TY - JOUR
T1 - Kallikrein generates angiotensin II but not bradykinin in the plasma of the urodele, Amphiuma tridactylum
AU - Conlon, J. M.
AU - Yano, K.
N1 - Funding Information:
Acknowledgements-This work was supported by a grant from the National Science Foundation (IBN 9418819).
PY - 1995/3
Y1 - 1995/3
N2 - Incubation of heat-denatured plasma from the urodele, Amphiuma tridactylum (three-toed amphiuma) or from the anurans Rana ridibunda (European green frog) and Rana catesbeiana (American bullfrog) with either glass beads, porcine pancreatic kallikrein or trypsin did not generate bradykinin-like immunoreactivity. However, peptides were generated in kallikrein-treated amphiuma plasma that contracted vascular rings from the bullfrog systemic arch and had a spasmogenic action on the bullfrog urinary bladder. These peptides, which were not generated in trypsin-treated plasma, were purified to homogeneity by reverse-phase HPLC and their primary structures established as: Asp-Arg-Val-Tyr-Val-His-Pro-Phe ([Asp1,Val5]angiotensin II) and Asn-Arg-Val-Tyr-Val-His-Pro-Phe ([Asn1,Val5]angiotensin II). Incubation of synthetic [Asn1,Val5]angiotensin II with amphiuma plasma resulted in deamidation to [Asp1,Val5]angiotensin II. The data suggest, therefore, that amphiuma plasma contains an l-asparagine amidohydrolase (asparaginase), as previously described for the eel. Although bradykinin-related peptides have been isolated from frog skin, this study provides evidence that the kallikrein-kinin system may be absent from the blood of amphibia.
AB - Incubation of heat-denatured plasma from the urodele, Amphiuma tridactylum (three-toed amphiuma) or from the anurans Rana ridibunda (European green frog) and Rana catesbeiana (American bullfrog) with either glass beads, porcine pancreatic kallikrein or trypsin did not generate bradykinin-like immunoreactivity. However, peptides were generated in kallikrein-treated amphiuma plasma that contracted vascular rings from the bullfrog systemic arch and had a spasmogenic action on the bullfrog urinary bladder. These peptides, which were not generated in trypsin-treated plasma, were purified to homogeneity by reverse-phase HPLC and their primary structures established as: Asp-Arg-Val-Tyr-Val-His-Pro-Phe ([Asp1,Val5]angiotensin II) and Asn-Arg-Val-Tyr-Val-His-Pro-Phe ([Asn1,Val5]angiotensin II). Incubation of synthetic [Asn1,Val5]angiotensin II with amphiuma plasma resulted in deamidation to [Asp1,Val5]angiotensin II. The data suggest, therefore, that amphiuma plasma contains an l-asparagine amidohydrolase (asparaginase), as previously described for the eel. Although bradykinin-related peptides have been isolated from frog skin, this study provides evidence that the kallikrein-kinin system may be absent from the blood of amphibia.
KW - Amphibia
KW - Amphiuma
KW - Angiotensin II
KW - Bradykinin
KW - HPLC purification
KW - Kallikrein
KW - Plasma
KW - Vasoactive peptide
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U2 - 10.1016/0742-8413(94)00099-V
DO - 10.1016/0742-8413(94)00099-V
M3 - Article
C2 - 7599980
AN - SCOPUS:0029053039
SN - 0742-8413
VL - 110
SP - 305
EP - 311
JO - Comparative Biochemistry and Physiology. Part C: Comparative
JF - Comparative Biochemistry and Physiology. Part C: Comparative
IS - 3
ER -