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At least 19 recordsLinked to original sources
PubMed1985

Antigen-dependent heterogeneity of human migration inhibitory factor.

Human migration inhibitory factor (MIF) produced by peripheral blood mononuclear cells stimulated with purified protein derivative, tetanus toxoid, streptokinase-streptodornase, or Candida albicans antigen was analyzed by gel filtration and isoelectrofocusing. In all cases, supernatants harvested after a 24-hr exposure of the mononuclear cells to the antigen yielded only one MIF species with an isoelectric point of 5. In contrast, isoelectrofocusing of supernatants obtained from cells exposed to the antigen for an additional 24 hr demonstrated that different antigens induce the elaboration of different MIF species. Streptokinase-streptodornase and tetanus toxoid induced the production of one MIF species with an isoelectric point of 5 (pH 5-MIF). Stimulation of cells with Candida antigen elaborated a MIF species with an isoelectric point of 3 (pH 3-MIF). In contrast, stimulation of cells with purified protein derivative induced the production of both pH 3-MIF and pH 5-MIF.

Antigens↗
PubMed1985

Glycolipid receptor for human migration inhibitory factor: fucose and sialic acid are important for the human monocyte response to migration inhibitory factor.

The role of carbohydrate in the interaction of human migration inhibitory factor (MIF) with human peripheral blood monocytes was investigated by studying the effects of different exoglycosidases on the cellular response to MIF. When monocytes were pretreated with neuraminidase, an exoglycosidase specific for sialic acid, they became unresponsive to MIF. Other glycosidases, such as beta-galactosidase and alpha-mannosidase, were inactive in this respect. The effect of neuraminidase was reversible since the response to MIF was restored to normal levels after 24 hr. In parallel studies, a glycolipid-enriched extract from U937 cells, a human macrophage-like cell line, known to enhance the monocyte response to MIF, lost this activity when treated with neuraminidase and alpha-L-fucosidase, but not with beta-galactosidase. This suggests the importance of terminal sialic acid and fucose residues for the interaction between monocyte membrane glycolipids and MIF.

Cell Line↗
PubMed1992

Recombinant human migration inhibitory factor has adjuvant activity.

Recombinant human migration inhibitory factor (MIF), isolated through functional expression cloning in COS-1 cells, up-regulates expression of genes encoding HLA-DR and interleukin 1 beta (IL-1 beta) and elaboration of IL-1 beta by human monocyte-derived macrophages. Administration of soluble bovine serum albumin or human immunodeficiency virus 120-kDa glycoprotein (HIV gp120) to mice in the presence of recombinant MIF together with incomplete Freund's adjuvant induced a strong T-cell proliferative response comparable to that of complete Freund's adjuvant. Recombinant MIF also increased antibody production, especially of IgG1 and IgM, in mice. Taken together, these results indicate that recombinant MIF may be useful as an adjuvant in the development of vaccines.

Adjuvants, Immunologic↗
PubMed1977

Mouse bone marrow-cultured macrophage as indicator cells for mouse and human migration inhibitory factor (MIF).

Macrophages cultured from mouse bone marrow served as excellent indicator cells for mouse as well as for human migration inhibitory factor (MIF) preparations. The tests were performed in the capillary system and showed high reproducibility. Using mouse or human MIF-containing supernatants, we found an inhibition of 53% compared with the controls. Similar results were obtained if concanavalin A-stimulated human peripheral blood lymphocytes were mixed with mouse test macrophages in a ratio of 1:5 or 1:10.

Animals↗
PubMed1985

Macrophage glycolipid receptors for human migration inhibitory factor (MIF): differentiated HL-60 cells exhibit MIF responsiveness and express surface glycolipids which both bind MIF and convert nonresponsive cells to responsiveness.

The human promyelocytic leukemia line HL-60 when treated with a phorbol diester (TPA) differentiates into cells (HL60-TPA) that respond to human migration inhibitory factor (MIF). Unresponsive HL-60 cells became responsive to MIF when preincubated with a glycolipid-enriched preparation extracted from HL60-TPA cells, human monocytes, human macrophage-like (U937) cell line, or with the purified glycolipid receptor for MIF from guinea pig peritoneal macrophages. Human blood monocytes exhibited an increased response to MIF when preincubated with glycolipids from HL60-TPA and U937 cells but not from HL-60 cells. Finally, glycolipids from HL60-TPA cells but not from HL-60 cells were able to reversibly bind MIF when covalently coupled to agarose. These studies suggest that TPA induces the differentiation of HL-60 cells into MIF-responsive cells through the expression of a glycolipid receptor for MIF.

Cell Differentiation↗
PubMed1990

Human migrating myoelectric complex in relation to gastrointestinal transit of a meal.

Feeding interrupts the migrating myoelectric complex in most mammals. This study aimed to assess whether resumption of the migrating myoelectric complex in the human duodenum after eating was related to the gastrointestinal transit of the meal. Five healthy subjects participated in the study. After eating a radiolabelled test meal consisting of mixed liquid and solids, duodenal myoelectric activity and gastrointestinal transit of the meal were determined simultaneously. In spite of considerable variation in entire gastric emptying time between subjects (range 2.5-5.0 hours), significant correlation was found between the completion of gastric emptying and the resumption of duodenal phase III activity within subjects (p less than 0.01). A new technique for recording the duodenal myoelectric activity was used.

Adult↗
PubMed1978

Human migration inhibitory factor: purification and immunochemical characterization.

Using gel filtration and preparative isotachophoresis, the migration inhibitory factor (MIF) was highly purified from human lymphocytes activated with concanavalin A. MIF is an acidic protein with a mol wt of approximately equal to 25,000 daltons as determined by gel filtration and analytical polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The protein inhibits migration of macrophages in the capillary test and in addition, has a slowing effect on the electrophoretic mobility of guinea pig peritoneal macrophages. Rabbit antibodies specific for this protein, as determined by immunochemical techniques, neutralized the biological effect of MIF on migration and on the electrophoretic mobility of macrophages.

Antigen-Antibody Reactions↗
PubMed1986

Generation and characterization of a monoclonal antibody (1C5) to human migration inhibitory factor (MIF).

A monoclonal antibody was raised in mice against human MIF of the Mr 14,000 kd, produced by Concanavalin A-stimulated peripheral blood mononuclear cells. A hybridoma (1C5) secreting an IgG 1 antibody was selected which binds, yet does not neutralize MIF in the macrophage migration assay. MIF activity may be released from immobilized antibodies by acidic buffer elution. The eluate consists of three major bands at Mr 8,000, 14,000 and 28,000 as revealed by SDS-polyacrylamide gel electrophoresis and molecular sieve chromatography (HPLC). By radioimmunoassay and enzyme-linked immunoassay, it could be shown that the antibody binds material with isoelectric points of 4.5 to 5.0 and of 3.0, which coincides precisely with the biological activities. Similar congruencies between the distribution of biologically reactive and binding material were found in molecular sieve and ion exchange chromatography. It is concluded that the antibody 1C5 reacts with most molecular weight entities of MIF which seem to be structurally related and which display similar characteristics as described for guinea pig and mouse MIF.

Antibodies, Monoclonal↗
PubMed1991

A unique fibrillar coat on the surface of migrating human primordial germ cells.

Primordial germ cells (PGCs) were studied by electron microscopy in human embryos at 27 and 30 days of gestation. PGCs were mainly found in the hindgut epithelium, some at the stage of separation from the endoderm, and others in migration through the mesenchyme of the dorsal mesentery between the primitive intestinal wall and the coelomic epithelium, including the coelomic angle. A few PGCs were still located in the endodermal epithelium. Before the process of separation and migration, PGCs appeared clearly different from neighboring somatic cells (endodermal, mesenchymal and epithelial cells of the hindgut and the coelomic layer). PGCs located in the endodermal epithelium were large and showed an irregular cell body often provided with filopodia-like processes that contacted somatic cells to form small areas of focal junctions. As a rule, PGCs possessed a large, round nucleus containing one or two conspicuous nucleoli. Lipid droplets, abundant glycogen particles, ribosomes and mitochondria were often observed in their cytoplasm. A detailed ultrastructural analysis revealed a delicate fibrillar coat frequently present on the free surface of PGCs during their migratory phase through the mesenchyme of the dorsal mesentery. This surface coat, likely corresponding to a glycocalyx, appeared as a particular, conspicuous filamentous layer of 30 nm thickness, mainly in the leading pseudopodial projections of PGCs migrating toward their target. The surface coat of PGCs can be associated with the binding sites of specific macromolecular components of the extracellular matrix, including fibronectin, and hence plays a role in PGCs recognition and migration during this special embryonic phase.(ABSTRACT TRUNCATED AT 250 WORDS)

Cell Membrane↗