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Do Secretin and Vasoactive Intestinal Peptide Have Independent Receptors on Striatal Neurons and Glial Cells in Primary Cultures?
Author(s) -
Chneiweiss H.,
Glowinski J.,
Premont J.
Publication year - 1986
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1986.tb04543.x
Subject(s) - secretin , vasoactive intestinal peptide , receptor , secretin family , adenylate kinase , medicine , endocrinology , biology , cyclase , neuropeptide , cell culture , chemistry , stimulation , microbiology and biotechnology , biochemistry , secretion , genetics
Vasoactive intestinal peptide (VIP) and secretin are two related peptides that activate adenylate cyclase on membranes of striatal neurons and glial cells from embryonic mouse brain grown in primary culture. On the two cell types, the maximal activation that could be induced by secretin was only 40% above basal activity, which represented < 15% of the maximal effect obtainable with VIP. From competition experiments performed on glial cells and the neuroblastoma × glioma hybrid, NG 108–15, a cell line known to possess both VIP and secretin sensitive‐adenylate cyclase, we demonstrate that secretin does not activate VIP receptors. Furthermore, secretin has an apparent high affinity (EC 50 10 −8 M ) for its receptors on striatal neurons and NG 108–15 whereas an apparent low affinity (EC 50 7 × 10 −6 M ) was found on striatal glial cells. This suggests the existence of either two distinct secretin receptors or a desensitized form.