TY - JOUR
T1 - Enkephalin convertase demonstrated in the pituitary and adrenal gland by 3hguanidinoethylmercaptosuccinic acid autoradiography
T2 - Dehydration decreases neurohypophyseal levels
AU - Strittmatter, Stephen M.
AU - Lynch, David R.
AU - De Souza, Errol B.
AU - Snyder, Solomon H.
PY - 1985/10
Y1 - 1985/10
N2 - [3H]Guanidinoethylmercaptosuccinic acid (GEMSA) autoradiography demonstrates the participate form of a carboxypeptidase B-like peptide processing enzyme, enkephalin convertase (EC 3.4.17.10), in the rat pituitary and adrenal glands. The maximal number of binding sites (Bmax) for [3H] GEMSA is 20 pmol/mg protein in the intermediate lobe of the pituitary, 12.0 pmol/mg protein in the posterior pituitary lobe, 15 pmol/mg protein in the anterior pituitary lobe, 5.8 pmol/mg protein in the adrenal medulla, and less than 0.3 pmol/mg protein in the adrenal cortex. The labeling pattern is homogeneous within each of these regions. Subcellular fractionation of the bovine adrenal medulla demonstrates that [3H]GEMSAbinding sites are localized to chromaffin granules. In Brattleboro rats and dehydrated rats, the level of posterior pituitary [3H] GEMSA binding is less than 25% of that in control animals. This decrease is abolished by arginine vasopressin treatment of Brattleboro rats or rehydration of dehydrated rats. There are no changes in [3H]GEMSA binding in the supraoptic nucleus or magnocellular portion of the paraventricular nucleus of the hypothalamus under any of these conditions, suggesting that the alterations observed in the neurohypophysis result from an increased rate of loss of enkephalin convertase. The level of anterior pituitary enkephalin convertase is unchanged by dehydration, adrenalectomy, or dexamethasone or in Brattleboro rats. [3H] GEMSA labeling in the intermediate pituitary lobe is unaffected by dehydration and haloperidol treatment and in Brattleboro rats. The adrenal medullary enzyme is not altered by reserpine, hypophysectomy, or splanchnic denervation or in Brattleboro rats.
AB - [3H]Guanidinoethylmercaptosuccinic acid (GEMSA) autoradiography demonstrates the participate form of a carboxypeptidase B-like peptide processing enzyme, enkephalin convertase (EC 3.4.17.10), in the rat pituitary and adrenal glands. The maximal number of binding sites (Bmax) for [3H] GEMSA is 20 pmol/mg protein in the intermediate lobe of the pituitary, 12.0 pmol/mg protein in the posterior pituitary lobe, 15 pmol/mg protein in the anterior pituitary lobe, 5.8 pmol/mg protein in the adrenal medulla, and less than 0.3 pmol/mg protein in the adrenal cortex. The labeling pattern is homogeneous within each of these regions. Subcellular fractionation of the bovine adrenal medulla demonstrates that [3H]GEMSAbinding sites are localized to chromaffin granules. In Brattleboro rats and dehydrated rats, the level of posterior pituitary [3H] GEMSA binding is less than 25% of that in control animals. This decrease is abolished by arginine vasopressin treatment of Brattleboro rats or rehydration of dehydrated rats. There are no changes in [3H]GEMSA binding in the supraoptic nucleus or magnocellular portion of the paraventricular nucleus of the hypothalamus under any of these conditions, suggesting that the alterations observed in the neurohypophysis result from an increased rate of loss of enkephalin convertase. The level of anterior pituitary enkephalin convertase is unchanged by dehydration, adrenalectomy, or dexamethasone or in Brattleboro rats. [3H] GEMSA labeling in the intermediate pituitary lobe is unaffected by dehydration and haloperidol treatment and in Brattleboro rats. The adrenal medullary enzyme is not altered by reserpine, hypophysectomy, or splanchnic denervation or in Brattleboro rats.
UR - http://www.scopus.com/inward/record.url?scp=0021962643&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021962643&partnerID=8YFLogxK
U2 - 10.1210/endo-117-4-1667
DO - 10.1210/endo-117-4-1667
M3 - Article
C2 - 3928337
AN - SCOPUS:0021962643
SN - 0013-7227
VL - 117
SP - 1667
EP - 1674
JO - Endocrinology
JF - Endocrinology
IS - 4
ER -