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AEBP1  -  AE binding protein 1

Homo sapiens

Synonyms: ACLP, AE-binding protein 1, Adipocyte enhancer-binding protein 1, Aortic carboxypeptidase-like protein
 
 
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Disease relevance of AEBP1

 

High impact information on AEBP1

  • Following injury by a dermal punch biopsy, ACLP(-/-) mice exhibited deficient wound healing compared with controls [2].
  • In addition, dermal fibroblasts isolated from ACLP(-/-) 18.5-day-postconception embryos exhibited a reduced proliferative capacity compared with wild-type cells [2].
  • These results indicate that ACLP is an ECM protein that is essential for embryonic development and dermal wound healing processes [2].
  • In cultured mouse aortic smooth muscle cells, ACLP mRNA and protein were up-regulated 2-3-fold after serum starvation [3].
  • These results indicate that ACLP may play a role in differentiated vascular smooth muscle cells [3].
 

Chemical compound and disease context of AEBP1

  • Our results suggest that AEBP1 plays a key functional role in in vivo modulation of adiposity via fat-cell proliferation and is involved in a sex-specific susceptibility to diet-induced obesity by the estrogen signaling pathway [1].
 

Biological context of AEBP1

  • A northern hybridization showed that in the differentiating murine osteoblastic cell line, AEBP1 is also expressed but that it is shut off in the final calcification phase, suggesting a transcriptional repressive effect on genes for bone formation [4].
  • The 50-kDa subunit is a member of the regulatory B-type carboxypeptidase family, which includes carboxypeptidases M, E/H, AEBP1, and a newly described member, carboxypeptidase D, which has three tandem active site domains [5].
  • Adipocyte enhancer binding protein 1 (AEBP1) is a transcriptional repressor of the aP2 gene, which encodes the adipocyte lipid binding protein and is involved in the differentiation of preadipocytes into mature adipocytes [6].
 

Anatomical context of AEBP1

  • This cDNA clone encodes a 845-amino acid protein that is almost identical to the mouse adipocyte transcription factor AEBP1 except that it has additional 105 amino acids in the N terminus [4].
  • A cDNA cloning of human AEBP1 from primary cultured osteoblasts and its expression in a differentiating osteoblastic cell line [4].
  • However, the distribution of CPZ and AEBP1 differ in pituitary and thyroid [7].
  • ACLP was expressed predominantly in the smooth muscle cells of the adult mouse aorta but not in the adventitia or in several other tissues [3].
  • Using a recently developed neural crest cell to smooth muscle cell in vitro differentiation system, we found that ACLP mRNA and protein were not expressed in neural crest cells but were up-regulated dramatically with the differentiation of these cells [3].
 

Other interactions of AEBP1

  • Like AEBP1 and CPX-2, CPX-1 contains an N-terminal region of 160 amino acids with sequence similarity to the discoidin domain of a variety of proteins [8].
  • Thus, HFD-fed AEBP1(TG) females display hyperinduction of AEBP1 and a marked reduction of PTEN level with concomitant hyperactivation of the survival signal in white adipose tissue [1].
 

Analytical, diagnostic and therapeutic context of AEBP1

References

  1. The role of AEBP1 in sex-specific diet-induced obesity. Zhang, L., Reidy, S.P., Nicholson, T.E., Lee, H.J., Majdalawieh, A., Webber, C., Stewart, B.R., Dolphin, P., Ro, H.S. Mol. Med. (2005) [Pubmed]
  2. Impaired abdominal wall development and deficient wound healing in mice lacking aortic carboxypeptidase-like protein. Layne, M.D., Yet, S.F., Maemura, K., Hsieh, C.M., Bernfield, M., Perrella, M.A., Lee, M.E. Mol. Cell. Biol. (2001) [Pubmed]
  3. Aortic carboxypeptidase-like protein, a novel protein with discoidin and carboxypeptidase-like domains, is up-regulated during vascular smooth muscle cell differentiation. Layne, M.D., Endege, W.O., Jain, M.K., Yet, S.F., Hsieh, C.M., Chin, M.T., Perrella, M.A., Blanar, M.A., Haber, E., Lee, M.E. J. Biol. Chem. (1998) [Pubmed]
  4. A cDNA cloning of human AEBP1 from primary cultured osteoblasts and its expression in a differentiating osteoblastic cell line. Ohno, I., Hashimoto, J., Shimizu, K., Takaoka, K., Ochi, T., Matsubara, K., Okubo, K. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  5. Chromosomal localization of the genes for human carboxypeptidase D (CPD) and the active 50-kilodalton subunit of human carboxypeptidase N (CPN1). Riley, D.A., Tan, F., Miletich, D.J., Skidgel, R.A. Genomics (1998) [Pubmed]
  6. Modeling and functional analysis of AEBP1, a transcriptional repressor. Lyons, P.J., Mattatall, N.R., Ro, H.S. Proteins (2006) [Pubmed]
  7. Cloning, sequence analysis, and distribution of rat metallocarboxypeptidase Z. Xin, X., Day, R., Dong, W., Lei, Y., Fricker, L.D. DNA Cell Biol. (1998) [Pubmed]
  8. Identification of mouse CPX-1, a novel member of the metallocarboxypeptidase gene family with highest similarity to CPX-2. Lei, Y., Xin, X., Morgan, D., Pintar, J.E., Fricker, L.D. DNA Cell Biol. (1999) [Pubmed]
 
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