Angiotensin I Converting Enzyme (ACE, also known as peptidyl-dipeptidase A, kininase II, or CD143) is a type I transmembrane zinc metallopeptidase that is important in the metabolism of the vaso-active peptides angiotensin II and bradykinin (1, 2). Two isoforms of ACE that exhibit distinct physiologic functions have been described: germinally expressed ACE (gACE) and somatic cell expressed ACE (sACE) (2,3). Both isoforms are transcribed from a single gene using alternative promoters (2, 3). The gACE isoform is exclusively expressed in the testes, whereas sACE is expressed on endothelial cells, epithelial cells, neuronal cells, and dendritic cells (4, 5). A soluble form of CD143 is likely shed from endothelial cells and is found in serum, plasma, seminal fluid, amniotic fluid and cerebral spinal fluid (1). Functionally, CD143 has a role in blood pressure regulation, electrolyte balance, reproduction, cardiovascular disease, kidney disease, cancer and Alzheimer’s disease (6 - 10). Inhibitors of ACE are used clinically to treat hypertension, cardiac failure, and diabetic retinopathy (6, 11).
1. Corvol, P. and T.A. Williams (1998) in Handbook of Proteolytic Enzymes, Barrett, A.J. et al. eds., Academic Press, San Diego, pp. 1066 - 1076. 2. Soubrier, F. et al. (1988) Proc. Natl. Acad. Sci. USA 85:9386. 3. Hubert, C. et al. (1991) J. Biol. Chem. 266:15377. 4. Balyasnikova, I.V. et al. (2003) Tissue Antigens 61:49. 5. Danilov, S.M. et al. (2003) Exp. Hematol. 31:1301. 6. Eriksson, U. et al. (2002) Curr. Biol. 12:R745. 7. Metzger, R. et al. (1999) Kidney Int. 56:1442. 8. Metzger, R. et al. (2000) Atherosclerosis 150:21. 9. Bauvois, B. (2004) Oncogene 23:317. 10. Hu, J. et al. (2001) J. Biol. Chem. 276:47863. 11. Turner, A.J. and N.M. Hooper (2002) Trends Pharmacol.
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