RESUMEN
Two transglutaminase-mediated modifications of the rat epididymal spermatozoon surface were demonstrated in vitro. Transglutaminase was effective in promoting the binding of spermidine to the sperm. Moreover, the enzyme, by reacting with one of the major proteins secreted by the rat seminal vesicle epithelium, produced a modified form of the protein with a higher molecular weight and the capability of binding to the sperm cells. A specific physiological role for the enzyme, bringing about modifications of the rat sperm surface in the seminal fluid environment, is suggested.
Asunto(s)
Aciltransferasas/farmacología , Espermatozoides/efectos de los fármacos , Animales , Autorradiografía , Electroforesis en Gel de Poliacrilamida , Epidídimo/fisiología , Masculino , Ratas , Semen/fisiología , Espermidina/metabolismo , TransglutaminasasRESUMEN
The in vitro effect of seminal vesicle protein IV (SV-IV) on the cytotoxic activity of human natural or acquired cellular immunity has been investigated by standard immunological procedures, a (51)Cr-release cytotoxicity assay, and labeled-ligand binding experiments. The data obtained demonstrate that: (1) fluoresceinated or [(125)I]-labeled SV-IV binds specifically to the surface of human purified non-adherent mononuclear cells (NA-MNC); (2) SV-IV suppresses the cytotoxicity of natural killer (NK) cells against K562 target cells, that of IL-2-stimulated NK (LAK) cells against DAUDI target cells, and that of VEL antigen-sensitized cytotoxic T lymphocytes (CTLs) against VEL target cells; (3) treatment of K562 target cells alone with SV-IV decreases their susceptibility to NK-induced lysis. These findings indicate that the protein SV-IV has a marked in vitro inhibitory effect on NK, LAK and CTL cytotoxicity, providing a better understanding of its immune regulatory functions.
Asunto(s)
Células Asesinas Activadas por Linfocinas/inmunología , Células Asesinas Naturales/inmunología , Leucocitos Mononucleares/inmunología , Proteínas de Secreción de la Vesícula Seminal/metabolismo , Linfocitos T Citotóxicos/inmunología , Línea Celular Tumoral , Citotoxicidad Inmunológica , Humanos , Inmunidad Celular , Células K562 , Células Asesinas Activadas por Linfocinas/metabolismo , Células Asesinas Naturales/metabolismo , Leucocitos Mononucleares/metabolismo , Proteínas de Secreción de la Vesícula Seminal/inmunología , Proteínas de Secreción de la Vesícula Seminal/aislamiento & purificación , Linfocitos T Citotóxicos/metabolismoRESUMEN
Human telomerase reverse transcriptase (hTERT) gene expression in resected specimens of oral squamous cell carcinoma (OSCC) and their surrounding tissue, either apparently normal or clearly histologically dysplastic, was evaluated by both real-time RT-PCR and immunohisto-chemical protein analyses. The expression level of hTERT in oral dysplasia and in OSCC was markedly higher than in normal tissues. The correlation between hTERT expression in OSCC and clinico-pathological parameters or survival of OSCC patients was statistically analyzed. Our study demonstrates that there is no significant relationship between hTERT expression and classical clinico-pathological parameters. Interestingly, survival analysis showed both overexpressing cases and lower survival rate in the early stage of OSCC (p=0.03 for immunohistochemistry; p=0.04 for RT real-time PCR). The histological location of hTERT in these tumors has been discussed in the context of the cancer stem cell theory.
Asunto(s)
Carcinoma de Células Escamosas/metabolismo , Carcinoma de Células Escamosas/patología , Expresión Génica , Neoplasias de la Boca/metabolismo , Neoplasias de la Boca/patología , Telomerasa/metabolismo , Adulto , Anciano , Anciano de 80 o más Años , Carcinoma de Células Escamosas/mortalidad , Femenino , Humanos , Inmunohistoquímica , Masculino , Persona de Mediana Edad , Neoplasias de la Boca/mortalidad , Pronóstico , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Análisis de Supervivencia , Telomerasa/genéticaRESUMEN
The effect of nontoxic, low concentrations (10(-8) M) of retinoic acid (RA) for a relatively long time (28 days) on a Kirsten ras-virus transformed cell line (Ki-SVC1), derived from the rat seminal vesicle epithelium, was investigated. In these experimental conditions, the cell treatment with RA induced a decrease of the proliferation rate, apoptosis and a marked reduction of both anchorage-independent growth and tumorigenicity. These biological responses were either preceded or associated with important changes in adenylate cyclase/protein kinase C signaling pathways, the activation of important apoptosis-linked genes and a marked decrease of the v-Ki-ras p21 protein. The significance of these findings is discussed.
Asunto(s)
Antineoplásicos/farmacología , Proteínas Proto-Oncogénicas p21(ras)/metabolismo , Tretinoina/farmacología , Adenilil Ciclasas/metabolismo , Animales , Apoptosis/efectos de los fármacos , División Celular/efectos de los fármacos , Línea Celular Transformada , Membrana Celular/efectos de los fármacos , Membrana Celular/metabolismo , AMP Cíclico/análisis , Citosol/efectos de los fármacos , Citosol/metabolismo , Relación Dosis-Respuesta a Droga , Regulación hacia Abajo , Hemangiosarcoma/patología , Trasplante de Neoplasias , Proteína Quinasa C/metabolismo , Proteínas Proto-Oncogénicas p21(ras)/análisis , Proteínas Proto-Oncogénicas p21(ras)/genética , ARN Mensajero/análisis , Ratas , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Transducción de Señal/efectos de los fármacosRESUMEN
SV-IV, a 9.8-kd protein isolated from rat seminal vesicle secretion, has been shown to have strong non-species-specific immunosuppressive, anti-inflammatory, antithrombotic, and antiphospholipase A2 properties. The present investigation was undertaken to determine the mechanism of action of its immunosuppressive effects. It was found that SV-IV is a potent inhibitor of interleukin-1 (IL-1) release from lipopolysaccharide (LPS)-activated human adherent monocytes and an effective inhibitor of IL-1-induced thymocyte proliferation. The ability of SV-IV to form a noncovalent dimeric association with IL-1 alpha but not with IL-1 beta, its ability to induce a marked decrease of IL-1 binding to its own receptors on the thymocyte surface, and its capacity to bind specifically to the macrophage plasma membrane might play an important role in the molecular mechanism of these inhibitory effects.
Asunto(s)
Interleucina-1/antagonistas & inhibidores , Interleucina-1/metabolismo , Proteínas de Secreción Prostática , Proteínas/farmacología , Animales , Sitios de Unión/efectos de los fármacos , Adhesión Celular/efectos de los fármacos , VIH-1/fisiología , Humanos , Interleucina-6/metabolismo , Lipopolisacáridos/farmacología , Activación de Linfocitos/fisiología , Monocitos/citología , Ratas , Proteínas de Plasma Seminal , Dióxido de Silicio/farmacologíaRESUMEN
The effect of SV-IV, one of the major proteins secreted from the rat seminal vesicle epithelium, on phagocytosis and chemotaxis of human polymorphonuclear leukocytes (PMNs) has been studied. Various cytological, biochemical, metabolic, and physical correlates of both biological activities have been found to be markedly reduced by the presence in the medium of micromolar concentrations of protein SV-IV. Moreover, the Scatchard analysis of the labeled SV-IV binding to PMN cell surface has demonstrated that such binding is specific. The binding sites contain only saturable components, completely displaceable by unlabeled SV-IV. The number of the specific sites has been calculated to be 87,000/cell, with a Kd of 1.72 X 10(-7) M. The molecular mechanism of the inhibitory effect is discussed along with the possible biological and clinical implications of the experimental findings.
Asunto(s)
Quimiotaxis de Leucocito/efectos de los fármacos , Neutrófilos/efectos de los fármacos , Fagocitosis/efectos de los fármacos , Proteínas de Secreción Prostática , Proteínas/farmacología , Vesículas Seminales/metabolismo , Animales , Adhesión Celular/efectos de los fármacos , Epitelio/metabolismo , Humanos , Masculino , Neutrófilos/inmunología , Consumo de Oxígeno/efectos de los fármacos , Ratas , Ratas Endogámicas , Receptores de Formil Péptido , Receptores Inmunológicos/análisis , Proteínas de Plasma SeminalRESUMEN
The effect of porins, major hydrophobic outer membrane proteins purified from Salmonella typhimurium, on human blood coagulation was investigated. It was found that micromolar concentrations of porins accelerated markedly human blood coagulation in vitro. Using appropriate experiments, data were obtained showing that the main target of the porin-induced procoagulant effect was thrombin. A possible binding of porins with thrombin has been suggested to be the basis of this effect. The implications of this finding in the pathogenesis of the disseminated intravascular coagulation syndrome (DIC) occurring during the Gram-negative septic shock is discussed.
Asunto(s)
Coagulación Sanguínea , Coagulación Intravascular Diseminada/fisiopatología , Porinas/metabolismo , Salmonella typhimurium/metabolismo , Trombina/metabolismo , Antitrombina III/metabolismo , Antitrombinas/metabolismo , Coagulación Intravascular Diseminada/etiología , Humanos , Tiempo de Tromboplastina Parcial , Péptido Hidrolasas/metabolismo , Porinas/farmacología , Porinas/fisiología , Tiempo de Protrombina , Choque Séptico/metabolismo , Choque Séptico/fisiopatología , Síndrome , Tiempo de Coagulación de la Sangre TotalRESUMEN
Cells transformed by Kirsten murine sarcoma virus (Ki-MSV) have basal adenylate cyclase activity (AC) higher than control cells and comparable level of forskolin-stimulated AC activity. Moreover, a higher protein kinase C (PKC) activity was found to be present in the transformed cells. The molecular mechanism underlying the increase of AC activity was investigated. Our findings strongly suggest that this biochemical event is due to a marked decrease of the alpha i negative control of the enzyme, even though the alpha i of transformed cells appears to possess fully functional domains interacting with both the effector enzyme and the agonist-activated receptor.
Asunto(s)
Adenilil Ciclasas/metabolismo , Transformación Celular Viral/genética , Genes ras , Proteína Quinasa C/metabolismo , Vesículas Seminales/enzimología , Adenosina Difosfato Ribosa/metabolismo , Toxina de Adenilato Ciclasa , Animales , Colforsina/farmacología , Activación Enzimática , Células Epiteliales , Epitelio/enzimología , Epitelio/metabolismo , Proteínas de Unión al GTP/metabolismo , Masculino , Ratas , Vesículas Seminales/citología , Vesículas Seminales/efectos de los fármacos , Transducción de Señal , Factores de Virulencia de Bordetella/farmacologíaRESUMEN
Retinoic acid (RA) and sodium butyrate (NaB) are regulators of cell growth and differentiation. We studied their effect on normal (SVC1) or v-Ki-ras-transformed (Ki-SVC1) rat seminal vesicle (SV) epithelial cell lines. The treatment of these cells with 10(-((7( M RA did not produce significant changes in the morphological and biochemical parameters analyzed. When RA was used in combination with 2 mM NaB, the treatment induced substantial morphological changes, apoptosis-independent growth arrest, up-regulation of tissue transglutaminase (tTGase), and down-regulation of beta and gamma RA receptor (RAR) mRNA expression. The same cells did not express RAR alpha either before or after NaB/RA treatment. A similar treatment did not change the amount of mRNA coding for the protein SV-IV (a typical differentiation marker of the SV epithelium) in normal or ras-transformed cells nor the level of v-Ki-ras mRNA in Ki-SVC1 cells. These findings suggest that a defective RA/RARs signaling pathway is probably the biochemical condition that underlies the unresponsiveness to RA of our in vitro culture system, and indirectly points to the possibility that the NaB/RA-induced effects were brought about by a cooperation at the transcription level between the histone deacetylase inhibitory activity of NaB and the ability of RA/RAR to modulate the expression of various genes involved in the control of cell growth and differentiation.
Asunto(s)
Butiratos/farmacología , Diferenciación Celular/efectos de los fármacos , División Celular/efectos de los fármacos , Vesículas Seminales/efectos de los fármacos , Tretinoina/farmacología , Animales , Apoptosis , Secuencia de Bases , Línea Celular Transformada , Cartilla de ADN , Regulación hacia Abajo , Células Epiteliales/citología , Células Epiteliales/efectos de los fármacos , Células Epiteliales/metabolismo , Genes ras , Masculino , ARN Mensajero/genética , ARN Mensajero/metabolismo , Ratas , Receptores de Ácido Retinoico/genética , Receptores de Ácido Retinoico/metabolismo , Vesículas Seminales/citología , Vesículas Seminales/metabolismo , Transglutaminasas/metabolismoRESUMEN
The seminal vesicle protein No. 4 (SV-IV) secreted from the rat seminal vesicle epithelium, possesses immunosuppressive and anti-inflammatory properties and it is a potent inhibitor of platelet aggregation both in vivo and in vitro. This research aimed to investigate the possible effect of SV-IV on the process of human blood coagulation. Preliminary experiments showed that the recalcification time (RT) of platelet-poor plasma (PPP) samples, obtained from both normal subjects and patients affected by some hemorrhagic disorders, was found to be markedly reduced in the presence of micromolar amounts of SV-IV. It was demonstrated that the concentration of free antithrombin III (AT III) occurring in blood sera obtained from PPP samples recalcified in the presence of SV-IV was significantly decreased in comparison with sera obtained from PPP recalcified in the absence of SV-IV. It was also shown that PPP treatment with SV-IV significantly reduced the concentration of free AT III without affecting the levels of other plasma serine protease inhibitors, such as alpha 2-macroglobulin, alpha 1-antitrypsin and C1-inhibitor. In addition, the RT of PPP treated with a specific rabbit anti-AT III polyclonal antiserum (anti-AT III treated PPP) was not modified by SV-IV. These findings were confirmed by the observation that the addition of SV-IV into an in vitro coagulation system, containing pure fibrinogen, alpha-thrombin and AT-III, resulted in complex suppression of thrombin inhibition by AT III. No other steps of the blood clotting process (prothrombinase complex, factor XIII, fibrinogen concentration) were affected by SV-IV.
Asunto(s)
Antitrombina III/antagonistas & inhibidores , Coagulación Sanguínea/efectos de los fármacos , Proteínas de Secreción Prostática , Proteínas/farmacología , Animales , Cloruro de Calcio , Relación Dosis-Respuesta a Droga , Factor XIII/metabolismo , Fibrinógeno/metabolismo , Hemorragia/fisiopatología , Humanos , Técnicas In Vitro , Proteínas/aislamiento & purificación , Ratas , Proteínas de Plasma Seminal , Serpinas/sangre , Tromboplastina/metabolismoRESUMEN
In summary, the present study documents that platelet aggregation triggered by thrombin, ADP, collagen and PAF both in vivo and in vitro, was prevented by SV-IV in a dose-dependent manner. Only platelet aggregation by AA was not affected by the protein, thus suggesting a possible involvement of PLA2 inhibition in the molecular mechanism at the basis of SV-IV anti-thrombotic effect.
Asunto(s)
Antineoplásicos/farmacología , Agregación Plaquetaria/efectos de los fármacos , Proteínas de Secreción Prostática , Proteínas/farmacología , Animales , Colágeno/antagonistas & inhibidores , Colágeno/farmacología , Inyecciones Intravenosas , Masculino , Factor de Activación Plaquetaria/antagonistas & inhibidores , Factor de Activación Plaquetaria/farmacología , Inhibidores de Agregación Plaquetaria , Ratas , Ratas Endogámicas , Proteínas de Plasma Seminal , Trombina/antagonistas & inhibidores , Trombina/farmacologíaRESUMEN
The nonspecies specific immunosuppressive and anti-inflammatory properties of a major protein (SV-IV) secreted from the epithelium of rat seminal vesicles (SV) are described. To detect the immunosuppressive effect, peripheral blood lymphocytes (PBL) were pretreated for 2 hr at 37 degrees with SV-IV, and the protein was maintained in the incubation medium during the whole culture time. We obtained evidence that, during preincubation of PBL and SV-IV the protein was transformed by a transglutaminase (TGase) released from PBL into modified low and high molecular weight forms able to bind to PBL surfaces. It is suggested that T lymphocytes are the possible targets of the immunosuppressive effect. SV-IV seems to inhibit only the early phase of the proliferative response of T lymphocytes to mitogens without having any direct effect on the enzymatic system involved in DNA synthesis. Moreover, the protein SV-IV was also shown to possess an anti-inflammatory property due to a block of the arachidonic acid cascade at the level of the enzyme phospholipase A2 (PLA2). The physiological significance of the immunosuppressive and anti-inflammatory properties of SV-IV are discussed in relation to different aspects of the mammalian reproduction.
Asunto(s)
Antiinflamatorios no Esteroideos/farmacología , Inmunosupresores/farmacología , Proteínas/farmacología , Vesículas Seminales/metabolismo , Animales , Concanavalina A/farmacología , ADN/biosíntesis , Dinoprostona/metabolismo , Epitelio/metabolismo , Antígenos HLA-D/análisis , Humanos , Activación de Linfocitos/efectos de los fármacos , Prueba de Cultivo Mixto de Linfocitos , Masculino , Fosfolipasas A/antagonistas & inhibidores , Fosfolipasas A2 , Proteínas/metabolismo , Ratas , Ratas Endogámicas , Receptores de Interleucina-2/análisis , Uteroglobina/farmacologíaRESUMEN
The protein SV-IV, one of the major secretory proteins produced by the rat seminal vesicle epithelium, has been found to possess a marked ability to inhibit in vitro the phagocytic properties of activated peritoneal rat macrophages, by a mechanism that apparently involves phagocytes and target cells. Although SV-IV is a substrate for transglutaminase (TGase), an enzyme secreted by activated macrophages, TGase does not seem to play any significant role either in the binding of the protein to the cells participating in the phagocytic process or in the inhibition of macrophage phagocytosis by SV-IV. The significance of the findings in relation to the reproductive process and their possible clinical implications are discussed.
Asunto(s)
Tolerancia Inmunológica/fisiología , Macrófagos/fisiología , Fagocitosis/fisiología , Proteínas de Secreción Prostática , Proteínas/fisiología , Vesículas Seminales/fisiología , Animales , Masculino , Microscopía Electrónica , Unión Proteica , Ratas , Ratas Endogámicas , Saccharomyces cerevisiae/inmunología , Proteínas de Plasma SeminalRESUMEN
Microgram amounts of protein SV-IV, a major secretory protein produced by adult rat seminal vesicle epithelium, markedly decrease the mouse humoral immune response to cellular xenogeneic or allogeneic antigens (sheep red blood cells (SRBC) or mouse epididymal spermatozoa). The significant reduction in the total number of splenocytes and their main cell subsets in SRBC-immunized mice, the dramatic decrease in the number of Ia+ splenic T cells and the marked inhibition of splenocyte ability to respond in vitro to polyclonal mitogen stimuli suggest that the macrophage accessory cells are the primary target of the SV-IV immunosuppressive activity in vivo. Moreover, the infection of SV-IV-treated mice with Salmonella typhimurium produced an increased mortality of the experimental animals associated with a marked decrease of the phagocytic and intracellular killing activities of their peritoneal macrophages.
Asunto(s)
Inmunosupresores/farmacología , Proteínas de Secreción Prostática , Proteínas/farmacología , Animales , Formación de Anticuerpos , Inmunidad Celular/efectos de los fármacos , Activación de Linfocitos , Subgrupos Linfocitarios , Masculino , Ratones , Ratones Endogámicos BALB C , Ratones Endogámicos C57BL , Fagocitosis , Ratas , Salmonelosis Animal/inmunología , Proteínas de Plasma SeminalRESUMEN
Both alpha- and beta-endorphin were shown to incorporate radioactive polyamines during incubation in the presence of purified transglutaminase and Ca2+, spermine acting as the best acyl acceptor substrate. The endorphin labelling is dependent on the time of exposure to the enzyme and on the substrate concentration. In the absence of acyl acceptor polyamines, isotopically labelled beta-endorphin gives rise to high molecular weight radioactive polymer(s). Moreover, when different proteins acting as transglutaminase substrates are added, beta-endorphin produces heterologous structures. These data indicate that the glutamine-71 of the beta-lipotropin chain, contained in both alpha- and beta-endorphin, functions as acyl donor substrate for the enzyme and that at least one beta-endorphin lysyl residue can serve as acyl acceptor.
Asunto(s)
Endorfinas , Transglutaminasas/metabolismo , betaendorfina , Técnicas In Vitro , Especificidad por Sustrato , alfa-EndorfinaRESUMEN
The anti-inflammatory effect of one of the major proteins secreted by rat seminal vesicles (SVIV) and of its spermidine derivative (Spd2-SVIV) was evaluated by measuring polymorphonuclear leukocyte migration, protein release, platelet-activating factor (PAF) and prostaglandin E2 levels in the mouse air-pouch exudate following zymesan treatment. Both proteins were found to markedly reduce dose dependently PAF and prostaglandin E2 levels in the exudate as well as the other parameters. Concurrent injection of either arachidonic acid or PAF, directly into the pouch, significantly counteracted the anti-inflammatory effect of SVIV and of its polyaminated derivative. These results support the notion that the molecular mechanism of the anti-inflammatory activity of SVIV and Spd2-SVIV is linked to the inhibition of both phospholipase A2 and acetyl:lyso-PAF acetyltransferase.
Asunto(s)
Inflamación/patología , Proteínas de Secreción Prostática , Proteínas/metabolismo , Espermidina/química , Zimosan/antagonistas & inhibidores , Animales , Dinoprostona/metabolismo , Masculino , Ratones , Factor de Activación Plaquetaria/metabolismo , Proteínas/química , Ratas , Proteínas de Plasma Seminal , Zimosan/farmacologíaRESUMEN
The inhibitory effect of one of the major proteins secreted by the rat seminal vesicles (SV-IV) on platelet-activating factor (PAF)-induced biological activities was investigated in vivo. SV-IV was found to prevent dose dependently both hypotension and acute bronchospasm caused by PAF administration in guinea-pigs. In addition, SV-IV inhibited both PAF- and ethanol-induced gastric mucosal injury in a dose-dependent manner.
Asunto(s)
Antiulcerosos/farmacología , Presión Sanguínea/efectos de los fármacos , Broncoconstricción/efectos de los fármacos , Factor de Activación Plaquetaria/antagonistas & inhibidores , Proteínas de Secreción Prostática , Proteínas/farmacología , Animales , Relación Dosis-Respuesta a Droga , Etanol , Cobayas , Masculino , Factor de Activación Plaquetaria/farmacología , Ratas , Ratas Wistar , Proteínas de Plasma Seminal , Úlcera Gástrica/inducido químicamente , Úlcera Gástrica/prevención & controlRESUMEN
The aim of the study was to evaluate the effect of the protein Seminal Vesicle Protein No. 4 (SV-IV), a potent inhibitor of antithrombin III (antithrombin), on the coagulation of blood obtained from patients affected by hemophilia A. In the coagulating blood of these patients, the antithrombin/thrombin ratio was found to be markedly higher (about 44) than in normal individuals (about 4. 4). This high ratio was related to the low efficiency of thrombin-generating reactions induced by the factor VIII deficiency and to the high levels of free (not bound to serine proteases) antithrombin present in the hemophilic serum (antithrombin concentration was the same in normal and hemophilic plasma). The elevated concentration of free antithrombin in hemophiliacs was primarily a consequence of a reduced consumption caused by the scarce availability in the hemophilic serum of factors Xa and IIa, which are serine proteases possessing strong binding affinity for antithrombin. Addition of SV-IV to coagulating hemophilic blood reduced markedly the serum antithrombin and thrombin-antithrombin complexes, normalizing, as a consequence, the clotting time and other coagulation parameters. Similar results were obtained by using appropriate concentration of factor VIII.
Asunto(s)
Antitrombina III/antagonistas & inhibidores , Coagulación Sanguínea/efectos de los fármacos , Hemofilia A/sangre , Proteínas/farmacología , Proteínas de Secreción de la Vesícula Seminal , Inhibidores de Serina Proteinasa/metabolismo , Antitrombina III/análisis , Antitrombina III/metabolismo , Calcio/sangre , Factor VIII/metabolismo , Factor Xa/análisis , Humanos , Tiempo de Protrombina , Trombina/metabolismo , Tiempo de Coagulación de la Sangre TotalAsunto(s)
Biosíntesis de Proteínas/efectos de los fármacos , ARN Mensajero/metabolismo , Ribosomas/análisis , Erizos de Mar/metabolismo , Animales , Tampones (Química) , Isótopos de Carbono , Sistema Libre de Células , Centrifugación por Gradiente de Densidad , Electroforesis en Gel de Poliacrilamida , Femenino , Fertilización , Cinética , Magnesio/farmacología , Concentración Osmolar , Óvulo , Extensión de la Cadena Peptídica de Translación , Factores de Elongación de Péptidos , Potasio/farmacología , Conejos , Reticulocitos/metabolismo , Espectrofotometría Ultravioleta , Factores de Tiempo , TritioRESUMEN
Human papilloma virus infection is thought to play a role in laryngeal carcinogenesis; the variable association reported in literature may be due to wide range of HPV genotypes. We report the case of a 51-year-old man affected by laryngeal squamous cell carcinoma; analysis of DNA extracted by cancer cells by an innovative molecular virology assay (INNO-LiPA HPV Genotyping Extra) showed the presence of two high-risk HPV genotypes, HPV-73 and -82. Immunohistochemical examination confirmed positivity for both capsid protein and viral oncogenic protein E7. Such association has never been reported in literature so far, and a brief discussion on the importance of assessing HPV status in laryngeal cancer is provided.