Authors : H. Banga-Mboko , J.S. Suchodolski and J.M. Steiner
Abstract: Bovine, ovine, caprine, porcine and hen Pepsinogen C (PgC) have been reviewed. Pepsinogens C, together with other gastric proenzymes, are thought to have evolved from a common ancestral aspartyl proteinase. PgC appears to have diverged first followed by prochymosin and pepsinogens A (PgA) and F. PgC is mainly expressed in adult animals. In contrast, in hens and quails, it is synthesized during the embryonic stage before hatching. The purification of PgC requires a combination of weak anion-exchange and strong anion-exchange chromatography. Additionally, size exclusion chromatography may be necessary. PgC in pigs and goats occurs in 2 isoforms, namely PgC-1 and Pg C-2, with approximately 370, 363 and 387 amino acid residues for goat, pig and hen PgC, respectively. The molecular mass porcine pepsinogen C is close to 38-41.4 kDa and 33-36.6 kDa for the zymogen and the active enzyme, respectively. Pepsinogens C in ruminants differ from those of humans and of other animal species in their phosphate content. Unlike PgA, PgC has a higher proteolytic activity against hemoglobin at pH 3 than at pH 2. Also, PgC is less susceptible to the most potent inhibitors of aspartic proteases, such as pepstatin. Investigation of PgC in farm animals is still limited to the gastric mucosal area, despite the fact that PgC C has been reported to be present in blood and in many other tissues. Therefore, studies to further our understanding of the physiological aspects and the clinical relevance of PgC are needed.
H. Banga-Mboko , J.S. Suchodolski and J.M. Steiner , 2007. Pepsinogen C in Farm Animals: A Review. Journal of Animal and Veterinary Advances, 6: 776-786.