Impact of abutment microstructure and insertion depth on crestal bone changes at nonsubmerged titanium implants with platform switch.

Objectives: To assess the impact of microgrooved abutments and the insertion depth on crestal bone changes at titanium implants with platform switch.

Materials And Methods: A total of n = 3 titanium implants (conical abutment connection) were inserted in each hemimandible of n = 6 foxhounds with the implant shoulder (IS) located at either epicrestal, supracrestal (+1 mm), or subcrestal (-1 mm) positions and randomly (split-mouth design) connected with machined or partially microgrooved healing abutments. At 20 weeks, tissue biopsies were processed for histological (primary outcome: net bone loss - NET) analyses.

[Synthesis of peptide fragments of high-affinity receptor FcepsilonR1 and study their binding with allergen-specific immunoglobulin E].

High-affinity receptor FcepsilonR1 is a key substance which participates in IgE-dependent allergic reactions of immediate type. A minimal sequence Arg136-Asn137-Trp138-Asp139, which takes part in binding with C3 and C4 fragments of IgE was determined by methods of computer analysis. As possible analogs of FcepsilonR1 receptor, capable of binding to Fc-fragment IgE, a number of peptide compounds containing this sequence were proposed.

[New bioaffine sorbents for selective elimination of autoantibodies against human thyroperoxidase in autoimmune thyroid diseases].

New bioaffine sorbents containing bioselective ligand, synthetic analog of the human thyroperoxidase antigenic determinant--tetrapeptide H-Glu-Gln-betaAla-Lys-OMe, immobilized on two polymeric matrixes--a polyacrylamide gel and CNBr-activated sepharose 4B were synthesized. The offered immunosorbents were shown have high selectivity in relation to autoantibodies against thyroperoxidase and can find an application for medicine and experimental biochemistry for selective elimination of autoantibodies from serum or plasma of the patients suffering from autoimmune thyroid diseases.

Effect of N-terminal tripeptides of bombesin, litorin, and their analogue on body temperature and vasomotor responses.

Intranasal administration of bombesin caused hypothermia in rats maintained under cold conditions. N-terminal tripeptide of bombesin exhibits intrinsic vasomotor activity, while intranasal administration of its modified analogue produced a more potent hypothermic effect than intranasal bombesin.

[Synthesis of modified fragments of fibrinogen and their effect on the activity of proteolytic enzymes].

New analogues of the Gly-Pro-Arg and Arg-Gly-Asp fragments of fibrinogen were synthesized: Gly-Pro-Arg-Pro (I), Gly-Pro-Arg-Pro-Met-OMe (II), Gly-Pro-Arg-Pro-Phe (III), Gly-Pro-Arg-Pro-Asp (IV), Gly-Pro-Arg-Pro-Glu (V), and Arg-Asn-Trp-Asp (VI). Their effect on the activity of proteases of various types was studied with the method of lysis of fibrin plates. All the peptides were found to inhibit plasmin activity (by 60-85%) and the gamma-subunit of nerve growth factor (by 55-93%).