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Albutensin A, an ileum-contracting peptide derived from serum albumin, acts through both receptors for complements C3a and C5a
Authors:Masakazu Takahashi   Shigeo Moriguchi   Toshiko Minami   Hiroyuki Suganuma   Akira Shiota   Yasuyuki Takenaka   Fumito Tani   Ryuzo Sasaki  Masaaki Yoshikawa
Affiliation:(1) Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, 606-8502 Kyoto, Japan;(2) Research Institute for Food Science, Kyoto University, Uji, 611-0011 Kyoto, Japan
Abstract:Albutensin A is an ileum-contracting peptide derived from serum albumin. The sequences of bovine, human and porcine albutensin A are ALKAWSVAR, AFKAWAVAR, and AFKAWSLAR, respectively. These albutensin A homologs all exhibited biphasic ileal contractions in the longitudinal strips of guinea pig ileum. The order of potency in the contraction was porcine > bovine > human homologs. The ileal contraction profiles were similar to those of oryzatensin and casoxin C, agonist peptides for complement C3a receptors derived from rice albumin and bovine kappa-casein, respectively. All three homologs of albutensin A have homology with the COOH-terminal sequences of complements C3a and C5a, which are essential for their activities; porcine albutensin A showed the highest homology. Indeed, porcine albutensin A was confirmed to act through both C3a and C5a receptors by a radioreceptor assay and cross-desensitization in the ileal contraction. In addition, bovine and human homologs also showed affinity for both receptors. This study suggests that a bioactive peptide acting through both C3a and C5a receptors is released by the proteolytic cleavage of serum proteins other than complement components.
Keywords:complements C3a and C5a  guinea pig ileum  ileum-contracting mechanism  serum albumin-derived peptide
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