Histamine as an intracellular messenger

Brandes, Lorne J.; LaBella, Frank S.; Glavin, Gary B.; Paraskevas, F; Saxena, Satya; McNicol, Archibald; Gerrard, Jon M.

doi:10.1016/0006-2952(90)90341-h

Cited by 75 publications

(43 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…More recently, two additional binding sites, termed intracellular histamine receptors (Hie), have been identified in the mierosome and in the nucleus [11,12]. The existence of these receptors, together with our recent evidence for histamine uptake by hematopoietic progenitors [13], is consistent with the idea that histamine does indeed play a physiological role inside hematopoietic progenitor cells.…”

Section: Introduction 2 Materials and Methodssupporting

confidence: 70%

Evidence for bidirectional histamine transport by murine hematopoietic progenitor cells

Corbel

1996

FEBS Letters

View full text Add to dashboard Cite

Murine hematopoietic progenitor cells synthesize substantial amounts of histamine in response to IL-3 or calcium ionophore. They also take up extracellular histamine by an active transport system. In the present study we demonstrate that this system mediates both influx and efflux of histamine. Indeed, MR16155 and thioperamide, the two 1-13 antagonists which are most effective in inhibiting histamine uptake, likewise diminish the release of preloaded histamine from bone marrow cells. These compounds also inhibit the release of histamine which has been newly synthesized by hematopoietic progenitors in response to IL-3 or calcium ionophore, as assessed by the accumulation of the mediator inside the cells in the presence of the antagonists. The potency of different histamine receptor antagonists as inhihitors of histamine release increases with their capacity to block histamine uptake.Key words: Hematopoietic progenitor; Histamine; Bidirectional transport; Interleukin-3 Histamine uptake is temperature-dependent and partially requires sodium exchange [13]. Although we have provided evidence that this phenomenon is not mediated by classical histamine receptors, Ha receptor antagonists, such as thioperamide and MR16155, are potent inhibitors. Conversely to the polyamine transport system, which exists in numerous cell types and has been extensively studied [14,15], histamine transport seems to be restricted to astrocytes, endothelial and glial cells, and is still poorly understood [16][17][18]. It has been suggested that astrocytes could use the same means of transport for histamine uptake and release [18]. Herein, we provide evidence for a bidirectional transporter in bone marrow cells (BMC) and in the IL-3-dependent cell line FDCP1, as assessed by the finding that the inhibitors of histamine uptake likewise decrease release of preloaded histamine. We also show that this system is involved in the release of endogenous histamine which is newly synthesized in response to IL-3 or calcium ionophore since we found a decrease in histamine release accompanied by an increase in intracellular histamine contents in the presence of H3 receptor antagonists.

show abstract

Section: Introduction 2 Materials and Methodssupporting

confidence: 70%

Evidence for bidirectional histamine transport by murine hematopoietic progenitor cells

Corbel

1996

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…binding sites in microsomes from several tissues and the potency to inhibit platelet aggregation (Brandes et al, 1990;1991). P450 inhibitors also block aggregation (Parnham et al, 1981), suggesting a close association between HIc and P450 in platelets.…”

Section: Discussionmentioning

confidence: 98%

“…Collaborative studies by our laboratory have centred on the physiological role of intracellular binding sites (HIc) for histamine (Brandes et al, 1990). A low affinity (jaM) site in microsomes has been implicated in a second messenger role for histamine in platelets (Saxena et al, 1989); additional high and low affinity nuclear sites, of different ligand specificity, appear to play a growth-modulatory role in lymphocytes (Brandes et al, 1990;1991).…”

Section: Introductionmentioning

confidence: 99%

“…A low affinity (jaM) site in microsomes has been implicated in a second messenger role for histamine in platelets (Saxena et al, 1989); additional high and low affinity nuclear sites, of different ligand specificity, appear to play a growth-modulatory role in lymphocytes (Brandes et al, 1990;1991). H1c exhibits strong preference for certain novel, antioestrogen-like compounds, lesser affinity for HI ligands and very low affinity for H2 ligands (Brandes et al, 1990). An important locus for H3 receptors is presynaptic nerve terminals; histamine and other H3 agonists reportedly interact at these receptors to suppress the synthesis and release of histamine (van Der Werf et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

H₃ receptor antagonist, thioperamide, inhibits adrenal steroidogenesis and histamine binding to adrenocortical microsomes and binds to cytochrome P450

LaBella

Queen

Glavin

et al. 1992

British J Pharmacology

View full text Add to dashboard Cite

show abstract

“…To the extent that high affinity histamine binding may be a general property of ferric heme proteins that interact with NO, the effects of histamine on guanylate cyclase and NO synthase (two heine proteins that interact with NO through a heme group, reference 19) should be investigated, mainly taking into consideration the fact that histamine has recently been proposed as an intraceUular mediator (27)(28)(29).…”

mentioning

confidence: 99%

High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus.

Ribeiro

Walker

1994

The Journal of Experimental Medicine

140

View full text Add to dashboard Cite

Summal'yThe salivary glands of Rhodnius prolixus contain a nitrosyl-heme protein, named nitrophorin, that releases the vasodilatory and antiplatelet compound nitric oxide (NO). Because imidazole compounds such as histamine can interact with Fe(III) heme proteins, we investigated whether such substances could interact with Rhodnius nitrophorins. Both imidazole and histamine, but not histidine can produce full change of the difference spectra of the Soret band in the 1-3 #M concentration range (at a heme protein concentration of 0.4 #M). The apparent Ko.5 for the binding of histamine with the heme protein is below 1 #M. Furthermore, the complex histamine-heme protein does not dissociate after molecular sieving chromatography. To investigate whether histamine could displace NO from the native nitrosyl nitrophorins, histamine was added to the native heme proteins, leading to displacement of the bound NO as observed by changes in the absorption spectra as well as by the production of nitrite. Finally, the antihistamine effect of the heme protein was demonstrated by its inhibition of the histamine-provoked contractures of the guinea pig ileum. It is concluded that histamine, a common autacoid found at the site of injury and exposure to antigenic substances such as the site of feeding by hematophagous arthropods, can be scavenged by the nitrosyl nitrophorin of R. prolixus, which, in return, will release the vasodilatory and platelet inhibiting NO to counteract the host hemostatic response.

show abstract

Histamine as an intracellular messenger

Cited by 75 publications

References 31 publications

Evidence for bidirectional histamine transport by murine hematopoietic progenitor cells

Evidence for bidirectional histamine transport by murine hematopoietic progenitor cells

H₃ receptor antagonist, thioperamide, inhibits adrenal steroidogenesis and histamine binding to adrenocortical microsomes and binds to cytochrome P450

High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus.

Contact Info

Product

Resources

About

Histamine as an intracellular messenger

Cited by 75 publications

References 31 publications

Evidence for bidirectional histamine transport by murine hematopoietic progenitor cells

Evidence for bidirectional histamine transport by murine hematopoietic progenitor cells

H3 receptor antagonist, thioperamide, inhibits adrenal steroidogenesis and histamine binding to adrenocortical microsomes and binds to cytochrome P450

High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus.

Contact Info

Product

Resources

About

H₃ receptor antagonist, thioperamide, inhibits adrenal steroidogenesis and histamine binding to adrenocortical microsomes and binds to cytochrome P450