Biomedical subjects

M A Tahri-Jouti

Publications and source records attributed to M A Tahri-Jouti.

5 recordsLinked to original sources

PubMed2001

Physiological difference during ethanol fermentation between calcium alginate-immobilized Candida tropicalis and Saccharomyces cerevisiae.

Calcium alginate-immobilized Candida tropicalis and Saccharomyces cerevisiae are compared for glucose fermentation. Immobilized C. tropicalis cells showed a slight morphological alteration during ethanol production at 40 degrees C, but their fermentation capacity was reduced by 25%. Under immobilization conditions, the two species demonstrated two different mathematical patterns when the relationship between growth rate, respiration rate, and ethanol tolerance was assessed. The interspecific difference in behavior of immobilized yeast cells is mainly due to their natural metabolic preference. The production of CO(2) by calcium alginate-immobilized C. tropicalis, as well as the lower supply of oxygen to the cells, are the major factors that reduce ethanol production.

Alginates↗

PubMed1991

Binding of endotoxin to macrophages: distinct effects of serum constituents.

The respective roles of serum lipoproteins, and of the complement component C3, in the binding of endotoxin (LPS) to macrophages were analyzed by an in vitro assay using [3H]LPS. The addition of an anti-C3 serum in the medium induced an apparent abolishment of the specific binding of LPS to mouse macrophages, but this effect appeared to be due to an actual increase of nonspecific binding. Isolated complexes of LPS with lipoproteins of high density (HDL3) and of very high density (VHDL) did not bind to macrophages. Furthermore, addition of HDL3 and VHDL in the incubation medium inhibited the specific binding of LPS to macrophages. These results suggest that C3 reduces nonspecific interactions between LPS and macrophages whereas associations between LPS and HDL3 or VHDL inhibit specific LPS-macrophage interactions.

Animals↗

PubMed1990

Specific binding of lipopolysaccharides to mouse macrophages--I. Characteristics of the interaction and inefficiency of the polysaccharide region.

Tritium-labeled lipopolysaccharide interacted specifically and reversibly with mouse peritoneal macrophages. The binding was higher at 22 degrees C than at 4 degrees C, but was no longer observable at 37 degrees C. The specificity of the interaction (inhibition with unlabeled LPS) was strictly dependent on the presence of serum, and required divalent cations. The binding was saturable. The specific binding sites of peritoneal macrophages were saturated with 6-9 x 10(6) LPS molecules/cell, and those of macrophage-like cell lines with 2-3 x 10(6) molecules/cell. The binding of LPS was not inhibited by ligands of scavenger receptors (maleylated BSA) or complement receptors (zymosan), but was strongly inhibited with dexamethasone, a glucocorticoid which is known to modulate the expression of other surface markers of macrophages. The polysaccharide region of the LPS, as well as 3-deoxy-2-octulosonic acid (KDO) coupled to bovine serum albumin, did not bind to macrophages, whereas a specific binding was observed with a lipid A-BSA conjugate.

Animals↗

PubMed1990

Specific binding of lipopolysaccharides to mouse macrophages--II. Involvement of distinct lipid a substructures.

The interaction of lipopolysaccharide-binding sites of mouse macrophages with the Lipid A region of endotoxins (LPS) was demonstrated by direct binding of labeled Lipid A conjugates, by inhibition of the binding of labeled LPS with anti-Lipid A monoclonal antibodies, and by the considerable reduction of this binding after chemical and enzymatic removal of the fatty acid esters of the LPS. The substructures of Lipid A required for the specific binding of LPS to macrophages were analyzed by the use of synthetic lipids consisting of mono- or disaccharide derivatives of glucosamine. The two phosphate groups of Lipid A (at positions 1 and 4') as well as certain hydroxyl groups, appeared to play a critical role in the binding. However, the reactivities of the synthetic lipids with the macrophage surface, as compared with those with anti-Lipid A antibodies, could hardly be explained by the existence of a single LPS receptor, and suggested the presence, on the macrophage surface, of different LPS-binding sites that recognize different substructures or spatial configurations of the lipid moiety of endotoxins.

Animals↗

PubMed1989

Effects of lipopolysaccharide on macrophages analyzed with anti-lipid A monoclonal antibodies and polymyxin B.

Six monoclonal antibodies (mAb) to the lipid A region of bacterial lipopolysaccharide (LPS), obtained from mice immunized with lipid A-coated Bordetella pertussis cells (mAb 3.E8, 2.21, 2.37, 2.41) or with lipid A covalently coupled to keyhole limpet hemocyanin (mAb R1 and R7), were examined for their potential to inhibit in vitro activities of LPS on macrophages. mAb R7 was inactive in vitro, but the five other mAb inhibited efficiently some in vitro activities of LPS. mAb R1, 2.21 and 3.E8 reduced the LPS-induced secretion of tumor necrosis factor (TNF) and interleukin 1 (IL 1) by macrophages, but did not modify the binding of LPS to macrophages. On the other hand, mAb 2.37 and 2.41 reduced LPS binding to macrophages and subsequent IL1 secretion, but did not modify TNF production. This is in agreement with our previous finding that IL1 and TNF productions can be selectively triggered by synthetic analogs of lipid A substructures (Lasfargues and Chaby, Cell. Immunol. 1988. 115: 165). The pattern of in vitro inhibition of LPS activities (LPS binding to macrophages and production of TNF and membrane IL 1) by polymyxin B was different from those of the two groups of anti-lipid A mAb mentioned above. These observations suggest the presence on lipid A of four functionally distinct substructures.

Animals↗