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1.
Arkh Patol ; 85(4): 59-64, 2023.
Artículo en Ruso | MEDLINE | ID: mdl-37530192

RESUMEN

The article describes a rare case of small cell neuroendocrine carcinoma of the endometrium in a 67-year-old woman. According to the literature, only about 90 such observations have been described worldwide. Histological examination revealed three necessary features: the small-cell nature of the tumor, the presence of epithelial and neuroendocrine markers. An IHC study revealed a positive expression of Syn, Chrom A, CD56, CK AE1/AE3 markers; the proliferative activity index was 70%.


Asunto(s)
Carcinoma Neuroendocrino , Carcinoma de Células Pequeñas , Femenino , Humanos , Anciano , Biomarcadores de Tumor/metabolismo , Inmunohistoquímica , Carcinoma de Células Pequeñas/genética , Carcinoma de Células Pequeñas/patología , Endometrio/metabolismo , Carcinoma Neuroendocrino/diagnóstico , Carcinoma Neuroendocrino/genética , Carcinoma Neuroendocrino/metabolismo
2.
Appl Opt ; 55(17): 4763-8, 2016 Jun 10.
Artículo en Inglés | MEDLINE | ID: mdl-27409037

RESUMEN

The influence of water vapor on the reflection coefficient of multilayer mirrors was studied using a gas cell with multiple reflections from the mirrors. A strong change in the reflection coefficient of the mirrors (up to 0.9%) was found when water vapor under a pressure of 23 mbar was injected into the cell, which was interpreted as a change in the refraction index of the layers of multilayer coatings when water vapor penetrated into the porous coating structure.

3.
Bioorg Khim ; 23(10): 771-82, 1997 Oct.
Artículo en Ruso | MEDLINE | ID: mdl-9490612

RESUMEN

The [Nle18]-(87-136)-bacterioopsin, a fragment of bacterioopsin from Halobacterium salinarium synthesized by solid phase technique, was solubilized in a 1:1 chloroform-methanol mixture containing 0.1 M LiClO4 and studied by two-dimensional 1H NMR spectroscopy. The complete assignment of proton resonances was performed in the DQF-COSY, TOCSY, and NOESY spectra of this peptide, and its spatial structure was computed. As a result, two helical regions (92-100 and 108-130) were identified, which correspond to the C-terminal part of segment C and to segment D of bacteriorhodopsin, respectively. The 92-100 region forms a right-handed alpha-helix, and the 108-130 region can adopt right-handed alpha-helical, 3(10)-helical, and combined (from the two) conformations. A comparison of the structure computed with the bacteriorhodopsin model deduced from the electron cryomicroscopy data showed good agreement in the 91-100 region (the root-mean-square deviation of the backbone atoms was less than 0.51 A) and considerable differences in the 108-130 region (1.82 A). A dynamic model of the conformation of the D transmembrane segment was suggested, and the accordance of the model to the functional dynamics of bacteriorhodopsin was discussed.


Asunto(s)
Bacteriorodopsinas/química , Secuencia de Aminoácidos , Bacteriorodopsinas/síntesis química , Halobacterium salinarum , Espectroscopía de Resonancia Magnética , Modelos Estructurales , Datos de Secuencia Molecular , Fragmentos de Péptidos/química
4.
Mol Gen Mikrobiol Virusol ; (3): 27-31, 1996.
Artículo en Ruso | MEDLINE | ID: mdl-8999315

RESUMEN

Peptides were synthesized, which, according to theoretical analysis of the antigenic structure of protein VP1 of foot-and-mouth disease (FMD) virus types A, 0, and Asia 1, corresponded to potential immunodominant protein sites. Activities of the peptides were studied by solid-phase indirect radioimmunoassay on polyethylene film with purified immunoglobulins against intact FMD virus. Virtually no cross reactions were observed. Blood sera of cattle convalescent after FMD were tested with the FMD virus and peptides containing VP1 fragments 141-160 (A22 No. 550), 140-160 (O1 No. 194), and 140-153 (Asia 1 No. 48). The specificity of interactions between the sera and peptides and the virus was uniform, this permitting the identification of the virus type which caused the disease.


Asunto(s)
Antígenos Virales/sangre , Aphthovirus/inmunología , Cápside/sangre , Fiebre Aftosa/inmunología , Epítopos Inmunodominantes/sangre , Secuencia de Aminoácidos , Animales , Proteínas de la Cápside , Bovinos , Fiebre Aftosa/virología , Datos de Secuencia Molecular , Péptidos/química
5.
Bioorg Khim ; 18(7): 942-50, 1992 Jul.
Artículo en Ruso | MEDLINE | ID: mdl-1445430

RESUMEN

A peptide VP1-(142-158)-MAP (Multiple antigen peptide system) consisting of two parts: a lysine matrix made up of three levels of lysine residues coupled with each other and amino acid sequence 142-158 of VP1 of FMD virus strain A(22)550--has been synthesized. Guinea-pigs inoculated with 20 mkg of the peptide incorporated with Freund's complete adjuvant were protected against challenge with 500 ID50 of homologous FMD virus. Sheep were immunized with a single inoculation of the peptide in a dose of 1.0 mg. Cattle inoculated twice with 1.5 mg of the peptide with incomplete adjuvant on the basis of synthetic oil developed high virus-specific antibody titres both after the first (5.3-7.6 log2 ND50/0.1 ml) and the second inoculation (10.2-11.0 log2 ND50/0.1 ml). The peptide-immunized animals were resistant to challenge with homologous virulent virus in a dose of 10(4) ID50. The immunogenic and protective capacities of the peptide VP1-(142-158)-MAP were shown to be greater as compared with those of its linear analogue-peptide VP1-(141-160).


Asunto(s)
Fiebre Aftosa/prevención & control , Lisina/química , Péptidos/uso terapéutico , Secuencia de Aminoácidos , Animales , Bovinos , Cromatografía en Gel , Susceptibilidad a Enfermedades , Cobayas , Inmunización , Datos de Secuencia Molecular
6.
Bioorg Khim ; 15(9): 1193-205, 1989 Sep.
Artículo en Ruso | MEDLINE | ID: mdl-2556150

RESUMEN

A synthesis of new fragments of VP1 protein with the specificity of A22 strain of foot-and-mouth disease virus is described. Immunization with the free 136-152 peptide and KLH-conjugates of the peptides 136-152 and 197-213 induced 60-80% protection of guinea pigs against challenge with the A22 virus. Synthetic peptides corresponding to the 10-24, 50-69 and 175-189 sequences of VP1 did not show any protective activity. We have found that uncoupled peptides 175-189 and 197-213 are able to induce antipeptide antibodies. However, these antibodies did not possess any neutralizing activity. Immunization of animals with the mixture of (136-152)O1K and (175-189)A22 has led to inhibition of the immune response to the (136-152)O1K fragment.


Asunto(s)
Antígenos Virales/inmunología , Aphthovirus/inmunología , Proteínas Virales/síntesis química , Secuencia de Aminoácidos , Animales , Cromatografía por Intercambio Iónico , Cromatografía en Capa Delgada , Cobayas , Datos de Secuencia Molecular , Proteínas Virales/inmunología
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