Biomedical subjects

Anne-Laure Bolcato-Bellemin

Publications and source records attributed to Anne-Laure Bolcato-Bellemin.

4 recordsLinked to original sources

PubMed2006

Glycated polyelectrolyte multilayer films: differential adhesion of primary versus tumor cells.

Glycated polymers have already been widely employed for cell transfection studies, as cells possess specific lectins. However, up to now, these glycated polymers have barely been investigated for their cell adhesive properties, save macrophages. In this work, we use polyelectrolyte multilayer films made of poly(L-lysine) and poly(L-glutamic) acid as polymeric substrates to investigate the role of sugar molecules (e.g., mannose and lactose) on the adhesion of primary cells as compared to that of a tumor cell line. The glycated polymeric films were compared to ungrafted and chemically cross-linked films, which are known to present opposite adhesive properties. A differential adhesion could be evidenced on mannose grafted films: primary chondrocytes adhere and proliferate well on these films, whereas chondrosarcoma cells do not grow well. Although present, the effect of lactose on cell adhesion was much less important. This adhesion, mediated by glycated polymers, appears to be specific. These results show that it is possible to use glycated polyelectrolytes not only as nonviral vectors but also as cell adhesive substrates.

Adhesiveness↗

PubMed2005

Antifungal coating by biofunctionalized polyelectrolyte multilayered films.

The surface of medical devices is a common site of bacterial and fungal adhesion, first step to the constitution of a resistant biofilm leading frequently to chronic infections. In order to prevent such complications, several physical and chemical modifications of the device surface have been proposed. Here, we experiment a new type of topical antifungal coating using the layer-by-layer technique. The nanometric multilayer film obtained by this technique is functionalized by the insertion of a chromogranin A-derived antifungal peptide (CGA 47-66, chromofungin). We show that the embedded peptide keeps its antifungal activity by interacting with the fungal membrane and penetrating into the cell. In vitro studies demonstrate that such an antifungal coating is able to inhibit the growth of yeast Candida albicans by 65% and completely stop the proliferation of filamentous fungus Neurospora crassa. The cytotoxicity of such a coating was also assessed by growing human gingival fibroblasts at its surface. Finally, the antifungal coating of poly(methylmethacrylate), a widely used material for biomedical devices, is successfully tested in an in vivo oral candidiasis rat model. Taken together, these results assessed the functionalized multilayer films containing a new potent antifungal non-toxic peptide, as a novel and promising technique for local antifungal protection.

Amino Acid Sequence↗

PubMed2004

Molecular cloning and characterization of mouse LITAF cDNA: role in the regulation of tumor necrosis factor-alpha (TNF-alpha) gene expression.

The inflammatory response to bacteria and bacterial products, such as lipopolysaccharides (LPSs), is mediated by a variety of secreted factors, but cytotoxic effects of LPS have been ascribed to the tumor necrosis factor alpha (TNF-alpha) activity. TNF-alpha is probably the most pleiotropic cytokine and, given the deleterious effects to the host of this factor, it has been postulated that its expression must be tightly regulated. Our laboratory has recently isolated, cloned and characterized a novel human transcription factor named LITAF or LPS-induced TNF-alpha factor. The present study reports the isolation, cloning and characterization of the mouse LITAF cDNA. Chromosomal localization revealed that mouse LITAF mapped to mouse chromosome 16, in a region highly homologous with the area on which human LITAF was previously located. Northern blot analysis shows that mouse LITAF is already expressed at embryonic day 7 of development, and is highly expressed in adult liver, heart and kidney. Moreover, upon LPS stimulation, we show that: (i) LITAF expression is increased in a mouse monocyte/macrophage cell line; and (ii) TNF-alpha expression is reduced in ES cell-derived macrophages lacking one copy of LITAF gene. Taken together, these results highlight the important role of LITAF in the regulation of TNF-alpha gene expression and suggest a potential role of LITAF in mouse organogenesis.

Amino Acid Sequence↗

PubMed2003

Kruppel-like factors regulate the Lama1 gene encoding the laminin alpha1 chain.

Laminin-1 (alpha1beta1gamma1), a basement membrane (BM) constituent, has been associated with differentiation processes and also with malignant progression. In the intestinal tissue, the alpha1 chain is expressed and secreted in the subepithelial BM during the developmental period; in the adult rodent tissue, it is restricted to the BM of the dividing cells. To understand how laminin alpha1 chain expression is regulated, we cloned and characterized a 2-kb promoter region of the Lama1 mouse gene. Analysis of the promoter was conducted in the Caco2-TC7 intestinal epithelial cells by transient transfection of serially deleted and site-directed mutated promoter constructs, by electrophoretic mobility shift assays, and expression of selected transcription factors. We determined that a proximal region, which includes an Sp1-binding GC box and a Krüppel-like element, was important for the promoter activity. This region is conserved between the human and mouse genes. Interestingly, two Krüppel-like factors KLF4 and KLF5 exhibit opposing effects on the Lama1 promoter activity that are decreased and increased, respectively, in the intestinal epithelial cells. These data corroborate the complementary expression of KLF4 and KLF5 along the intestinal crypt-villus axis and the parallel expression of KLF5 and laminin alpha1 chain in the crypt region. Finally, we showed that glucocorticoids stimulate the promoter activity. This study is the first characterization of the Lama1 promoter; we identified regulatory elements that may account for the expression pattern of the endogenous protein in the mouse intestine.

Animals↗