Ae binding protein 1
AE binding protein 1 is a protein that in humans is encoded by the AEBP1 gene.[1]
Function
Function
AE binding protein 1 is a member of carboxypeptidase A protein family. The protein may function as a transcriptional repressor and play a role in adipogenesis and smooth muscle cell differentiation. Studies in mice suggest that the AEBP1 gene that encodes the protein functions in wound healing and abdominal wall development. Overexpression of this gene is associated with glioblastoma.[1]
External links
External links
- Human AEBP1 genome location and AEBP1 gene details page in the UCSC Genome Browser.
Further reading
Further reading
- Tumelty KE, Smith BD, Nugent MA, Layne MD (2014). “Aortic carboxypeptidase-like protein (ACLP) enhances lung myofibroblast differentiation through transforming growth factor β receptor-dependent and -independent pathways”. Journal of Biological Chemistry. 289 (5): 2526–36. doi:10.1074/jbc.M113.502617. PMC 3908388. PMID 24344132.
- Lyons PJ, Muise AM, Ro HS (2005). “MAPK modulates the DNA binding of adipocyte enhancer-binding protein 1”. Biochemistry. 44 (3): 926–31. doi:10.1021/bi0480178. PMID 15654748.
- Majdalawieh A, Ro HS (2010). “PPARgamma1 and LXRalpha face a new regulator of macrophage cholesterol homeostasis and inflammatory responsiveness, AEBP1”. Nuclear Receptor Signaling. 8: e004. doi:10.1621/nrs.08004. PMC 2858268. PMID 20419060.
- Muise AM, Ro HS (1999). “Enzymic characterization of a novel member of the regulatory B-like carboxypeptidase with transcriptional repression function: Stimulation of enzymic activity by its target DNA”. The Biochemical Journal. 343 (2): 341–5. doi:10.1042/0264-6021:3430341. PMC 1220559. PMID 10510298.
- Feldkamp ML, Bowles NE, Botto LD (2012). “AEBP1 gene variants in infants with gastroschisis”. Birth Defects Research Part A: Clinical and Molecular Teratology. 94 (9): 738–42. doi:10.1002/bdra.23041. PMID 22821744.
- Layne MD, Yet SF, Maemura K, Hsieh CM, Bernfield M, Perrella MA, Lee ME (2001). “Impaired abdominal wall development and deficient wound healing in mice lacking aortic carboxypeptidase-like protein”. Molecular and Cellular Biology. 21 (15): 5256–61. doi:10.1128/MCB.21.15.5256-5261.2001. PMC 87249. PMID 11438679.
- Ohno I, Hashimoto J, Shimizu K, Takaoka K, Ochi T, Matsubara K, Okubo K (1996). “A cDNA cloning of human AEBP1 from primary cultured osteoblasts and its expression in a differentiating osteoblastic cell line”. Biochemical and Biophysical Research Communications. 228 (2): 411–4. doi:10.1006/bbrc.1996.1675. PMID 8920928.
- Majdalawieh A, Ro HS (2010). “Regulation of Ikappa Balpha function and NF-kappaB signaling: AEBP1 is a novel proinflammatory mediator in macrophages”. Mediators of Inflammation. 2010: 823821. doi:10.1155/2010/823821. PMC 2855089. PMID 20396415.
- Song L, Fricker LD (1997). “Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase”. The Journal of Biological Chemistry. 272 (16): 10543–50. doi:10.1074/jbc.272.16.10543. PMID 9099699.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Looking for the patient version?
© 2026 MyEClinic – IFTM Institut für Telematik in der Medizin GmbH