Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, elastase 3A has little elastolytic activity. Like most of the human elastases, elastase 3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. Elastase 3A preferentially cleaves proteins after alanine residues. Elastase 3A may also function in the intestinal transport and metabolism of cholesterol. Both elastase 3A and elastase 3B have been referred to as protease E and as elastase 1.[7]
^Shirasu Y, Takemura K, Yoshida H, Sato Y, Iijima H, Shimada Y, Mikayama T, Ozawa T, Ikeda N, Ishida A, et al. (Dec 1988). "Molecular cloning of complementary DNA encoding one of the human pancreatic protease E isozymes". J Biochem. 104 (2): 259–64. doi:10.1093/oxfordjournals.jbchem.a122454. PMID2460440.
Shimada S, Yamaguchi K, Takahashi M, Ogawa M (2002). "Pancreatic elastase IIIA and its variants are expressed in pancreatic carcinoma cells". Int. J. Mol. Med. 10 (5): 599–603. doi:10.3892/ijmm.10.5.599 (inactive 1 November 2024). PMID12373299.{{cite journal}}: CS1 maint: DOI inactive as of November 2024 (link)
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
