MICROBIOCENOSIS OF THE ORAL CAVITY IN CHILDREN WITH INBORN CLEFT LIP AND PALATE

Treatment of children with ARH is one of the most difficult tasks of modern reconstructive surgery of the maxillofacial area. The problem lies not only in the correction of the anatomical defect, but also in the full restoration of the function of the structures of the palatopharyngeal region. The microbiocenosis of the oral cavity is an important indicator of the functional and metabolic activity of the tissues of the oral cavity. The modern stage in the development of dentistry is characterized by the introduction of new effective preventive and diagnostic measures, which has become possible thanks to the discoveries made in the study of the mechanisms of formation of the pathological condition. The modern stage in the development of dentistry is characterized by the introduction of new effective preventive and diagnostic measures, which has become possible thanks to the discoveries made in the study of the mechanisms of formation of the pathological condition. The results of microbiological studies showed that in children with ADH before surgery, a significant shift in the qualitative composition of microflora towards pathogenic species was revealed, as well as quantitative changes in the normal stabilizing microflora of the oral cavity. Correction of microbiocenosis of the oral cavity is required before and after uranoplasty

Syntenin-1 Is a New Component of Tetraspanin-Enriched Microdomains: Mechanisms and Consequences of the Interaction of Syntenin-1 with CD63

Tetraspanins are clustered in specific microdomains (named tetraspanin-enriched microdomains, or TERM) in the plasma membrane and regulate the functions of associated transmembrane receptors, including integrins and receptor tyrosine kinases. We have identified syntenin-1, a PDZ domain-containing protein, as a new component of TERM and show that syntenin-1 specifically interacts with the tetraspanin CD63. Detailed biochemical and heteronuclear magnetic resonance spectroscopy (NMR) studies have demonstrated that the interaction is mediated by the C-terminal cytoplasmic region of the tetraspanin and the PDZ domains of syntenin-1. Upon interaction, NMR chemical shift perturbations were predominantly localized to residues around the binding pocket of PDZ1, indicating a specific mode of recognition of the cytoplasmic tail of CD63. In addition, the C terminus of syntenin-1 has a stabilizing role in the CD63-syntenin-1 association, as deletion of the last 17 amino acids abolished the interaction. The CD63-syntenin-1 complex is abundant on the plasma membrane, and the elevated expression of the wild-type syntenin-1 slows down constitutive internalization of the tetraspanin. Furthermore, internalization of CD63 was completely blocked in cells expressing a syntenin-1 mutant lacking the first 100 amino acids. Previous results have shown that CD63 is internalized via AP-2-dependent mechanisms. Hence, our data indicate that syntenin-1 can counteract the AP-2-dependent internalization and identify this tandem PDZ protein as a new regulator of endocytosis