Identification of a histamine release inhibitory factor produced by human mononuclear cells in vitro.

Alam, Rafeul; Lett-Brown, Michael A.

doi:10.1172/jci113826

Cited by 32 publications

(11 citation statements)

References 28 publications

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“…4). By contrast, our MAb did not recognize IL-8/ MDNCF/NAP-1, which (a) has a molecular mass of 8 kD, which is in the same range as CTAP-III (25) (35) may be specific for individual components. Our purified factor released histamine in the microgram range, and this is consistent with the microgram quantities of CTAP-III that are required to stimulate DNA synthesis in fibroblast cultures.…”

Section: Methodscontrasting

confidence: 62%

Relationship of one form of human histamine-releasing factor to connective tissue activating peptide-III.

Baeza¹,

Reddigari²,

Kornfeld³

et al. 1990

J. Clin. Invest.

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We have previously reported purification of three forms of histamine-releasing factors (HRFs) from mixtures of streptokinase-streptodornase stimulated human mononuclear cells and platelets with apparent molecular masses of 10-12, 15-17, and 4041 kD (1989. J. Clin. Invest. 83:1204-1210. We have also prepared mouse MAbs against the 10-12-kD HRF (1989. J. Allergy Clin. Immunol. 83:281). Affinity-purified 10-12-kD HRF appears as a broad band upon polyacrylamide gel electrophoresis in the presence of SDS. We determined the NH2-terminal amino acid sequence of the top and bottom halves of this broad band. Sequence analysis revealed striking homology between this HRF and connective tissue activating peptide-Ill (CTAP-III), a platelet-derived 8-10-kD protein known to cause mitogenesis and extracellular matrix formation in fibroblast cultures. 19 of 21 NH2-terminal residues in the top half of the HRF band were identical to the NH2-terminal sequence of CTAP-III. 20 of 21 NH2-terminal residues in the bottom half were identical to the NH2-terminal sequence of neutrophil-activating peptide-2, which is derived from CTAP-III by proteolytic cleavage between residues 15 and 16. Purified CTAP-III also released histamine from basophils. Rabbit antiserum raised against either native or recombinant CTAP-IIl recognized affinity-purified HRF in immunodot blot assays, and MAb against HRF recognized C(AP-III in both dot blot and microtiter plate based immunoassays. These data demonstrate the first structural, functional, and immunologic relationship between one form of human HRF and a previously described cell product. (J. Clin. Invest. 1990Invest. . 85:1516Invest. -1521 basophil secretion * histamine release * histamine-releasing factor purification

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Section: Methodscontrasting

confidence: 62%

Relationship of one form of human histamine-releasing factor to connective tissue activating peptide-III.

Baeza¹,

Reddigari²,

Kornfeld³

et al. 1990

J. Clin. Invest.

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“…Moreover, the effect of SNP having disappeared through the cell purification was restored by the addition of monocytes/macrophages to a purified basophil/mast cell population showing that monocytes/macrophages might contribute to the inhibitory effect of SNP on basophils/mast cells stumulated by anti-IgE or A23187. A histamine release inhibitory factor has been reported as a cytokine which could inhibit histamine release from mast cells [28]. As the sufficient preincubation time required for the inhibitory effect of SNP was 30 min, however, SNP and secretagogues were not supposed to stimulate monocytes/macrophages to generate a cytokine such as histamine release inhibitory factor involved in the degranulation of mast cells in such a short period.…”

Section: Discussionmentioning

confidence: 99%

Exogenous Nitric Oxide Regulates the Degranulation of Human Basophils and Rat Peritoneal Mast Cells

Iikura¹,

Takaishi²,

Hirai³

et al. 1998

Int Arch Allergy Immunol

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This study was designed to investigate whether anti-IgE-induced or ionophore A23187-induced histamine release from human basophils is regulated by exogenous nitric oxide (NO), and to assess some similarities between the effect of NO on basophils and that on rat peritoneal mast cells (RPMC). The NO donor, sodium nitroprusside (SNP), inhibited A23187-induced histamine release from crude human basophils and crude RPMC in a dose-dependent fashion. This downregulation was still observed when SNP was washed out just before the cell stimulation, indicating that the effect of SNP was irreversible. The downregulation disappeared in both purified cell populations after the removal of contaminating cells. However, when purified cells were preincubated with SNP in the presence of 5 mM N-acetylcysteine (NAC), increasing the bioavailability of NO, the downregulation was recovered. The presence of NAC significantly augmented the downregulation of SNP on A23187-induced histamine release from both crude cell populations. In contrast, SNP had no effect on anti-IgE-induced histamine release from either crude or purified basophil preparation in the absence of NAC, and SNP plus NAC inhibited anti-IgE-induced histamine release from both cell preparations. The same results were obtained with crude and purified RPMC preparations under the same conditions. These results show that SNP similarly downregulated exocytosis of basophils and RPMC, and acquired the potent effect in the presence of NAC, indicating that exogenous NO plays a part in the regulation of basophil and mast cell activation.

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“…Immunoregulatory cells produce a number of substances that stimulate the growth and function of mast cells and basophils. Histamine releasing as well as histamine release-inhibitory factors have been described [13]. …”

Section: Discussionmentioning

confidence: 99%

Histamine Synthesis by White& ;Cells during Storage of Platelet Concentrates

Muylle¹,

Beert²,

Mertens³

et al. 1998

Vox Sanguinis

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Objectives: To resolve the question whether histamine, like some cytokines, is actively synthesized during storage of platelet concentrates. Methods: We prepared conventional buffy coat platelet concentrates and stored them in the usual way at 22 °C. Disodium cromoglycate was added to one series, saline to the controls. Samples were taken at intervals, to be tested for histamine and interleukin-6 (IL-6). Results: The plasma histamine level increased from a median of 1.02 ng/ml (range 0.11–3.27) to 12.9 ng/ml (range 4.30–32.9) whereas the total histamine content of the platelet concentrates remained unchanged during the 5-day storage period. In contrast, the total content of IL-6 increased rapidly. Conclusion: Histamine is not synthesized during storage of platelets, whereas IL-6 is. The addition of disodium cromoglycate, a substance that inhibits granulocyte activation, had no effect on the release of histamine or on the total histamine content at various storage times.

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Identification of a histamine release inhibitory factor produced by human mononuclear cells in vitro.

Cited by 32 publications

References 28 publications

Relationship of one form of human histamine-releasing factor to connective tissue activating peptide-III.

Relationship of one form of human histamine-releasing factor to connective tissue activating peptide-III.

Exogenous Nitric Oxide Regulates the Degranulation of Human Basophils and Rat Peritoneal Mast Cells

Histamine Synthesis by White& ;Cells during Storage of Platelet Concentrates

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