Vast release of submaxillary mouse renin to saliva after stimulation with cholinergic, β-adrenergic but especially α-adrenergic agonists
- 1 April 1982
- journal article
- research article
- Published by Oxford University Press (OUP) in Acta Endocrinologica
- Vol. 99 (4) , 636-640
- https://doi.org/10.1530/acta.0.0990636
Abstract
.alpha.-Adrenergic stimulation with phenylephrine causes release of vast amounts of mouse submaxillary gland renin to saliva. The amount released is about 100-fold higher than that released after .beta.-adrenergic stimulation with isoproterenol and about 1000-fold higher than the amount released after cholinergic stimulation with pilocarpine. .alpha.-Blockade with phenoxybenzamine before phenylephrine stimulation strongly inhibits the renin release. However, phenoxybenzamine or .beta.-blockade with propranolol before isoproterenol stimulation have no effect on the amount of renin released. Thus, the release of submaxillary mouse renin to saliva is triggered mainly by activation of .alpha.-adrenergic receptors. Renin in cholinergic and .alpha.- and .beta.-adrenergic stimulated saliva has the same MW and the same specific enzymatic activity as renin in the submaxillary gland. This indicates that renin is secreted to saliva, and probably also to the blood, in its fully enzymically active 40,000 MW form regardless of the stimulus used. The vast amounts of renin released to saliva (up to 600 Goldblatt Units) demonstrate that submaxillary mouse renin is secreted predominantly to saliva and much less to the blood. The mouse submaxillary gland therefore seems to have an exocrine rather than an endocrine role for release of renin.This publication has 3 references indexed in Scilit:
- Effect of adrenergic agonists on big and small reninAmerican Journal of Physiology-Endocrinology and Metabolism, 1980
- Concentrations of Epidermal Growth Factor, Nerve Growth Factor, and Submandibular Gland Renin in Male and Female Mouse Tissue and Fluids*Endocrinology, 1979
- Renin in the mouse submaxillary gland has a molecular weight of 40 000Biochimica et Biophysica Acta (BBA) - Protein Structure, 1979