RESUMEN
Several recent reports imply the possibility of cariogenicity and periodontal disease linked to denture plaque containing Candida albicans. Adhesion of oral bacteria and Candida species to the extracellular matrix, such as type I collagen, fibronectin and denatured type I collagen, was examined by using adenosine triphosphate (ATP) analysis. The adhesion of C. albicans to intact and denatured type I collagen was significantly greater than those of oral bacteria and other species of Candida. This result suggests that C. albicans possesses the ability to adhere specifically to extracellular matrix, as compared with other Candida species or oral bacteria.
Asunto(s)
Adhesión Bacteriana/fisiología , Candida albicans/fisiología , Adhesión Celular/fisiología , Colágeno/metabolismo , Boca/microbiología , Colágeno/química , Proteínas de la Matriz Extracelular/metabolismo , Fibronectinas/metabolismo , Técnicas In Vitro , Streptococcus/fisiología , Propiedades de SuperficieRESUMEN
An inhibition assay of Candida albicans adhesion to gelatin-immobilized membranes was compared with that to intact type I collagen-immobilized membranes using an arginine-glycine-aspartic acid (RGD) containing peptide. As compared with a protein-free membrane, gelatin and collagen significantly enhanced the adherence of C. albicans. The adhesion of the yeast to gelatin was significantly inhibited by the RGD peptides, but not by arginine-glycine-glutamic acid (RGE) peptides. In contrast, attachment to collagen was not inhibited by RGD peptides. These results suggest that the RGD sequence of gelatin and the integrin-like proteins of yeasts may be involved in adherence.
Asunto(s)
Candida albicans/fisiología , Colágeno Tipo I/química , Adhesividad , Candida albicans/efectos de los fármacos , Gelatina/química , Humanos , Integrinas/fisiología , Membranas Artificiales , Oligopéptidos/farmacología , Receptores Inmunológicos/fisiología , Propiedades de SuperficieRESUMEN
The differentiation of human embryo chondrocytes was markedly induced by the addition of Bt2cAMP to the culture medium. Using this culture system, a novel human cDNA for a basic helix-loop-helix (bHLH) protein (named DEC1) expressed primarily in the chondrocytes in response to Bt2cAMP was cloned by the subtractive hybridization method. DEC1 protein consists of 412 amino acids and exhibits structural similarities to the mammalian HES family, Drosophila hairy, and Enhancer of split m7 in the bHLH region. Northern blot analysis showed that DEC1 mRNA was expressed in various tissues including the cartilage, lung, spleen, and intestine, but not in the brain. These findings suggest that the bHLH factor DEC is involved in the control of cell differentiation in several tissues including cartilage.