Specific binding of 3H-mepyramine to histamine H1 receptors in intestinal smooth muscle

Hill, Stephen J.; Young, J. M.; Marrian, D. H.

doi:10.1038/270361a0

Cited by 135 publications

(41 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A histamine concentration as high as 100 pM was not necessarily strong enough to deplete the Ca" of the stores and was estimated to be equivalent to a concentra tion of CCh in the 10 to 100-pM range. This is consistent with the previous findings in the same smooth muscle that histamine, compared with CCh, is less effective in increas ing the total amount of inositol phosphates including IP3 (8), and the binding sites (receptors) for histamine are less-densely distributed (17). In single voltage-clamped cells dispersed from the longitudinal smooth muscle of guinea pig jejunum, measurements of intracellular Ca" concentration by the use of a fluorescent dye revealed that the histamine-induced Ca" transient due to the release of Ca" stores is smaller in magnitude than the CCh-induced one (18).…”

Section: Discussionsupporting

confidence: 82%

Contractile Responses to Histamine and GTPγS in β-Escin-Treated Skinned Smooth Muscle of Guinea Pig Ileum

Fukami

Itagaki

Komori

et al. 1993

Japanese Journal of Pharmacology

View full text Add to dashboard Cite

ABSTRACT-To characterize the calcium (Ca")-releasing effects of histamine and GTPrS, the drug-in duced tension developments were measured in (3-escin-treated skinned longitudinal smooth muscle of guinea pig ileum. Intracelluar Ca2+ stores were loaded with Ca" by incubating the muscle for 10 min in a Ca" containing solution. Histamine (10-100 pM), applied after Ca" -loading, produced a transient rise in ten sion. The effect of histamine was not preserved after treatment with 20 mM caffeine, a Ca2+-store releaser. The effect of histamine was potentiated by GTP; inhibited by GDP(3S, an antagonist of GTP for binding to G-proteins; or heparin, an antagonist of inositol 1,4,5-trisphosphate (IP3) for binding to its receptor; and mimicked by IP3. When GTPrS (20 ttM) was applied and continued to be present for 15 min, a transient rise in tension followed by a small, sustained rise in tension was elicited. The effect of GTPrS was completely inhibited by GDP(3S. The initial, transient component of the biphasic GTPrS response was abolished or markedly inhibited after treatment with caffeine, heparin or the calcium ionophore A23187. The present results suggest that histamine and GTPrS cause a release of Ca 21 from caffeine-sensitive stores which is mediated by IP3 formed through a G-protein-coupled mechanism. The GTPrS-induced Ca 2+ release is not considered to involve such an IP3-independent process as described in chemically-skinned arterial muscle.

show abstract

Section: Discussionsupporting

confidence: 82%

Contractile Responses to Histamine and GTPγS in β-Escin-Treated Skinned Smooth Muscle of Guinea Pig Ileum

Fukami

Itagaki

Komori

et al. 1993

Japanese Journal of Pharmacology

View full text Add to dashboard Cite

show abstract

“…Some of the early studies on localization and physiologic/pharmacological implications of H 1 receptors, discussed extensively in Hill et al (1997), are only listed here: blood vessels (Barger and Dale, 1910;Dale and Laidlaw, 1910;Folkow et al, 1948;Black et al, 1972), other smooth muscle preparations (Marshall and Cherry, 1955;Ash and Schild, 1966;Black et al, 1972;Hill, 1990) and heart (Sakuma et al, 1988). The distribution of H 1 receptors in different mammalian tissues was first studied using selective radioligands such as [ 3 H]mepyramine (Hill et al, 1977), later using in situ hybridization (Fig. 5) (Villemagne et al, 1991;Yanai et al, 1992).…”

Section: Anatomic Frameworkmentioning

confidence: 99%

International Union of Basic and Clinical Pharmacology. XCVIII. Histamine Receptors

Panula

Chazot

Cowart

et al. 2015

Pharmacological Reviews

490

623

View full text Add to dashboard Cite

“…The H, receptor has been labeled in crude membranes with the reversible ligand [3H]mepyramine (2,3). More recently, 1251-iodobolpyramine, a highly specific probe chemically derived from mepyramine, has been developed for a more sensitive assay (4,5).…”

mentioning

confidence: 99%

Characterization of histamine H1-receptor binding peptides in guinea pig brain using [125I]iodoazidophenpyramine, an irreversible specific photoaffinity probe.

Ruat

Körner

Garbarg

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

These features establish the compound as one of the most potent H1-receptor antagonists known so far. Upon UV irradiation, 5% of the bound radioactivity was covalently incorporated into cerebellar membrane polypeptides as shown by standard NaDodSO4/PAGE. Two bands of 47 and 56 kDa were consistently labeled, labeling being prevented by various H1-receptor antagonists with the expected potencies and stereoselectivity. In the presence of protease inhibitors, labeling of the 56-kDa peptide increased at the expense of the 47-kDa peptide, suggesting that the latter was produced by hydrolysis of the former under the action of membrane proteases. In the absence of 2-mercaptoethanol, a band of 35040 kDa appeared, apparently at the expense of the lighter bands, suggesting that the latter might be linked by one or more disulflde bridges to a higher molecular mass complex. We propose that at least part of the ligand binding domain of the histamine H, receptor resides within a subunit of apparent molecular mass 56,000.

show abstract

Specific binding of 3H-mepyramine to histamine H1 receptors in intestinal smooth muscle

Cited by 135 publications

References 13 publications

Contractile Responses to Histamine and GTPγS in β-Escin-Treated Skinned Smooth Muscle of Guinea Pig Ileum

Contractile Responses to Histamine and GTPγS in β-Escin-Treated Skinned Smooth Muscle of Guinea Pig Ileum

International Union of Basic and Clinical Pharmacology. XCVIII. Histamine Receptors

Characterization of histamine H1-receptor binding peptides in guinea pig brain using [125I]iodoazidophenpyramine, an irreversible specific photoaffinity probe.

Contact Info

Product

Resources

About