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1.
Dysphagia ; 38(4): 1096-1105, 2023 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-36243794

RESUMEN

Patients with oral cancer have poor nutritional status before treatment. However, there have been no reports of the detailed evaluation of preoperative oral function in patients with oral squamous cell carcinoma (OSCC). Therefore, this study aimed to evaluate the preoperative oral function of patients with OSCC and examine the relationship with nutritional status. Oral function measurements (microorganisms, oral dryness, occlusal force, tongue pressure, masticatory function, Eating Assessment Tool, and Postoperative Oral Dysfunction Scale) and Mini Nutritional Assessment-Short Form (MNA-SF) data were collected from 51 patients with OSCC (men: 37, women: 14, mean age: 72.1 years) who visited the Shimane University Hospital, Department of Oral and Maxillofacial Surgery, from September 2019 to September 2021. The tongue was the most prevalent primary gingiva site [22 patients (43.1%)], and 36 patients (70.6%) had advanced cancer. Comparisons between nutritional status and each related factor revealed significant differences in the number of individuals in the household, cancer stage, presence of pulmonary disease, number of teeth, microorganisms (grade), and masticatory function (mg/dL) (p < 0.05). Multiple regression analysis using the total MNA-SF score as the dependent variable with adjustment for confounding factors showed significant association between oral dryness and tongue pressure (p < 0.05). No significant association was found for the Eating Assessment Tool or Postoperative Oral Dysfunction scale. Patients with OSCC may have decreased oral function because of the tumor at the time of diagnosis, which causes a decline in nutritional status. Preoperative interventions are necessary to improve nutrition based on the state of oral function.


Asunto(s)
Carcinoma de Células Escamosas , Desnutrición , Neoplasias de la Boca , Masculino , Humanos , Femenino , Anciano , Estudios Transversales , Lengua/fisiología , Neoplasias de la Boca/complicaciones , Neoplasias de la Boca/cirugía , Presión , Estado Nutricional , Evaluación Nutricional
2.
Am J Physiol Regul Integr Comp Physiol ; 311(1): R66-78, 2016 07 01.
Artículo en Inglés | MEDLINE | ID: mdl-27122370

RESUMEN

Most vertebrates, including cartilaginous fishes, maintain their plasma SO4 (2-) concentration ([SO4 (2-)]) within a narrow range of 0.2-1 mM. As seawater has a [SO4 (2-)] about 40 times higher than that of the plasma, SO4 (2-) excretion is the major role of kidneys in marine teleost fishes. It has been suggested that cartilaginous fishes also excrete excess SO4 (2-) via the kidney. However, little is known about the underlying mechanisms for SO4 (2-) transport in cartilaginous fish, largely due to the extraordinarily elaborate four-loop configuration of the nephron, which consists of at least 10 morphologically distinguishable segments. In the present study, we determined cDNA sequences from the kidney of holocephalan elephant fish (Callorhinchus milii) that encoded solute carrier family 26 member 1 (Slc26a1) and member 6 (Slc26a6), which are SO4 (2-) transporters that are expressed in mammalian and teleost kidneys. Elephant fish Slc26a1 (cmSlc26a1) and cmSlc26a6 mRNAs were coexpressed in the proximal II (PII) segment of the nephron, which comprises the second loop in the sinus zone. Functional analyses using Xenopus oocytes and the results of immunohistochemistry revealed that cmSlc26a1 is a basolaterally located electroneutral SO4 (2-) transporter, while cmSlc26a6 is an apically located, electrogenic Cl(-)/SO4 (2-) exchanger. In addition, we found that both cmSlc26a1 and cmSlc26a6 were abundantly expressed in the kidney of embryos; SO4 (2-) was concentrated in a bladder-like structure of elephant fish embryos. Our results demonstrated that the PII segment of the nephron contributes to the secretion of excess SO4 (2-) by the kidney of elephant fish. Possible mechanisms for SO4 (2-) secretion in the PII segment are discussed.


Asunto(s)
Pez Eléctrico/metabolismo , Túbulos Renales Proximales/metabolismo , Riñón/metabolismo , Proteínas de Transporte de Membrana/metabolismo , Sulfatos/metabolismo , Secuencia de Aminoácidos , Animales , ADN Complementario/genética , Embrión no Mamífero/metabolismo , Proteínas de Peces/metabolismo , Nefronas/metabolismo , Oocitos/metabolismo , Distribución Tisular , Xenopus
3.
Plant J ; 80(3): 437-48, 2014 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-25142187

RESUMEN

C-Glycosides are characterized by their C-C bonds in which the anomeric carbon of the sugar moieties is directly bound to the carbon atom of aglycon. C-Glycosides are remarkably stable, as their C-C bonds are resistant to glycosidase or acid hydrolysis. A variety of plant species are known to accumulate C-glycosylflavonoids; however, the genes encoding for enzymes that catalyze C-glycosylation of flavonoids have been identified only from Oryza sativa (rice) and Zea mays (maize), and have not been identified from dicot plants. In this study, we identified the C-glucosyltransferase gene from the dicot plant Fagopyrum esculentum M. (buckwheat). We purified two isozymes from buckwheat seedlings that catalyze C-glucosylation of 2-hydroxyflavanones, which are expressed specifically in the cotyledon during seed germination. Following purification we isolated the cDNA corresponding to each isozyme [FeCGTa (UGT708C1) and FeCGTb (UGT708C2)]. When expressed in Escherichia coli, both proteins demonstrated C-glucosylation activity towards 2-hydroxyflavanones, dihydrochalcone, trihydroxyacetophenones and other related compounds with chemical structures similar to 2',4',6'-trihydroxyacetophenone. Molecular phylogenetic analysis of plant glycosyltransferases shows that flavonoid C-glycosyltransferases form a different clade with other functionally analyzed plant glycosyltransferases.


Asunto(s)
Fagopyrum/enzimología , Flavonoides/metabolismo , Glucosiltransferasas/metabolismo , Secuencia de Bases , Clonación Molecular , Cotiledón/enzimología , Cotiledón/genética , ADN Complementario/genética , Fagopyrum/genética , Glucosiltransferasas/genética , Datos de Secuencia Molecular , Filogenia , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo , Plantones/enzimología , Plantones/genética , Análisis de Secuencia de ADN
4.
J Med Chem ; 57(15): 6781-94, 2014 Aug 14.
Artículo en Inglés | MEDLINE | ID: mdl-25057800

RESUMEN

A series of novel tetrahydropyridinecarboxamide TRPV1 antagonists were prepared and evaluated in an effort to optimize properties of previously described lead compounds from piperazinecarboxamide series. The compounds were evaluated for their ability to block capsaicin and acid-induced calcium influx in CHO cells expressing human TRPV1. The most potent of these TRPV1 antagonists were further characterized in pharmacokinetic, efficacy, and body temperature studies. On the basis of its pharmacokinetic, in vivo efficacy, safety, and toxicological properties, compound 37 was selected for further evaluation in human clinical trials.


Asunto(s)
Aminopiridinas/química , Analgésicos/química , Dolor/tratamiento farmacológico , Canales Catiónicos TRPV/antagonistas & inhibidores , Aminopiridinas/farmacocinética , Aminopiridinas/farmacología , Analgésicos/farmacocinética , Analgésicos/farmacología , Animales , Temperatura Corporal/efectos de los fármacos , Células CHO , Calcio/metabolismo , Capsaicina/farmacología , Cricetulus , Adyuvante de Freund , Ganglios Espinales/citología , Humanos , Concentración de Iones de Hidrógeno , Masculino , Dolor/etiología , Ratas Sprague-Dawley , Células Receptoras Sensoriales/efectos de los fármacos , Células Receptoras Sensoriales/fisiología , Estereoisomerismo , Relación Estructura-Actividad
5.
No To Hattatsu ; 45(1): 17-20, 2013 Jan.
Artículo en Japonés | MEDLINE | ID: mdl-23593740

RESUMEN

OBJECTIVE: Valproate sodium (VPA) treatment is known to reduce blood carnitine levels; however, some enteral nutrition formulas contain carnitine. The objective of this study was to verify the hypothesis that blood carnitine levels are lower after VPA treatment in patients on enteral nutrition than in those on normal diet. METHODS: Forty-five epilepsy patients under medical treatment in our hospital were classified according to their alimentation type into normal diet group (n = 31) and 14 on enteral nutrition group (n = 14). The differences in the blood free carnitine levels between the two groups were evaluated. RESULTS: Plasma free carnitine levels were below the normal value in 15 of 31 patients on normal diet and 13 of 14 patients on enteral nutrition. There was a significant reduction of the levels of carnitine in the enteral nutrition group (p < 0.001). CONCLUSIONS: Although normal diet contains sufficient amount of carnitine, most enteral nutrition formulas lack carnitine; and hence, blood carnitine levels in patients on enteral nutrition after VPA treatment is low. It is therefore suggested that carnitine supplemented diet is necessary for patients treated with VPA, especially for those who receive enteral nutrition.


Asunto(s)
Carnitina/sangre , Suplementos Dietéticos , Nutrición Enteral , Ácido Valproico/uso terapéutico , Adolescente , Adulto , Carnitina/deficiencia , Niño , Preescolar , Epilepsia/tratamiento farmacológico , Femenino , Humanos , Masculino , Persona de Mediana Edad , Ácido Valproico/efectos adversos , Adulto Joven
6.
Nihon Shokakibyo Gakkai Zasshi ; 107(4): 620-4, 2010 Apr.
Artículo en Japonés | MEDLINE | ID: mdl-20379096

RESUMEN

We report a rare case of internal hernia through an abnormal defect in the broad ligament of the uterus. A 49-year-old woman, without any previous surgery, was admitted because of vomiting and lower abdominal pain. Three days after admission a small amount of small intestinal gas was pointed out on her plain abdominal X-ray film. An enema examination by ileus tube revealed a pooling of gastrografin on the left side of the pelvic cavity, showing an obstruction of the ileum. Therefore, an emergency operation was performed, whereupon we found an abnormal defect in the left broad ligament of the uterus. This case describes an internal hernia through an abnormal defect in a female ileus patient without a history of surgery.


Asunto(s)
Ligamento Ancho/anomalías , Hernia/etiología , Femenino , Humanos , Ileus/etiología , Persona de Mediana Edad
7.
Jpn J Clin Oncol ; 40(6): 503-7, 2010 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-20106881

RESUMEN

OBJECTIVE: The objective of this study was to evaluate the benefits of combination therapy consisting of recombinant human interleukin-2 and sorafenib for survival efficacy and the suppression of metastasis in murine renal cell carcinoma models. METHODS: Lung-metastasized renal cell carcinoma mice were treated with various combinations of recombinant human interleukin-2 and sorafenib. Tumor growth was observed using a bioluminescence imaging system. Next, the nephrectomized renal cell carcinoma mice were administered various combinations of recombinant human interleukin-2 and sorafenib, followed by a lung resection in order to examine lung metastasis by bioluminescence imaging. RESULTS: The increased life-span ratio in mice receiving combination therapy was 1.45, whereas that in mice treated with sorafenib or recombinant human interleukin-2 alone therapy was 1.28 and 1.07, respectively. The concomitant administration of recombinant human interleukin-2 and sorafenib had a metastasis-inhibitory effect, whereas the other treatments failed. CONCLUSIONS: These findings indicate that combination therapy of recombinant human interleukin-2 and sorafenib may offer better outcomes than either monotherapy with recombinant human interleukin-2 or sorafenib with respect to survival benefits and the prevention of pulmonary metastasis in renal cell carcinoma patients.


Asunto(s)
Protocolos de Quimioterapia Combinada Antineoplásica/uso terapéutico , Bencenosulfonatos/administración & dosificación , Carcinoma de Células Renales/secundario , Interleucina-2/administración & dosificación , Neoplasias Renales/patología , Neoplasias Pulmonares/prevención & control , Neoplasias Pulmonares/secundario , Piridinas/administración & dosificación , Animales , Carcinoma de Células Renales/tratamiento farmacológico , Carcinoma de Células Renales/mortalidad , Carcinoma de Células Renales/cirugía , Línea Celular Tumoral , Femenino , Neoplasias Renales/tratamiento farmacológico , Neoplasias Renales/mortalidad , Neoplasias Renales/cirugía , Neoplasias Pulmonares/mortalidad , Ratones , Ratones Endogámicos BALB C , Nefrectomía , Niacinamida/análogos & derivados , Compuestos de Fenilurea , Proteínas Recombinantes/administración & dosificación , Sorafenib , Tasa de Supervivencia
8.
Cardiovasc Intervent Radiol ; 30(3): 512-4, 2007.
Artículo en Inglés | MEDLINE | ID: mdl-17171304

RESUMEN

We report a case of cerebral lipiodol embolism following transcatheter chemoembolization (TACE) for hepatocellular carcinoma. A 70-year-old woman with a large unresectable hepatocellular carcinoma underwent TACE. Her level of consciousness deteriorated after the procedure, and magnetic resonance imaging and non-contrast computed tomography revealed a cerebral lipiodol embolism. Despite intensive care, the patient died 2 weeks later. The complication might have been due to systemic-pulmonary shunts caused by previous surgeries and/or direct invasion of the recurrent tumor.


Asunto(s)
Carcinoma Hepatocelular/terapia , Quimioembolización Terapéutica/efectos adversos , Medios de Contraste/efectos adversos , Embolia Intracraneal/inducido químicamente , Aceite Yodado/efectos adversos , Neoplasias Hepáticas/terapia , Recurrencia Local de Neoplasia/terapia , Anciano , Encéfalo/efectos de los fármacos , Encéfalo/patología , Medios de Contraste/administración & dosificación , Diagnóstico por Imagen , Epirrubicina/administración & dosificación , Resultado Fatal , Femenino , Humanos , Embolia Intracraneal/diagnóstico
9.
Int J Mol Med ; 15(6): 1033-9, 2005 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-15870910

RESUMEN

Melanin-concentrating hormone (MCH) is known to be an important regulator for feeding and energy balance. MCH was recently reported to stimulate water intake independent of food intake. The purpose of the present study is to examine the dipsogenic response of MCH with special emphasis on sweetened beverages, the preference for which is well documented in diabetic animals. Our results showed that intracerebroventricular injection of MCH acutely increased food as well as water intake. Human (h)MCH and salmon (s)MCH increased water intake independent of food intake, which was not suppressed by angiotensin antagonists. hMCH and sMCH significantly increased both sucrose solution and food intake; on the other hand, agouti-related protein (AgRP) stimulated food but not sucrose intake when provided simultaneously. MCH-treated rats significantly increased the ingestion of sucrose and glucose solution, but not of saccharin, indicating that MCH-induced dipsogenic response is more related to caloric content than sweet taste per se. Significant correlation was observed between the sucrose intake and the mRNA expression of MCH and MCHR1 in normal rats. These results indicate that MCH may be an important regulator of sugar intake in normal as well as in obese diabetic animals.


Asunto(s)
Conducta de Ingestión de Líquido/efectos de los fármacos , Hormonas Hipotalámicas/administración & dosificación , Hormonas Hipotalámicas/farmacología , Melaninas/administración & dosificación , Melaninas/farmacología , Hormonas Hipofisarias/administración & dosificación , Hormonas Hipofisarias/farmacología , Sacarosa/metabolismo , Proteína Relacionada con Agouti , Angiotensina II/farmacología , Angiotensinas/antagonistas & inhibidores , Animales , Ritmo Circadiano , Relación Dosis-Respuesta a Droga , Conducta Alimentaria/efectos de los fármacos , Humanos , Hormonas Hipotalámicas/genética , Hipotálamo/química , Inyecciones Intraventriculares , Masculino , Melaninas/genética , Fragmentos de Péptidos/farmacología , Hormonas Hipofisarias/genética , ARN Mensajero/metabolismo , Ratas , Ratas Sprague-Dawley , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Salmón , Cloruro de Sodio/metabolismo , Factores de Tiempo
10.
J Biol Chem ; 280(21): 20204-15, 2005 May 27.
Artículo en Inglés | MEDLINE | ID: mdl-15778505

RESUMEN

Trappins are found in human, bovine, hippopotamus, and members of the pig family, but not in rat and mouse. To clarify the evolution of the trappin genes and the functional significance of their products, we isolated the trappin gene in guinea pig, a species belonging to a rodent family distinct from rat and mouse. Guinea pig trappin was confirmed to encode the same domain structure as trappin, consisting of a signal sequence, an extra large transglutaminase substrate domain, and a whey acidic protein motif. Northern blot analysis and in situ hybridization histochemistry as well as immunohistochemistry demonstrated that guinea pig trappin is expressed solely in the secretory epithelium of the seminal vesicle and that its expression is androgen-dependent. We confirmed that guinea pig trappin is cross-linked by prostate transglutaminase and that the whey acidic protein motif derived from guinea pig trappin has an inhibitory activity against leukocyte elastase. Genome sequence analysis showed that guinea pig trappin belongs to the family of REST (rapidly evolving seminal vesicle transcribed) genes.


Asunto(s)
Evolución Molecular , Regulación de la Expresión Génica , Proteínas/análisis , Proteínas/genética , Transglutaminasas/metabolismo , Secuencia de Aminoácidos , Andrógenos/farmacología , Animales , Sitios de Unión , Western Blotting , Calcio/farmacología , Bovinos , Reactivos de Enlaces Cruzados , ADN Complementario/química , Regulación de la Expresión Génica/efectos de los fármacos , Cobayas , Humanos , Inmunohistoquímica , Elastasa de Leucocito/antagonistas & inhibidores , Masculino , Ratones , Proteínas de la Leche/química , Proteínas de la Leche/metabolismo , Datos de Secuencia Molecular , Próstata/enzimología , Proteínas Inhibidoras de Proteinasas Secretoras , Proteínas/química , Ratas , Vesículas Seminales/química , Alineación de Secuencia , Porcinos , Distribución Tisular
11.
Plant Cell Rep ; 24(1): 52-8, 2005 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-15692822

RESUMEN

The tobacco retrotransposon Tto1 is one of the few known active retrotransposons, and its transposition in tobacco, rice and Arabidopsis has been reported to be activated by tissue culture. We introduced Tto1 into a diploid potato by means of Agrobacterium-mediated transformation and obtained two transformed plants carrying Tto1. We then induced plant regeneration via callus formation from leaf explants of Tto1-transformed plants and determined the copy number of Tto1 in the regenerants. A drastic increase in the number of Tto1 copies was not observed. Transcripts of Tto1 were detected in the leaf but not in the callus, suggesting that the transposition of Tto1 may not be activated by tissue culture in potato. The results indicated that the potato is a recalcitrant plant with respect to Tto1 transposition and that the behavior of Tto1 can differ depending on the host plant.


Asunto(s)
Nicotiana/genética , Retroelementos/genética , Solanum tuberosum/genética , Región de Flanqueo 3' , Región de Flanqueo 5' , Secuencia de Bases , Diploidia , Ingeniería Genética/métodos , Plantas Modificadas Genéticamente
12.
Biol Reprod ; 71(5): 1583-90, 2004 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-15240421

RESUMEN

We determined the cDNA and gene structures of guinea pig caltrin II, a unique member of the calcium transporter inhibitors containing a whey acidic protein (WAP) motif, and we established that it is a secretory protein with a potential 21-amino acid signal peptide in its N-terminus. Northern blot analysis and in situ hybridization histochemistry indicated that the expression of caltrin II is restricted to luminal epithelial cells in the seminal vesicles. Its message levels markedly decreased either after castration (and were restored by simultaneous administration of testosterone) or after treatment of the animals with estradiol, suggesting that the expression of caltrin II is androgen-dependent. Recombinant caltrin II had an elastase-inhibitor activity. Comparison of sequence between the caltrin II and related genes and their molecular evolutionary analyses revealed that caltrin II and seminal vesicle secretory proteins (SVPs) appear to be evolved from a common ancestor gene that is made by the fusion of semenogelin and trappin genes. Caltrin II and SVPs lost the transglutaminase substrate domain and the WAP motif, respectively, within a single exon, resulting in the exertion of different functions.


Asunto(s)
Andrógenos/fisiología , Evolución Molecular , Cobayas/genética , Cobayas/metabolismo , Proteínas de la Leche/genética , Proteínas de Secreción de la Vesícula Seminal/genética , Proteínas de Secreción de la Vesícula Seminal/metabolismo , Secuencias de Aminoácidos , Secuencia de Aminoácidos , Animales , Clonación Molecular , ADN Complementario , Células Epiteliales/metabolismo , Masculino , Datos de Secuencia Molecular , Elastasa Pancreática/antagonistas & inhibidores , Isoformas de Proteínas/genética , Isoformas de Proteínas/metabolismo , Isoformas de Proteínas/farmacología , ARN Mensajero/metabolismo , Proteínas Recombinantes/farmacología , Proteínas de Secreción de la Vesícula Seminal/farmacología , Vesículas Seminales/metabolismo
13.
Eur J Biochem ; 269(24): 6152-61, 2002 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-12473111

RESUMEN

An RBCC (RING finger, B-box, and coiled-coil) protein was identified that belongs to the superfamily of zinc-binding proteins and is specifically expressed in the gill of eel, Anguilla japonica. Euryhaline fishes such as eels can migrate between freshwater and seawater, which is considered to be accomplished by efficient remodeling of the architecture and function of the gill, a major osmoregulatory organ. To identify molecules involved in such adaptive changes, we performed differential display using mRNA preparations from freshwater and seawater eel gills and obtained an RBCC clone among several differentially expressed clones. The clone encoded a protein of 514 amino acid residues with structural features characteristic of the RBCC protein; we therefore named it eRBCC (e for eel). eRBCC mRNA was specifically expressed in the gills with a greater extent in the gills of freshwater eels. Immunohistochemistry revealed that the expression of eRBCC is confined to particular epithelial cells of the gills including freshwater-specific lamellar chloride cells. The RING finger of eRBCC was found to have a ubiquitin ligase activity, suggesting an important regulatory role of eRBCC in the remodeling of branchial cells.


Asunto(s)
Anguilas/genética , Ligasas/biosíntesis , Ligasas/química , Dedos de Zinc , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Northern Blotting , Western Blotting , Células COS , Clonación Molecular , ADN Complementario/metabolismo , Anguilas/metabolismo , Células Epiteliales , Perfilación de la Expresión Génica , Branquias/metabolismo , Inmunohistoquímica , Ligasas/metabolismo , Microscopía Fluorescente , Datos de Secuencia Molecular , Unión Proteica , Estructura Terciaria de Proteína , ARN Mensajero/metabolismo , Ribonucleasas/metabolismo , Homología de Secuencia de Aminoácido , Factores de Tiempo , Distribución Tisular , Ubiquitina/metabolismo
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