Characterization of neurotensin binding to rat gastric smooth muscle receptor sites.

Abstract:

:The binding of monoiodo 125I-Trp11-neurotensin to purified rat gastric fundus smooth muscle plasma membranes was characterized. Specific binding of ligand in subcellular fractions from rat fundus smooth muscle showed a distribution that paralleled that of several plasma membrane marker enzymes. 125I-Trp11-neurotensin binding to smooth muscle plasma membranes at 25 degrees C was maximal at 30 min, reversible and saturable. Scatchard analysis of equilibrium data indicated the existence of two classes of binding sites with dissociation constants (Kd) of 56 pmol and 1.92 nM, and corresponding binding capacities (Bmax) of 6.6 fmol/mg and 11.4 fmol/mg of membrane protein. Analogues and fragments of neurotensin competed for 125I-Trp11-neurotensin binding with a rank order of potency similar to that previously reported for their contracting effect in rat fundus strips. Na+ decreased in a concentration dependent manner the binding of labelled ligand to the high affinity site. At 100 mM, Na+ induced a 6-fold increase in the IC50 of neurotensin for inhibition of 125I-Trp11-neurotensin binding. At this concentration of Na+, the IC50 for neurotensin was 1 nM, a value close to the Kd of the low affinity site.

journal_name

Peptides

journal_title

Peptides

authors

Kitabgi P,Kwan CY,Fox JE,Vincent JP

doi

10.1016/0196-9781(84)90117-7

subject

Has Abstract

pub_date

1984-09-01 00:00:00

pages

917-23

issue

5

eissn

0196-9781

issn

1873-5169

pii

0196-9781(84)90117-7

journal_volume

5

pub_type

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