Renin-like Activity, Angiotensin I-Converting Enzyme-like Activity, and Osmoregulatory Peptides in the Dogfish Rectal Gland

Abstract

Renin-like activity (RLA) and angiotensin I-converting enzyme-like activity (ACELA), two key enzymes of the renin-angiotensin cascade (RAS), were sought in the dogfish rectal gland. RLA was 1.1 ± 0.2 ng Ang I/mg protein/hr after incubation with porcine angiotensinogen and 0.8 ± 0.1 ng Ang I/mg protein/hr after incubation with homologous plasma. ACELA was 7.22 ± 1.08 and 8.87 ± 1.9 nmol hippurate generated/min/mg protein respectively, at 0 and 37°. The presence of these enzymes may indicate the presence of an endogenous RAS-like system in the rectal gland. Angiotensin II (Ang II) and atrial natriuretic peptide (ANP) binding sites were demonstrated autoradiographically in the subcapsular region of the gland, suggesting a possible interaction of the two hormones in the blind outer ends of the rectal gland tubules. Immunoreactivities toward Ang II, ANP, bombesin, vasoactive intestinal polypeptide (VIP), glucagon, and somatostatin were differentially localized in the rectal gland within three concentric zones with potentially different functional activities. In the capsule, there was a strong positive ir-glucagon reaction and a slightly weaker reaction for ir-somatostatin and VIP. In the blind outer ends of the tubeles (in the subcapsular zone), strong immunoreactivity was present toward all the tested peptides except glucagon and somatostatin. In the inner zone and in the central canal, only a weak immunoreactivity toward Ang II and glucagon was observed.