Functional disorders in patients with lip and nose deformity after cheilorhinoplasty. / Funktsional'nye narusheniya u patsientov s deformatsiei guby i nosa posle odnostoronnei kheilorinoplastiki.

Clinical analysis of the nasolabial complex in patients suffering of the unilateral cleft lip and palate deformity after cheilorhinoplasty is presented in the article. Functional disorders such as nasal breathe impairment and it's relation to the nasolabial muscle dystonia in the dependency of primary cheilorhinoplasty type are analyzed. The plan of surgical treatment as well as the postoperative rehabilitation using the botulotoxin injections is offered.

[Nasal breath recovery and rhinoplasty in cleft lip and palate patient with unilateral choanal atresia].

The paper presents the analysis of clinical case of endoscopic nasal breath restoration and elimination of the secondary cleft lip nasal deformity in 27 years old patient with unilateral choanal atresia and secondary nasal deformity after rhinocheiloplasty. Preoperative examination revealed the absence of nasal breathing on collateral side due to complete bone choanal atresia. Surgical treatment included endoscopic choanal repair, elimination of the secondary nasal deformity, septoplasty, conchotomy and lateroposition of the inferior conchae. The treatment resulted in nasal breath restoration and elimination of nasal deformity. Long-term follow-up at 1 and 12 months post-operatively proved stable positive aesthetic and functional results.

Human sperm surface glycoprotein involved in sperm-zona pellucida interaction.

To identify peptide-specific antibodies which define sperm surface antigens, hybridomas were derived from the splenocytes of mice immunized with swollen human spermatozoa which had been subjected to limited proteolytic cleavage under reducing conditions prior to immunization. A total of 13.7% of the hybrid clones secreted antibodies which reacted with deglycosylated human seminal plasma glycoproteins when screened by an ELISA. A monoclonal antibody, designated mAb 4A8 sp., specifying a peptide epitope of human epididymal and a sperm surface glycoprotein was selected which inhibited human sperm-egg binding in a dose-dependent manner, and totally blocked sperm penetration in vitro. This inhibition did not result from an effect of the antibody on the motility of spermatozoa, nor was it due to premature induction of the acrosome reaction. Exclusion of oligosaccharide chains by chemical hydrolysis with trifluoromethane sulphonic acid (TFMS), enzymatic degradation and binding of lectins, did not abrogate the reactivity of mAb 4A8 to the cognate epitope whereas antibody binding was precluded upon digestion with proteolytic enzymes. In Western immunoblots of human seminal plasma glycoproteins, the antigen presented as a set of immunoreactive polypeptides, a major glycoprotein of M(r) 78 kDa and less prominent bands of M(r) 56 and 44 kDa. Immunocytochemical staining of a number of human reproductive and somatic tissues revealed strong immunostaining of the luminal epithelium of the epididymis as well as of spermatozoa in the lumen. Immunolocalization to the plasma membrane of ejaculated human spermatozoa was demonstrated by immunofluorescence, although on undigested spermatozoa the antigen epitope was less accessible. Upon capacitation the antigen persisted on the sperm surface and was present on the head of capacitated acrosome-intact spermatozoa. The pronounced peripheral immunostaining of the sperm head was accentuated after DTT/trypsin treatment, implicating the dynamic accessibility of the epitope on the plasma membrane of capacitated spermatozoa. It is suggested that the protein in question appears on the sperm membrane as a consequence of its modification in the epididymis (insertion and processing), and may be involved in the processes leading to sperm attachment and interaction with the human zona pellucida.

Monoclonal antibodies reacting against capacitated but not with freshly ejaculated boar spermatozoa.

PROBLEM: The involvement of individual sperm proteins in differentiation of antigenically specific and functionally defined regions on sperm membrane has not yet been completely elucidated. METHOD: BALB/c mice were immunized with live capacitated boar spermatozoa and used for production of monoclonal antibodies (MAbs). ELISA, IIF, SDS-PAGE, IVF, and cytologic methods were used for selection and biological characterization of MAbs as well as for identification of corresponding antigens. RESULTS: MAb1F10, MAb2E2, and MAb4B12 react with antigens in the acrosome portion of live capacitated spermatozoa, MAb 1F10 reacted with human sperm cells along with those from bull, ram, mouse, dog, whereas MAb2E2--with mouse's spermatozoa and MAB4B12-with bull's, mouse's, and dog's spermatozoa. Some glycolytic enzymes seemed to reduce mildly the reactions of the MAbs with enzyme treated sperm cells; proteolytic enzymes eliminated the binding of MAbs to the sperm acrosome. These MAbs have no sperm agglutinating and/or sperm-immobilizing activities and reduced the number of spermatozoa binding to zona pellucida. CONCLUSIONS: MAb1F10, MAb2E2, and MAb4B12 seemed to recognize membrane associated antigens with potential role in the initial stages of fertilization, specific for capacitated but not for freshly ejaculated spermatozoa.

Monoclonal antibodies to porcine zona pellucida that block the initial stages of fertilization.

Zona pellucida (ZP) is thought to be of utmost biological importance in the early stages of fertilization and implantation. Current hybridoma technology was used to produce monoclonal antibodies (MAbs) against specific antigens to porcine ZP. Two monoclonal antibodies (4F2 and 2D9) were raised that reacted against ZP antigens shared by human and porcine ZP. These antibodies were shown to block fertilization of human oocytes in in vitro fertilization (IVF). It is likely that MAb 4F2 recognized a protein epitope localized on the outer surface of ZP. These antibodies may be quite useful immunologic probes for studying the precise mechanisms of the early events of fertilization in mammals.