Disease relevance of AEBP1

• The role of AEBP1 in sex-specific diet-induced obesity [1].
• Here we show that transgenic overexpression of AEBP1 during adipogenesis coupled with a high-fat diet (HFD) resulted in massive obesity in female transgenic (AEBP1(TG)) mice via adipocyte hyperplasia [1].
• The majority of ACLP(-/-) mice die perinatally due to gastroschisis, a severe disruption of the anterior abdominal wall and herniation of the abdominal organs [2].

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

• The DNA binding domain of AEBP1 was mapped by electrophoretic mobility shift assays to a region of the C-terminus rich in basic residues [6].

References