3H-Substance P binding to salivary gland membranes. Regulation by guanyl nucleotides and divalent cations

Ming Lee Chi Ming Lee, J. A. Javitch, Solomon H Snyder

Research output: Contribution to journalArticle

Abstract

With appropriate measures to protect 3H-substance P (3H-SP) from proteolytic degradation and from nonspecific adsorption to glass-fiber filters, we have been able to demonstrate reliably a high-affinity specific binding of 3H-SP to rat submaxillary/sublingual gland membranes with a K(D) of 1 nM and B(max) of 6 pmoles/g of tissue. The relative potencies of various SP fragments and related analogues in reducing 3H-SP binding parallel their potencies in stimulating phosphatidylinositol turnover, amylase release, and salivation, thus supporting an association of the observed 3H-SP binding site with the physiological SP receptors in this tissue. This binding is selectively stimulated by some divalent cations (Mn2+ > Mg2+ > Ca2+) but inhibited by several guanyl nucleotides, suggesting a possible linkage to adenylate cyclase. However, no effect of SP on either the basal or the norepinephrine-stimulated adenylate cyclase activity could be demonstrated in salivary gland homogenates.

Original languageEnglish (US)
Pages (from-to)563-569
Number of pages7
JournalMolecular Pharmacology
Volume23
Issue number3
StatePublished - 1983

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Divalent Cations
Substance P
Salivary Glands
Nucleotides
Membranes
Adenylyl Cyclases
Sublingual Gland
Salivation
Submandibular Gland
Amylases
Phosphatidylinositols
Adsorption
Norepinephrine
Binding Sites

ASJC Scopus subject areas

  • Pharmacology

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3H-Substance P binding to salivary gland membranes. Regulation by guanyl nucleotides and divalent cations. / Chi Ming Lee, Ming Lee; Javitch, J. A.; Snyder, Solomon H.

In: Molecular Pharmacology, Vol. 23, No. 3, 1983, p. 563-569.

Research output: Contribution to journalArticle

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