+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Phenotypic analysis of Meltrin alpha (ADAM12)-deficient mice: involvement of Meltrin alpha in adipogenesis and myogenesis



Phenotypic analysis of Meltrin alpha (ADAM12)-deficient mice: involvement of Meltrin alpha in adipogenesis and myogenesis



Molecular and Cellular Biology 23(1): 55-61



Meltrin alpha (ADAM12) is a metalloprotease-disintegrin whose specific expression patterns during development suggest that it is involved in myogenesis and the development of other organs. To determine the roles Meltrin alpha plays in vivo, we generated Meltrin alpha-deficient mice by gene targeting. Although the number of homozygous embryos are close to the expected Mendelian ratio at embryonic days 17 to 18, ca. 30% of the null pups born die before weaning, mostly within 1 week of birth. The viable homozygous mutants appear normal and are fertile. Most of the muscles in the homozygous mutants appear normal, and regeneration in experimentally damaged skeletal muscle is unimpeded. In some Meltrin alpha-deficient pups, the interscapular brown adipose tissue is reduced, although the penetrance of this phenotype is low. Impaired formation of the neck and interscapular muscles is also seen in some homozygotes. These observations suggest Meltrin alpha may be involved in regulating adipogenesis and myogenesis through a linked developmental pathway. Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a candidate substrate of Meltrin alpha, and we found that TPA (12-O-tetradecanoylphorbol-13-acetate)-induced ectodomain shedding of HB-EGF is markedly reduced in embryonic fibroblasts prepared from Meltrin alpha-deficient mice. We also report here the chromosomal locations of Meltrin alpha in the mouse and rat.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 046973785

Download citation: RISBibTeXText

PMID: 12482960


Related references

Phenotypic Analysis of Meltrin a (ADAM12)-Deficient Mice: Involvement of Meltrin a in Adipogenesis and Myogenesis. Molecular and Cellular Biology 23(1): 61, 2003

Phenotypic Analysis of Meltrin (Adam12)-Deficient Mice: Involvement of Meltrin in Adipogenesis and Myogenesis. Molecular and Cellular Biology 23(1): 55-61, 2003

Endogenous meltrin alpha is ubiquitously expressed and associated with the plasma membrane but exogenous meltrin alpha is retained in the endoplasmic reticulum. Journal of Biochemistry 128(6): 941-949, 2000

Role of meltrin {alpha} (ADAM12) in obesity induced by high- fat diet. Endocrinology 146(4): 1752-1763, 2005

The expression of ADAM12 (meltrin alpha) in human giant cell tumours of bone. Molecular Pathology 55(6): 394-397, 2002

Expression of ADAM12 (Meltrin-alpha) gene in giant cell tumor of bone. Zhonghua Bing Li Xue Za Zhi 30(5): 350-352, 2001

A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo. Journal of Biological Chemistry 273(1): 157-166, 1998

PACSIN3 binds ADAM12/meltrin alpha and up-regulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor. Journal of Biological Chemistry 278(46): 46029-46034, 2003

Endogenous Meltrin Is Ubiquitously Expressed and Associated with the Plasma Membrane but Exogenous Meltrin Is Retained in the Endoplasmic Reticulum. Journal of Biochemistry 128(6): 941-949, 2000

Analysis for transcript expression of meltrin alpha in normal, regenerating, and denervated rat muscle. Journal of Muscle Research and Cell Motility 21(5): 475-480, 2000

Human ADAM 12 (meltrin alpha) is an active metalloprotease. Journal of Biological Chemistry 273(27): 16993-7, 1998

Expression of meltrin-alpha mRNA is not restricted to fusagenic cells. Journal of Cellular Biochemistry 67(1): 136-142, 1997

Meltrin-alpha, a novel metalloprotease-disintegrin, participates in myotube formation. Cell Structure & Function 20(6): 585, 1995

Identification of meltrin alpha cytoplasmic domain-binding proteins. Cell Structure & Function 26(5): 416, 2001

Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src. Oncogene 19(51): 5842-5850, 2000