Literature DB >> 7461702

Non-specific binding by macrophages: existence of different adhesive mechanisms and modulation by metabolic inhibitors.

A M Benoliel, C Capo, P Bongrand, A Ryter, R Depieds.   

Abstract

Rat peritoneal cells were made to bind test particles of five different species: immunoglobulin-coated sheep red cells (IGSRC), glutaraldehyde-treated sheep red cells (GSRC), leishmania, latex beads and tumour cells. The dependence of binding on various physicochemical parameters was studied: the binding of latex or leishmania resisted cold (4 degrees), azide, cytochalasin B, ethyleneglycol and dimethylsulphoxide (DMSO). The binding of IGSRC resisted cold and azide, but it was inhibited by cytochalasin B, ethyleneglycol and DMSO. The binding of GSRC was inhibited by cold, azide and ethyleneglycol, but not by cytochalasin B and DMSO. The binding of tumour cells was inhibited by azide, cytochalasin B, ethyleneglycol and DMSO. An attempt was made to saturate selectively some adhesive sites of macrophage membranes: glutaraldehyde-treated bovine albumin (GBSA) inhibited the ingestion of latex and GSRC, not leishmania and IGSRC, whereas a crude leishmania extract (CLE) inhibited the ingestion of all tested particles except latex. Antigen-antibody complexes inhibited the ingestion of IGSRC and leishmania, not latex and GSRC. Rat macrophages were made to bind radio-iodinated GBSA (GIBSA). The uptake of glutaraldehyde-treated albumin was proportional to the amount of substrate the cells were incubated with over a wide concentration range. This uptake was not a result of endocytosis, and it was far more efficient than that of peroxidase. Macrophage-particle interaction was studied with electron microscopy. The binding of IGSRC and leishmania to macrophages involved large areas where the interacting membranes were separated by a low density gap of constant width. The interaction of GSRC and latex with macrophages was much more patchy and irregular. Further, no redistribution of the macrophage surface polysaccharides seemed associated with the binding of GSRC. It was concluded that several different mechanisms and different membrane adhesive structures are involved in non-specific recognition by macrophages. Further, non-specific binding sometimes requires an active cell participation. Several testable hypotheses are described, which suggest further experiments in order to obtain a fuller insight into the mechanism of rosette formation.

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Year:  1980        PMID: 7461702      PMCID: PMC1458149     

Source DB:  PubMed          Journal:  Immunology        ISSN: 0019-2805            Impact factor:   7.397


  25 in total

1.  Alloimmune peritoneal macrophages as specific effector cells: characterization of specific macrophage cytotoxin.

Authors:  C E Piper; K L McIvor
Journal:  Cell Immunol       Date:  1975-06       Impact factor: 4.868

2.  Antigen binding T and B lymphocytes. I. Differences in cellular specificity and influence of metabolic activity on interaction of antigen with T and B cells.

Authors:  G J Hämmerling; H O McDevitt
Journal:  J Immunol       Date:  1974-05       Impact factor: 5.422

3.  Loss of cell surface material from peritoneal exudate cells associated with lymphocyte-mediated inhibition of macrophage migration from capillary tubes.

Authors:  A M Dvorak; M E Hammond; H F Dvorak; M J Karnovsky
Journal:  Lab Invest       Date:  1972-12       Impact factor: 5.662

4.  Positive and negative colloidal iron as cell surface electron stains.

Authors:  G J Gasic; L Berwick; M Sorrentino
Journal:  Lab Invest       Date:  1968-01       Impact factor: 5.662

5.  Antigen-macrophage interaction. I. Hapten-specific inhibition of antigen interaction with macrophages from immune animals.

Authors:  B E Cohen; A S Rosenthal; W E Paul
Journal:  J Immunol       Date:  1973-09       Impact factor: 5.422

6.  Properties of antibodies cytophilic for macrophages.

Authors:  A Berken; B Benacerraf
Journal:  J Exp Med       Date:  1966-01-01       Impact factor: 14.307

7.  Phagocytosis of immune complexes by macrophages. Different roles of the macrophage receptor sites for complement (C3) and for immunoglobulin (IgG).

Authors:  B Mantovani; M Rabinovitch; V Nussenzweig
Journal:  J Exp Med       Date:  1972-04-01       Impact factor: 14.307

8.  The interaction of soluble horseradish peroxidase with mouse peritoneal macrophages in vitro.

Authors:  R M Steinman; Z A Cohn
Journal:  J Cell Biol       Date:  1972-10       Impact factor: 10.539

9.  The cytotoxic effect of mouse macrophages on syngeneic and allogeneic erythrocytes.

Authors:  H Melsom; R Seljelid
Journal:  J Exp Med       Date:  1973-03-01       Impact factor: 14.307

10.  The interaction between Toxoplasma gondii and mammalian cells. I. Mechanism of entry and intracellular fate of the parasite.

Authors:  T C Jones; S Yeh; J G Hirsch
Journal:  J Exp Med       Date:  1972-11-01       Impact factor: 14.307

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  6 in total

1.  Determination of binding strength and kinetics of binding initiation. A model study made on the adhesive properties of P388D1 macrophage-like cells.

Authors:  J L Mege; C Capo; A M Benoliel; P Bongrand
Journal:  Cell Biophys       Date:  1986-04

2.  Use of cell contour analysis to evaluate the affinity between macrophages and glutaraldehyde-treated erythrocytes.

Authors:  J L Mege; C Capo; A M Benoliel; P Bongrand
Journal:  Biophys J       Date:  1987-08       Impact factor: 4.033

3.  TMA-DPH a fluorescent probe of membrane dynamics in living cells. How to use it in phagocytosis.

Authors:  D Illinger; M Kubina; G Duportail; P Poindron; J Bartholeyns; J G Kuhry
Journal:  Cell Biophys       Date:  1989-02

4.  Enhanced binding of phosphatidylserine-containing lipid vesicle targets to RAW264 macrophages.

Authors:  D Rimle; W Dereski; H R Petty
Journal:  Mol Cell Biochem       Date:  1984-09       Impact factor: 3.396

5.  Macrophage signal recognition.

Authors:  D M Weir
Journal:  Agents Actions       Date:  1984-08

6.  Role of Ca2+ ion on Leishmania-macrophage attachment.

Authors:  S Misra; K Naskar; D Sarkar; D K Ghosh
Journal:  Mol Cell Biochem       Date:  1991-03-27       Impact factor: 3.396

  6 in total

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