Phenotypic Analysis of Meltrin α (ADAM12)-Deficient Mice: Involvement of Meltrin α in Adipogenesis and Myogenesis

REFERENCES

• Asakura, M., M. Kitakaze, S. Takashima, Y. Liao, F. Ishikura, T. Yoshinaka, H. Ohmoto, K. Node, K. Yoshino, H. Ishiguro, H. Asanuma, S. Sanada, Y. Matsumura, H. Takeda, S. Beppu, M. Tada, M. Hori, and S. Higashiyama. 2002. Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nat. Med. 8: 35–40.
   PubMed Web of Science ®Google Scholar
• Black, R. A., C. T. Rauch, C. J. Kozlosky, J. J. Peschon, J. L. Slack, M. F. Wolfson, B. J. Castner, K. L. Stocking, P. Reddy, S. Srinivasan, N. Nelson, N. Boiani, K. A. Schooley, M. Gerhart, R. Davis, J. N. Fitzner, R. S. Johnson, R. J. Paxton, C. J. March, and D. P. Cerretti. 1997. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385: 729–733.
   PubMed Web of Science ®Google Scholar
• Black, R. A., and J. M. White. 1998. ADAMs: focus on the protease domain. Curr. Opin. Cell Biol. 10: 654–659.
   PubMed Web of Science ®Google Scholar
• Blobel, C. P., T. G. Wolfsberg, C. W. Turck, D. G. Myles, P. Primakoff, and J. M. White. 1992. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356: 248–252.
   PubMed Web of Science ®Google Scholar
• Borneman, A., R. Kuschel, and A. Fujisawa-Sehara. 2000. Analysis for transcript expression of meltrin alpha in normal, regenerating, and denervated rat muscle. J. Muscle Res. Cell Motil. 21: 475–480.
   PubMedGoogle Scholar
• Bridges, L. C., P. H. Tani, K. R. Hanson, C. M. Roberts, M. B. Judkins, and R. D. Bowditch. 2002. The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin α4β1. J. Biol. Chem. 277: 3784–3792.
   PubMed Web of Science ®Google Scholar
• Buxbaum, J. D., K. N. Liu, Y. Luo, J. L. Slack, K. L. Stocking, J. J. Peschon, R. S. Johnson, B. J. Castner, D. P. Cerretti, and R. A. Black. 1998. Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273: 27765–27767.
   PubMed Web of Science ®Google Scholar
• Cho, C., D. O. Bunch, J. E. Faure, E. H. Goulding, E. M. Eddy, P. Primakoff, and D. G. Myles. 1998. Fertilization defects in sperm from mice lacking Fertilin β. Science 281: 1857–1859.
   PubMed Web of Science ®Google Scholar
• Dangain, J., and G. Vrbova. 1984. Muscle development in mdx mutant mice. Muscle Nerve 7: 700–704.
   PubMedGoogle Scholar
• Eto, K., W. Puzon-McLaughlin, D. Sheppard, A. Sehara-Fujisawa, X. P. Zhang, and Y. Takada. 2000. RGD-independent binding of integrin alpha9beta1 to the ADAM-12 and -15 disintegrin domains mediates cell-cell interaction. J. Biol. Chem. 275: 34922–34930.
   PubMed Web of Science ®Google Scholar
• Florini, J. R., D. Z. Ewton, and S. A. Coolican. 1996. Growth hormone and the insulin-like growth factor system in myogenesis. Endocrinol. Rev. 17: 481–517.
   PubMed Web of Science ®Google Scholar
• Gilpin, B. J., F. Loechel, M. G. Mattei, E. Engvall, R. Albrechtsen, and U. M. Wewer. 1998. A novel, secreted form of human ADAM 12 (Meltrin α) provokes myogenesis in vivo. J. Biol. Chem. 273: 157–166.
   PubMed Web of Science ®Google Scholar
• Goishi, K., S. Higashiyama, M. Klagsbrun, M. Ishikawa, E. Mekada, and N. Taniguchi. 1995. Phorbol ester induces the rapid processing of cell surface heparin-binding EGF-like growth factor: conversion from juxtacrine to paracrine growth factor activity. Mol. Biol. Cell 6: 967–980.
   PubMedGoogle Scholar
• Hogan, B., R. Beddington, F. Costantini, and E. Lacy. 1994. Manipulating the mouse embryo: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Iba, K., R. Albrechtsen, B. Gilpin, C. Frohlich, F. Loechel, A. Zolkiewska, K. Ishiguro, T. Kojima, W. Liu, J. K. Langford, R. D. Sanderson, C. Brakebusch, R. Fassler, and U. M. Wewer. 2000. The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading. J. Cell Biol. 149: 1143–1156.
   PubMed Web of Science ®Google Scholar
• Kawaguchi, N., X. Xu, R. tajima, P. Kronqvist, C. Sundberg, F. Loechel, R. Albrechtsen, and U. M. Wewer. 2002. ADAM 12 protease induces adipogenesis in transgenic mice. Am. J. Pathol. 160: 1895–1903.
   PubMedGoogle Scholar
• Kurisaki, T., A. Masuda, N. Osumi, Y. Nabeshima, and A. Fujisawa-Sehara. 1998. Spatially- and temporally-restricted expression of meltrin α (ADAM12) and β (ADAM19) in mouse embryo. Mech. Dev. 73: 211–215.
   PubMedGoogle Scholar
• Lieber, T., S. Kidd, and M. W. Young. 2002. Kuzbanian-mediated cleavage of Drosophila Notch. Genes Dev. 16: 209–221.
   PubMedGoogle Scholar
• Loechel, F., J. W. Fox, G. Murphy, R. Albrechtsen, and U. M. Wewer. 2000. ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3. Biochem. Biophys. Res. Commun. 278: 511–515.
   PubMed Web of Science ®Google Scholar
• Lyon, M. F., Y. Cocking, and X. Gao. 1996. Mouse chromosome atlas. Mouse Genome 95: 731–798.
   Google Scholar
• Matsuda, Y., Y. N. Harada, S. Natsuume-Sakai, K. Lee, T. Shiomi, and V. M. Chapman. 1992. Location of the mouse complement factor H gene (cfh) by FISH analysis and replication R-banding. Cytogenet. Cell Genet. 61: 282–285.
   PubMedGoogle Scholar
• Matsuda, Y., T. Imai, T. Shiomi, T. Saito, M. Yamauchi, T. Fukao, Y. Akao, N. Seki, H. Ito, and T. A. Hori. 1996. Comparative genome mapping of the ataxia-telangiectasia region in mouse, rat, and Syrian hamster. Genomics 34: 347–352.
   PubMedGoogle Scholar
• Moss, M. L., S. L. Jin, M. E. Milla, D. M. Bickett, W. Burkhart, H. L. Carter, W. J. Chen, W. C. Clay, J. R. Didsbury, D. Hassler, C. R. Hoffman, T. A. Kost, M. H. Lambert, M. A. Leesnitzer, P. McCauley, G. McGeehan, J. Mitchell, M. Moyer, G. Pahel, W. Rocque, L. K. Overton, F. Schoenen, T. Seaton, J. L. Su, J. D. Becherer, et al. 1997. Cloning of a disintegrin metalloproteinase that processes precursor tumour necrosis factor-alpha. Nature 385: 733–736.
   PubMed Web of Science ®Google Scholar
• Musaro, A., K. McCullagh, A. Paul, L. Houghton, G. Dobrowolny, M. Molinaro, E. R. Barton, H. L. Sweeney, and N. Rosenthal. 2001. Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle. Nat. Genet. 27: 195–200.
   PubMed Web of Science ®Google Scholar
• Musaro, A., K. J. McCullagh, F. J. Naya, E. N. Olson, and N. Rosenthal. 1999. IGF-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NF-ATc1. Nature 400: 581–585.
   PubMed Web of Science ®Google Scholar
• Nagy, A., J. Rossant, R. Nagy, W. Abramow-Newerly, and J. C. Roder. 1993. Derivation of completely cell culture-derived mice from early-passage embryonic stem cells. Proc. Natl. Acad. Sci. USA 90: 8424–8428.
   PubMed Web of Science ®Google Scholar
• Nath, D., P. M. Slocombe, A. Webster, P. E. Stephens, A. J. Docherty, and G. Murphy. 2000. Meltrin γ (ADAM-9) mediates cellular adhesion through α6β1 integrin, leading to a marked induction of fibroblast cell motility. J. Cell Sci. 113(Pt. 12): 2319–2328.
   PubMedGoogle Scholar
• Pan, D., and G. M. Rubin. 1997. Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 90: 271–280.
   PubMed Web of Science ®Google Scholar
• Pittenger, M. F., A. M. Mackay, S. C. Beck, R. K. Jaiswal, R. Douglas, J. D. Mosca, M. A. Moorman, D. W. Simonetti, S. Craig, and D. R. Marshak. 1999. Multilineage potential of adult human mesenchymal stem cells. Science 284: 143–147.
   PubMed Web of Science ®Google Scholar
• Primakoff, P., and D. G. Myles. 2000. The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet. 16: 83–87.
   PubMed Web of Science ®Google Scholar
• Qi, H., M. D. Rand, X. Wu, N. Sestan, W. Wang, P. Rakic, T. Xu, and S. Artavanis-Tsakonas. 1999. Processing of the Notch ligand delta by the metalloprotease Kuzbanian. Science 283: 91–94.
   PubMed Web of Science ®Google Scholar
• Rosen, E. D., and B. M. Spiegelman. 2000. Molecular regulation of adipogenesis. Annu. Rev. Cell Dev. Biol. 16: 145–171.
   PubMed Web of Science ®Google Scholar
• Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Satoh, H., M. C. Yoshida, and M. Sasaki. 1989. High resolution chromosome banding in the Norway rat, Rattus norvegicus. Cytogenet. Cell Genet. 50: 151–154.
   PubMedGoogle Scholar
• Schlondorff, J., and C. P. Blobel. 1999. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding. J. Cell Sci. 112(Pt. 21): 3603–3617.
   PubMed Web of Science ®Google Scholar
• Shi, Z., W. Xu, F. Loechel, U. M. Wewer, and L. J. Murphy. 2000. ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3. J. Biol. Chem. 275: 18574–18580.
   PubMed Web of Science ®Google Scholar
• Shirakabe, K., S. Wakatsuki, T. Kurisaki, and A. Fujisawa-Sehara. 2001. Roles of Meltrin β/ADAM19 in the processing of neuregulin. J. Biol. Chem. 276: 9352–9358.
   PubMed Web of Science ®Google Scholar
• Somssich, I. E., and H. Hameister. 1996. Standard karyotype of early replicating bands (RBG-banding), p. 1450–1451. In M. F. Lyon, S. Rastan, and S. D. M., Brown, (ed.), Genetic variants and strains of the laboratory mouse. Oxford University Press, Oxford, England.
   Google Scholar
• Soriano, P., C. Montgomery, R. Geske, and A. Bradley. 1991. Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell 64: 693–702.
   PubMed Web of Science ®Google Scholar
• Sotillos, S., F. Roch, and S. Campuzano. 1997. The metalloprotease-disintegrin Kuzbanian participates in Notch activation during growth and patterning of Drosophila imaginal discs. Development 124: 4769–4779.
   PubMedGoogle Scholar
• Stedman, H. H., H. L. Sweeney, J. B. Shrager, H. C. Maguire, R. A. Panettieri, B. Petrof, M. Narusawa, J. M. Leferovich, J. T. Sladky, and A. M. Kelly. 1991. The mdx mouse diaphragm reproduces the degenerative changes of Duchenne muscular dystrophy. Nature 352: 536–539.
   PubMed Web of Science ®Google Scholar
• Taylor, S. M., and P. A. Jones. 1979. Multiple new phenotypes induced in 10T1/2 and 3T3 cells treated with 5-azacytidine. Cell 17: 771–779.
   PubMed Web of Science ®Google Scholar
• Turner, A. J., and N. M. Hooper. 1999. Role for ADAM-family proteinases as membrane protein secretases. Biochem. Soc. Trans. 27: 255–259.
   PubMedGoogle Scholar
• Wolfsberg, T. G., P. Primakoff, D. G. Myles, and J. M. White. 1995. ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J. Cell Biol. 131: 275–278.
   PubMed Web of Science ®Google Scholar
• Yagami-Hiromasa, T., T. Sato, T. Kurisaki, K. Kamijo, Y. Nabeshima, and A. Fujisawa-Sehara. 1995. A metalloprotease-disintegrin participating in myoblast fusion. Nature 377: 652–656.
   PubMedGoogle Scholar
• Yagi, T., S. Nada, N. Watanabe, H. Tamemoto, N. Kohmura, Y. Ikawa, and S. Aizawa. 1993. A novel negative selection for homologous recombinants using diphtheria toxin A fragment gene. Anal. Biochem. 214: 77–86.
   PubMedGoogle Scholar
• Yamada, J., T. Kuramoto, and T. Serikawa. 1994. A rat genetic linkage map and comparative maps for mouse or human homologous rat genes. Mamm. Genome 5: 63–83.
   PubMedGoogle Scholar
• Zhou, M., R. Graham, G. Russell, and P. I. Croucher. 2001. MDC-9 (ADAM-9/Meltrin γ) functions as an adhesion molecule by binding the αvβ5 integrin. Biochem. Biophys. Res. Commun. 280: 574–580.
   PubMedGoogle Scholar