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Biomedical subjects

H G Remold

Publications and source records attributed to H G Remold.

At least 73 records · Page 4Linked to original sources
PubMed1984

Dissociation of human interferon-gamma-like activity from migration-inhibition factor.

Supernatants harvested from concanavalin A-stimulated human peripheral mononuclear cells after 24 hr of incubation contain one interferon species similar to human interferon-gamma (IFN-gamma) with a pI of 4.6-5.3 (first day pH 5 IFN-gamm). In contrast, during the subsequent 24 hr of incubation two species with properties of IFN-gamma are produced with pI of 3.6-4.0 (second day pH 4 IFN-gamma) and 4.6-5.6 (second day pH 5 IFN-gamma), respectively. First day pH 5 IFN-gamma and second day pH 5 IFN-gamma have been found to differ on the basis of trypsin sensitivity. This pattern of polymorphism is similar to the pattern previously described for human migration-inhibitory factor (MIF) which can be separated into first day pH 5 MIF, second day pH 3 MIF, and second day pH 5 MIF. However, IFN-gamma-like species can be differentiated from MIF biochemically and antigenically. Fractions with second day pH 4 IFN-gamma have no MIF activity and fractions with second day pH 3 MIF contain no IFN activity. In addition, first and second day pH 5 MIF, which also contain IFN-gamma activity, can be separated from the latter by precipitation as well as neutralization with polyclonal and monoclonal anti-human MIF antibodies.

Antibodies↗
PubMed1984

Activation of human macrophages. Comparison of other cytokines with interferon-gamma.

Cytokines affecting mononuclear phagocytes were screened for activation of human macrophages to secrete H2O2 and kill toxoplasmas. In contrast to recombinant interferon-gamma (rIFN gamma), the following factors, tested in partially or highly purified form and over a wide range of concentrations, did not augment these functions: native interferon-alpha (nIFN alpha), rIFN alpha A, rIFN alpha D, rIFN beta, colony stimulating factor (type 1) (CSF-1), CSF for granulocytes and macrophages (GM-CSF), pluripotent CSF (p-CSF), tumor necrosis factor (TNF), native interleukin 2 (nIL-2), and rIL-2. Partially purified migration inhibitory factor (MIF) enhanced H2O2-releasing capacity submaximally without inducing antitoxoplasma activity, and warrants further study.

Biological Products↗
PubMed1983

Production of migration-inhibitory factor by a human T-lymphoblast cell line.

Migration-inhibitory-factor (MIF) activity was detected in culture supernatants of the human T-lymphoblast cell line Mo after stimulation with phytohemagglutinin and phorbol myristate acetate. MIF activity was not detected in unstimulated cultures reconstituted with phytohemagglutinin and phorbol myristate acetate. Conditioned medium from the cell line Mo was fractionated by Sephadex G-100 gel filtration. MIF-containing Sephadex fractions corresponding to a Mr of 60,000 to 70,000 were further fractionated by isoelectrofocusing, resulting in a sharp peak of activity with a pI of 4.6 to 5.2. This MIF species constitutes a major form secreted by Mo cells; it adheres to Con A-Sepharose, is trypsin-resistant, and is denser than pure protein as determined by CsCl density gradient centrifugation. These are the same physicochemical characteristics previously established for second-day pH5-MIF from peripheral blood mononuclear cells (W.Y. Weiser et al., J. Immunol. 126, 1958, 1981). In contrast, Sephadex fractions corresponding to larger molecules (Mr 70,000-90,000) contain at least two additional MIF species. These larger MIF forms have a pI of 3.0 to 3.5 and of 4.6 to 5.2 and lack affinity to Con A Sepharose. Thus, the Mo T-cell line produces large quantities of at least three different species of human MIF.

Cell Line↗
PubMed1982

Isolation of a guinea pig macrophage glycolipid with the properties of the putative migration inhibitory factor receptor.

We have previously established that preincubation of guinea pig macrophages with crude preparations of macrophage glycolipids enhances their response to a mediator of cellular immunity, migration inhibitory factor. This biologically active moiety found in the extracted material was attributed to a single glycolipid component. This component was purified to homogeneity by phase partition, ion exchange, adsorption, and thin layer chromatography. It migrates in the ganglioside region on thin layer plates, contains sialic acid and sphingosine. There is no apparent identity with any of the common gangliosides possessing the gangliotetraose structure. Homogeneity was demonstrated by rechromatography in four additional solvent systems. These results are discussed in the context of their implications for a deeper understanding of the putative receptor function of this glycolipid.

Animals↗
PubMed1981

Purification of guinea pig pH 3 migration inhibitory factor.

Macrophage migration inhibitory factor (MIF) from the guinea pig was recently shown to reside in two discrete and separable proteins referred to as pH 3 MIF and pH 5 MIF. One subfraction of pH 3 MIF has now been purified to apparent homogeneity from supernatants of stimulated lymph node cells. To monitor purification, biosynthetically radiolabeled MIF was prepared. Sensitized lymphocytes were stimulated in the presence of [3H]leucine by concanavalin A to produce radiolabeled mediators. MIF was purified approximately 30,000-fold from the culture fluid by using gel filtration, sucrose density gradient electrophoresis, isoelectric focusing, and hydrophobic affinity chromatography. This procedure yielded a single 3H-labeled polypeptide with an apparent Mr of 35,000 that coincides with MIF activity.

Animals↗
PubMed1981

Studies on human migration inhibitory factor: characterization of three molecular species.

Human migration inhibitory factor (MIF), obtained from supernatants of peripheral blood mononuclear cells stimulated with concanavalin A, was analyzed by gel filtration, isoelectrofocusing, and CsCl density gradient centrifugation. A distinct pattern of heterogeneity was determined on the basis of its harvesting time and biochemical criteria. Supernatants from cells cultured for 1 day contained a single peak of MIF activity with an isoelectric point of 4.3 to 5.2, an apparent m.w. of 23,000, and a density of 1.314 g/ml, the same as the density of the marker protein, 125I-HSA (1st day pH 5-MIF). Furthermore, this species of human MIF was sensitive to treatment with trypsin, strongly suggesting its being a protein, but not to treatment with neuraminidase and corresponds therefore to guinea pig pH 5-MIF. However, when 2nd day supernatants were analyzed under the same conditions, 2 MIF species were found. One species with an isoelectric point of 2.4 to 3.3 had an apparent m.w. of 65,000 (2nd day 3-MIF). The other species with an isoelectric point of 4.3 to 5.6 had an apparent m.w. of 23-43,000 (2nd day pH 5-MIF). Upon centrifugation in CsCl density gradients, the density (rho 25 of 1.314 to 1.414 g/ml) of both species was found to be greater than that of the pure protein, 125I-HSA. In addition, both species were chymotrypsin and neuraminidase sensitive but not trypsin sensitive, further suggesting their glycoprotein nature.

Animals↗
PubMed1980

Role of sialic acid in the macrophage glycolipid receptor for MIF.

Acidic glycolipids from guinea pig macrophages enhance the response of macrophages to migration inhibitory factor (MIF), suggesting a role of glycolipid receptors for this lymphocyte mediator. Neuraminidase treatment of these glycolipids results in the loss of their biologic activity. This activity remains intact after incubation of the glycolipids with beta-galactosidase. In order to investigate whether sialic acid is essential for the macrophage's response to MIF, macrophages were incubated with neuraminidase. Neuraminidase treatment of peritoneal exudate cells results in the abrogation of macrophage responsiveness to MIF. Other exoglycosidases such as beta-galactosidase and beta-glucosidase had no effect upon the macrophage response. The effect of neuraminidase was found to be reversible within 18 hr. These experiments suggest that macrophage glycolipids containing sialic acid are components of the macrophage receptor for MIF.

Animals↗