuchida, K.1    Arai, K.Y.2    Kuramoto, Y.3    Yamakawa, N.4    Hasegawa, Y.5    Sugino, H.6
  • 39
    • 0036790467 scopus 로고    scopus 로고
    • Activins, inhibins, and follistatins: from endocrinology to signaling A paradigm for the new millennium
    • Welt C., Sidis Y., Keutmann H., and Schneyer A. Activins, inhibins, and follistatins: from endocrinology to signaling A paradigm for the new millennium. Exp Biol Med (Maywood) 227 (2002) 724-752
    • (2002) Exp Biol Med (Maywood) , vol.227 , pp. 724-752
    • Welt, C.1    Sidis, Y.2    Keutmann, H.3    Schneyer, A.4
  • 40
    • 0038642113 scopus 로고    scopus 로고
    • Cripto forms a complex with activin and type II activin receptors and can block activin signalling
    • Gray P.C., Harrison C.A., and Vale W. Cripto forms a complex with activin and type II activin receptors and can block activin signalling. Proc Natl Acad Sci USA 100 (2003) 5193-5198
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5193-5198
    • Gray, P.C.1    Harrison, C.A.2    Vale, W.3
  • 41
    • 0031685620 scopus 로고    scopus 로고
    • TGF-beta signal transduction
    • Massague J. TGF-beta signal transduction. Annu Rev Biochem 67 (1998) 753-791
    • (1998) Annu Rev Biochem , vol.67 , pp. 753-791
    • Massague, J.1
  • 42
    • 0034654497 scopus 로고    scopus 로고
    • Controlling TGF-beta signaling
    • Massague J., and Chen Y.G. Controlling TGF-beta signaling. Genes Dev 14 (2000) 627-644
    • (2000) Genes Dev , vol.14 , pp. 627-644
    • Massague, J.1    Chen, Y.G.2
  • 43
    • 23044466047 scopus 로고    scopus 로고
    • Specificity and versatility in TGF-beta signaling through Smads
    • Feng X.H., and Derynck R. Specificity and versatility in TGF-beta signaling through Smads. Annu Rev Cell Dev Biol 21 (2005) 659-693
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 659-693
    • Feng, X.H.1    Derynck, R.2
  • 45
    • 0028931686 scopus 로고
    • Signaling activity of homologous and heterologous transforming growth factor-beta receptor kinase complexes
    • Vivien D., Attisano L., Wrana J.L., and Massague J. Signaling activity of homologous and heterologous transforming growth factor-beta receptor kinase complexes. J Biol Chem 270 (1995) 7134-7141
    • (1995) J Biol Chem , vol.270 , pp. 7134-7141
    • Vivien, D.1    Attisano, L.2    Wrana, J.L.3    Massague J4
  • 46
    • 0028876138 scopus 로고
    • Ligand-induced recruitment and phosphorylation of reduced TGF-beta type I receptor
    • Vivien D., and Wrana J.L. Ligand-induced recruitment and phosphorylation of reduced TGF-beta type I receptor. Exp Cell Res 221 (1995) 60-65
    • (1995) Exp Cell Res , vol.221 , pp. 60-65
    • Vivien, D.1    Wrana, J.L.2
  • 47
    • 0029834067 scopus 로고    scopus 로고
    • Partnership between DPC4 and SMAD proteins in TGF-beta signalling pathways
    • Lagna G., Hata A., Hemmati-Brivanlou A., and Massague J. Partnership between DPC4 and SMAD proteins in TGF-beta signalling pathways. Nature 383 (1996) 832-836
    • (1996) Nature , vol.383 , pp. 832-836
    • Lagna, G.1    Hata, A.2    Hemmati-Brivanlou, A.3    Massague, J.4
  • 48
    • 0031438047 scopus 로고    scopus 로고
    • TGF-beta signalling from cell membrane to nucleus through SMAD proteins
    • Heldin C.H., Miyazono K., and ten Dijke P. TGF-beta signalling from cell membrane to nucleus through SMAD proteins. Nature 390 (1997) 465-471
    • (1997) Nature , vol.390 , pp. 465-471
    • Heldin, C.H.1    Miyazono, K.2    ten Dijke, P.3
  • 49
    • 0029003377 scopus 로고
    • Osteogenic protein-1 binds to activin type II receptors and induces certain activin-like effects
    • Yamashita H., ten Dijke P., Huylebroeck D., Sampath T.K., Andries M., Smith J.C., et al. Osteogenic protein-1 binds to activin type II receptors and induces certain activin-like effects. J Cell Biol 130 (1995) 217-226
    • (1995) J Cell Biol , vol.130 , pp. 217-226
    • Yamashita, H.1    ten Dijke, P.2    Huylebroeck, D.3    Sampath, T.K.4    Andries, M.5    Smith, J.C.6
  • 50
    • 0032482928 scopus 로고    scopus 로고
    • Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo
    • Iemura S., Yamamoto T.S., Takagi C., Uchiyama H., Natsume T., Shimasaki S., et al. Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo. Proc Natl Acad Sci USA 95 (1998) 9337-9342
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9337-9342
    • Iemura, S.1    Yamamoto, T.S.2    Takagi, C.3    Uchiyama, H.4    Natsume, T.5    Shimasaki, S.6
  • 53
    • 0035829654 scopus 로고    scopus 로고
    • The Mad1 transcription factor is a novel target of activin and TGF-beta action in keratinocytes: possible role of Mad1 in wound repair and psoriasis
    • Werner S., Beer H.D., Mauch C., and Luscher B. The Mad1 transcription factor is a novel target of activin and TGF-beta action in keratinocytes: possible role of Mad1 in wound repair and psoriasis. Oncogene 20 (2001) 7494-7504
    • (2001) Oncogene , vol.20 , pp. 7494-7504
    • Werner, S.1    Beer, H.D.2    Mauch, C.3    Luscher, B.4
  • 54
    • 0344054050 scopus 로고    scopus 로고
    • A comprehensive guide for the recognition and classification of distinct stages of hair follicle morphogenesis
    • Paus R., Muller-Rover S., Van Der Veen C., Maurer M., Eichmuller S., Ling G., et al. A comprehensive guide for the recognition and classification of distinct stages of hair follicle morphogenesis. J Invest Dermatol 113 (1999) 523-532
    • (1999) J Invest Dermatol , vol.113 , pp. 523-532
    • Paus, R.1    Muller-Rover, S.2    Van Der Veen, C.3    Maurer, M.4    Eichmuller, S.5    Ling, G.6
  • 55
    • 34248527846 scopus 로고
    • The coat of the mouse (Mus musculus)
    • Dry F.W. The coat of the mouse (Mus musculus). J Genet 16 (1929) 287-340
    • (1929) J Genet , vol.16 , pp. 287-340
    • Dry, F.W.1
  • 56
    • 0001553080 scopus 로고
    • The development of mouse hair in vitro with some observations on pigmentation
    • Hardy M.H. The development of mouse hair in vitro with some observations on pigmentation. J Anat 83 (1949) 364-384
    • (1949) J Anat , vol.83 , pp. 364-384
    • Hardy, M.H.1
  • 57
    • 84981823392 scopus 로고
    • Prenatal formation of hair follicle types
    • Mann S.J. Prenatal formation of hair follicle types. Anat Rec 144 (1962) 135-142
    • (1962) Anat Rec , vol.144 , pp. 135-142
    • Mann, S.J.1
  • 58
    • 0030390495 scopus 로고    scopus 로고
    • Changing patterns of cell adhesion molecules during mouse pelage hair follicle development. 1. Follicle morphogenesis in wild-type mice
    • Hardy M.H., and Vielkind U. Changing patterns of cell adhesion molecules during mouse pelage hair follicle development. 1. Follicle morphogenesis in wild-type mice. Acta Anat (Basel) 157 (1996) 169-182
    • (1996) Acta Anat (Basel) , vol.157 , pp. 169-182
    • Hardy, M.H.1    Vielkind, U.2
  • 59
    • 0028156743 scopus 로고
    • Expression of messenger ribonucleic acids encoding the inhibin/activin system during mid- and late-gestation rat embryogenesis
    • Roberts V.J., and Barth S.L. Expression of messenger ribonucleic acids encoding the inhibin/activin system during mid- and late-gestation rat embryogenesis. Endocrinology 134 (1994) 914-923
    • (1994) Endocrinology , vol.134 , pp. 914-923
    • Roberts, V.J.1    Barth, S.L.2
  • 61
    • 0342902626 scopus 로고    scopus 로고
    • Strong induction of activin expression after injury suggests an important role of activin in wound repair
    • Hubner G., Hu Q., Smola H., and Werner S. Strong induction of activin expression after injury suggests an important role of activin in wound repair. Dev Biol 173 (1996) 490-498
    • (1996) Dev Biol , vol.173 , pp. 490-498
    • Hubner, G.1    Hu, Q.2    Smola, H.3    Werner, S.4
  • 62
    • 0034524132 scopus 로고    scopus 로고
    • The Myc/Max/Mad network and the transcriptional control of cell behavior
    • Grandori C., Cowley S.M., James L.P., and Eisenman R.N. The Myc/Max/Mad network and the transcriptional control of cell behavior. Annu Rev Cell Dev Biol 16 (2000) 653-699
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 653-699
    • Grandori, C.1    Cowley, S.M.2    James, L.P.3    Eisenman, R.N.4
  • 63
    • 0028176755 scopus 로고
    • Activin/inhibin beta B subunit gene disruption leads to defects in eyelid development and female reproduction
    • Vassalli A., Matzuk M.M., Gardner H.A., Lee K.F., and Jaenisch R. Activin/inhibin beta B subunit gene disruption leads to defects in eyelid development and female reproduction. Genes Dev 8 (1994) 414-427
    • (1994) Genes Dev , vol.8 , pp. 414-427
    • Vassalli, A.1    Matzuk, M.M.2    Gardner, H.A.3    Lee, K.F.4    Jaenisch, R.5
  • 64
    • 0028918915 scopus 로고
    • Multiple defects and perinatal death in mice deficient in follistatin
    • Matzuk M.M., Lu N., Vogel H., Sellheyer K., Roop D.R., and Bradley A. Multiple defects and perinatal death in mice deficient in follistatin. Nature 374 (1995) 360-363
    • (1995) Nature , vol.374 , pp. 360-363
    • Matzuk, M.M.1    Lu, N.2    Vogel, H.3    Sellheyer, K.4    Roop, D.R.5    Bradley, A.6
  • 65
    • 24044509109 scopus 로고    scopus 로고
    • Activin controls skin morphogenesis and wound repair predominantly via stromal cells and in a concentration-dependent manner via keratinocytes
    • Bamberger C., Scharer A., Antsiferova M., Tychsen B., Pankow S., and Muller M. Activin controls skin morphogenesis and wound repair predominantly via stromal cells and in a concentration-dependent manner via keratinocytes. Am J Pathol 167 (2005) 733-747
    • (2005) Am J Pathol , vol.167 , pp. 733-747
    • Bamberger, C.1    Scharer, A.2    Antsiferova, M.3    Tychsen, B.4    Pankow, S.5    Muller, M.6
  • 66
    • 0029743671 scopus 로고    scopus 로고
    • Tissue-specific binding of radiolabeled activin A by activin receptors and follistatin in postimplantation rat and mouse embryos
    • Roberts V.J., Bentley C.A., Guo Q., Matzuk M.M., and Woodruff T.K. Tissue-specific binding of radiolabeled activin A by activin receptors and follistatin in postimplantation rat and mouse embryos. Endocrinology 137 (1996) 4201-4209
    • (1996) Endocrinology , vol.137 , pp. 4201-4209
    • Roberts, V.J.1    Bentley, C.A.2    Guo, Q.3    Matzuk, M.M.4    Woodruff, T.K.5
  • 67
    • 0035477312 scopus 로고    scopus 로고
    • impaired wound healing in transgenic mice overexpressing the activin antagonist follistatin in the epidermis
    • Wankell M., Munz B., Hubner G., Hans W., Wolf E., Goppelt A., et al. impaired wound healing in transgenic mice overexpressing the activin antagonist follistatin in the epidermis. EMBO J 20 (2001) 5361-5372
    • (2001) EMBO J , vol.20 , pp. 5361-5372
    • Wankell, M.1    Munz, B.2    Hubner, G.3    Hans, W.4    Wolf, E.5    Goppelt, A.6
  • 68
    • 0033214191 scopus 로고    scopus 로고
    • Overexpression of activin A in the skin of transgenic mice reveals new activities of activin in epidermal morphogenesis, dermal fibrosis and wound repair
    • Munz B., Smola H., Engelhardt F., Bleuel K., Brauchle M., Lein I., et al. Overexpression of activin A in the skin of transgenic mice reveals new activities of activin in epidermal morphogenesis, dermal fibrosis and wound repair. EMBO J 18 (1999) 5205-5215
    • (1999) EMBO J , vol.18 , pp. 5205-5215
    • Munz, B.1    Smola, H.2    Engelhardt, F.3    Bleuel, K.4    Brauchle, M.5    Lein, I.6
  • 69
    • 0027178459 scopus 로고
    • Inhibition of skin development by overexpression of transforming growth factor beta 1 in the epidermis of transgenic mice
    • Sellheyer K., Bickenbach J.R., Rothnagel J.A., Bundman D., Longley M.A., Krieg T., et al. Inhibition of skin development by overexpression of transforming growth factor beta 1 in the epidermis of transgenic mice. Proc Natl Acad Sci USA 90 (1993) 5237-5241
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5237-5241
    • Sellheyer, K.1    Bickenbach, J.R.2    Rothnagel, J.A.3    Bundman, D.4    Longley, M.A.5    Krieg, T.6
  • 70
    • 0000425845 scopus 로고
    • Tissue-specific and differentiation-specific expression of a human K14 keratin gene in transgenic mice
    • Vassar R., Rosenberg M., Ross S., Tyner A., and Fuchs E. Tissue-specific and differentiation-specific expression of a human K14 keratin gene in transgenic mice. Proc Natl Acad Sci USA 86 (1989) 1563-1567
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1563-1567
    • Vassar, R.1    Rosenberg, M.2    Ross, S.3    Tyner, A.4    Fuchs, E.5
  • 72
    • 33846426443 scopus 로고    scopus 로고
    • Profiling of genes differentially expressed in a rat of early and later gestational ages with high-density oligonucleotide DNA array
    • Chen W., Fu X., Ge S., Sun T., Zhou G., Han B., et al. Profiling of genes differentially expressed in a rat of early and later gestational ages with high-density oligonucleotide DNA array. Wound Repair Regen 15 (2007) 147-155
    • (2007) Wound Repair Regen , vol.15 , pp. 147-155
    • Chen, W.1    Fu, X.2    Ge, S.3    Sun, T.4    Zhou, G.5    Han, B.6
  • 73
    • 4644356541 scopus 로고    scopus 로고
    • Activin: an important regulator of wound repair, fibrosis, and neuroprotection
    • Sulyok S., Wankell M., Alzheimer C., and Werner S. Activin: an important regulator of wound repair, fibrosis, and neuroprotection. Mol Cell Endocrinol 225 (2004) 127-132
    • (2004) Mol Cell Endocrinol , vol.225 , pp. 127-132
    • Sulyok, S.1    Wankell, M.2    Alzheimer, C.3    Werner, S.4
  • 75
    • 2942516214 scopus 로고    scopus 로고
    • Wounds increase activin in skin and a vasoactive neuropeptide in sensory ganglia
    • Cruise B.A., Xu P., and Hall A.K. Wounds increase activin in skin and a vasoactive neuropeptide in sensory ganglia. Dev Biol 271 (2004) 1-10
    • (2004) Dev Biol , vol.271 , pp. 1-10
    • Cruise, B.A.1    Xu, P.2    Hall, A.K.3
  • 76
    • 34250782560 scopus 로고    scopus 로고
    • Imbalance between activin A and follistatin drives postburn hypertrophic scar formation in human skin
    • Fumagalli M., Musso T., Vermi W., Scutera S., Daniele R., Alotto D., et al. Imbalance between activin A and follistatin drives postburn hypertrophic scar formation in human skin. Exp Dermatol 16 (2007) 600-610
    • (2007) Exp Dermatol , vol.16 , pp. 600-610
    • Fumagalli, M.1    Musso, T.2    Vermi, W.3    Scutera, S.4    Daniele, R.5    Alotto, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.