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1.
Aliment Pharmacol Ther ; 24(9): 1333-40, 2006 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-17059514

RESUMO

BACKGROUND: Although thiopurines have a proven role in maintenance therapy for Crohn's disease, an alternative therapy is needed for patients intolerant or resistant to thiopurines. AIM: To evaluate the effectiveness of home enteral nutrition as a maintenance therapy regimen in which half of the daily calorie requirement is provided by an elemental diet and the remaining half by a free diet. We refer to this home enteral nutrition therapy as 'half elemental diet'. METHODS: Between 2002 and 2005, 51 patients in remission from two hospitals were randomly assigned to a half elemental diet group (n = 26) or a free diet group (n = 25). The primary outcome measure of this study was the occurrence of relapse over the 2-year period. RESULTS: The relapse rate in the half elemental diet group was significantly lower [34.6% vs. 64.0%; multivariate hazard ratio 0.40 (95% CI: 0.16-0.98)] than that in the free diet group after a mean follow-up of 11.9 months. Compliance was similar in the two groups. No adverse event occurred in any of the patients throughout the study. CONCLUSION: This randomized-controlled trial shows the effectiveness of an half elemental diet, which is a promising maintenance therapy for Crohn's disease patients.


Assuntos
Doença de Crohn/dietoterapia , Alimentos Formulados , Adulto , Nutrição Enteral/métodos , Feminino , Seguimentos , Humanos , Masculino , Nutrição Parenteral/métodos , Recidiva , Resultado do Tratamento
2.
J Endocrinol Invest ; 29(10): 924-7, 2006 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-17185903

RESUMO

Subacute thyroiditis (SAT) is an extremely rare cause of thyrotoxicosis in pregnant women. Untreated, thyrotoxicosis may result in complications, such as prematurity and congenital malformations in the fetus. We report two cases of first trimester subacute thyroiditis, one mild and one severe. The severe case, as demonstrated by laboratory and ultrasound findings, was successfully treated with prednisolone. In this case, it was thought that the benefits of pharmacological therapy outweighed the risk of potential teratogenesis by the medication. In contrast, the milder case was managed conservatively and resolved without treatment. These cases illustrate how laboratory and ultrasound findings can be used to determine whether treatment should be initiated and, once begun, if medication levels need to be adjusted. In both cases, the pregnancies resulted in healthy full-term infants.


Assuntos
Complicações na Gravidez/diagnóstico , Complicações na Gravidez/tratamento farmacológico , Tireoidite Subaguda/diagnóstico , Tireoidite Subaguda/tratamento farmacológico , Adulto , Feminino , Glucocorticoides/uso terapêutico , Humanos , Prednisolona/uso terapêutico , Gravidez , Complicações na Gravidez/diagnóstico por imagem , Primeiro Trimestre da Gravidez , Índice de Gravidade de Doença , Tireoidite Subaguda/diagnóstico por imagem , Resultado do Tratamento , Ultrassonografia
3.
Int J Cosmet Sci ; 28(4): 299-309, 2006 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-18489270

RESUMO

The causative substances for axillary osmidrosis, which are often found in apocrine sweat, are the decomposed/denatured products of short-chain fatty acid and other biological metabolite compounds produced by axillary-resident bacteria. Conventional underarm deodorants suppress the process of odour production mostly by the following mechanism: (1) suppression of perspiration, (2) reduction in numbers of resident bacteria, (3) deodorization and (4) masking. The most important and effective method to reduce odour is to suppress the growth of resident bacteria with antimicrobials, which have several drawbacks, especially in their safety aspect. To solve these problems, we focused on Ag-zeolite (silver-exchanged zeolite) that hold stable Ag, an inorganic bactericidal agent, in its structure, and therefore, poses less risk in safety. Its bactericidal effect on skin-resident bacteria was found to be excellent and comparable with that of triclosan, a most frequently used organic antimicrobial in this product category. The dose-response study of Ag-zeolite powder spray (0-40 w/w%) using 39 volunteers revealed that 5-40 w/w% Ag-zeolite could show a sufficient antimicrobial effect against skin-resident bacteria. The comparison study using 0.2 w/w% triclosan as the control and 10 w/w% Ag-zeolite indicated that: (1) one application of the powder spray containing 10 w/w% Ag-zeolite could show a sufficient antimicrobial effect against the resident bacteria and its effect continued for 24 h, (2) a powder spray containing 0.2 w/w% triclosan was unable to show a sufficient antimicrobial effect, and (3) no adverse event was observed. These studies show that Ag-zeolite has a superior antimicrobial ability that is rarely found in conventional antimicrobials used in deodorant products and a strong antiaxillary odour deodorant ability because of its long-lasting effect. During clinical study, patch tests with humans and other clinical studies of this product showed no adverse events related to the treatment with the Ag-zeolite product.

4.
Endocrinology ; 124(2): 870-7, 1989 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-2463906

RESUMO

Somatomedin/insulin-like growth factor (IGF)-like polypeptides (designated SMP) were purified from the serum-free conditioned medium of cultured rat epithelial-like cells, 18,54-SF. A monoclonal antibody (MAb) was produced against partially purified SMP. The antibody was immunoglobulin G1 relatively specific for multiplication-stimulating activity III-2 (rat IGF-II), with a Kd value of 5.6 X 10(-9) M. The antibody showed 100% cross-reactivity with human IGF-II and 10% cross-reactivity with human IGF-I, but did not cross-react with insulin. For purification of SMP, therefore, immunoaffinity chromatography on Sepharose coupled with the MAb was used besides a procedure including ion exchange chromatography, gel filtration, and reverse phase HPLC. The purified SMP (at least five polypeptides) each gave a single peak on reverse phase HPLC and appeared as a single band with an apparent mol wt of 5000-8000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The major components of SMP (designated HP1-SMP and HP3-SMP), which were purified about 100-fold from conditioned medium, stimulated DNA synthesis in human fibroblasts in culture and sulfation in chick embryonic cartilage in culture. These polypeptides showed almost the same cross-reactivity as multiplication-stimulating activity III-2 on RIA with the MAb. The partial amino acid sequences of HP1- and HP3-SMP were determined, and these polypeptides were identified with rat IGF-II.


Assuntos
Anticorpos Monoclonais , Epitopos/análise , Fator de Crescimento Insulin-Like II/metabolismo , Somatomedinas/metabolismo , Animais , Anticorpos Monoclonais/isolamento & purificação , Linhagem Celular , Cromatografia de Afinidade , Cromatografia em Gel , Cromatografia por Troca Iônica , Epitélio , Fator de Crescimento Insulin-Like II/imunologia , Fator de Crescimento Insulin-Like II/isolamento & purificação , Radioimunoensaio , Ratos
5.
J Histochem Cytochem ; 47(4): 525-32, 1999 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-10082754

RESUMO

We have characterized the subcellular distribution of S100A3, a cysteine-rich calcium binding protein, in human scalp hair shaft. This was accomplished using rapid-freezing immunocytochemistry, a technique that combines rapid-freezing, freeze-substitution fixation without chemical fixatives, and subsequent electron microscopic detection of immunocytochemical labeling. This technique preserves both the antigenicity and the ultrastructural integrity of fully keratinized tissues, which are highly unmanageable when prepared for immunoelectron microscopy. In the hair shaft, S100A3 was primarily identified in the endocuticle and was also present in the intermacrofibrillar matrix surrounding macrofibril bundles of intermediate filament keratins in cortex cells. Double immunolabeling of S100A3 and hair keratins revealed the in situ spatial relationship between them. In the endocuticle, S100A3 was present on the inner portion of the endocuticle adjacent to the cell membrane complex, whereas hair keratins were present on the outer portion. These results provide the first ultrastructural evidence that an S100 protein is localized in specific subcompartments in human hair cells. (J Histochem Cytochem 47:525-532, 1999)


Assuntos
Proteínas de Ligação ao Cálcio/metabolismo , Cabelo/metabolismo , Proteínas S100 , Adolescente , Western Blotting , Criança , Feminino , Técnica Indireta de Fluorescência para Anticorpo , Substituição ao Congelamento , Folículo Piloso/metabolismo , Humanos , Queratinas/metabolismo , Microscopia Imunoeletrônica , Manejo de Espécimes
6.
J Endocrinol ; 132(2): 305-10, 1992 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-1311750

RESUMO

Using a polyclonal antibody against a synthetic fusion protein corresponding to 167 amino acids of the N-terminal region of the human renal mineralocorticoid receptor (MR), an immunohistochemical study was performed to investigate the intraglandular and intracellular localization of the receptor in human kidney, salivary gland, pancreas, mammary gland and sweat gland both at the light and electron microscopic levels. In the kidney, immunoreactivity was observed in distal convoluted tubules, branches of Henle's loop, and collecting tubules in the renal cortex, and papillary and Henle's loops' ducts in the renal medulla. No significant differences in the distribution of immunoreactivity were observed using different fixatives (10% neutral formalin, 100% methanol, 4% paraformaldehyde, PLP (periodate-lysine-2% paraformaldehyde) solution and Zamboni solution) and processing methods (paraffin embedding and frozen sectioning). Immunoreactivity in the kidney was observed in both the cytoplasm and nucleus, with cytoplasmic staining predominant, regardless of the methods of tissue preparation. Immunoelectron microscopy, employing a pre-embedding method, demonstrated the presence of immunoreaction precipitates in nuclei, endoplasmic reticulum, perinuclear cisternae, free cytoplasm and cell membranes. In nuclei, immunoreactivity was observed in euchromatin but not in heterochromatin, which is consistent with an association of MR with specific DNA regulatory elements located in transcriptionally active euchromatin. In other organs, MR was expressed in cells of the excretory ductal system where mineralocorticoids are known to play a role in electrolyte homeostasis.


Assuntos
Rim/química , Mineralocorticoides/análise , Receptores de Esteroides/análise , Animais , Mama/química , Membrana Celular/química , Núcleo Celular/química , Citoplasma/química , Humanos , Imuno-Histoquímica , Microscopia Imunoeletrônica , Pâncreas/química , Coelhos , Receptores de Mineralocorticoides , Glândulas Salivares/química , Glândulas Sudoríparas/química
7.
J Exp Psychol Gen ; 118(4): 323-37, 1989 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-2531197

RESUMO

The process of encoding new information involves the imposition of preexisting interpretive categories on newly encountered stimuli, even if the categories do not match perfectly those stimuli. We hypothesized that such encoding of stimuli as supportive of preexisting encoding dispositions may become a source of a perceiver's subjective experiences that support these dispositions. Through this nonconsciously operating mechanism, encoding rules may gradually develop in a self-perpetuating manner, even in the absence of any objectively supportive evidence. Results demonstrated this self-perpetuating process in three studies involving different stimulus materials and experimental tasks (matrix-scanning paradigm and two "intuitive judgment" tasks). The self-perpetuating development of encoding biases is discussed as one of the elementary mechanisms involved in the development of interpretive categories and other individually differentiated cognitive dispositions.


Assuntos
Atenção , Formação de Conceito , Memória , Rememoração Mental , Adulto , Encéfalo/anatomia & histologia , Simulação por Computador , Aprendizagem por Discriminação/fisiologia , Feminino , Humanos , Inteligência/fisiologia , Masculino , Reconhecimento Visual de Modelos/fisiologia
8.
J Cancer Res Clin Oncol ; 121(4): 211-8, 1995.
Artigo em Inglês | MEDLINE | ID: mdl-7751319

RESUMO

Aplysiatoxin and debromoaplysiatoxin, a debrominated form of aplysiatoxin, have both been shown to be potent tumor promoters in a two-stage carcinogenesis experiment on mouse skin. However, debromoaplysiatoxin did not behave like aplysiatoxin in most of the biological assay systems using cultured cells. The discrepancy was supposed to be due to a factor in the bovine serum used for culture, a similar factor not being present in sera of eight other animal species examined. The factor was purified to homogeneity from bovine serum by ammonium sulfate fractionation and chromatographies on DEAE-cellulose, Sephadex G-150, hydroxyapatite, and a reversed-phase HPLC column. The factor was a 40-kDa protein, and partial amino-acid sequencing of its tryptic peptides indicated that the factor is alpha 1-acid glycoprotein. Both the purified factor and the commercially available bovine alpha 1-acid glycoprotein abolished in vitro the activation of protein kinase C by debromoaplysiatoxin but not that by aplysiatoxin. Debromoaplysiatoxin induced differentiation of HL-60 cells into macrophages at a comparable concentration to aplysiatoxin, when serum-free medium was used. These results suggest that alpha 1-acid glycoprotein, which interacts specifically with debromoaplysiatoxin, contained in bovine serum must have masked the in vitro properties of the tumor promoter in the biological assay systems.


Assuntos
Anticarcinógenos/isolamento & purificação , Carcinógenos/toxicidade , Toxinas de Lyngbya/antagonistas & inibidores , Toxinas de Lyngbya/toxicidade , Orosomucoide/farmacologia , Células 3T3/efeitos dos fármacos , Células 3T3/metabolismo , Sequência de Aminoácidos , Animais , Anticarcinógenos/farmacologia , Bovinos , Interações Medicamentosas , Ativação Enzimática , Fator de Crescimento Epidérmico/metabolismo , Humanos , Cinética , Camundongos , Camundongos Endogâmicos BALB C , Dados de Sequência Molecular , Orosomucoide/isolamento & purificação , Orosomucoide/fisiologia , Dibutirato de 12,13-Forbol/metabolismo , Proteína Quinase C/metabolismo , Coelhos , Ratos , Sensibilidade e Especificidade , Homologia de Sequência de Aminoácidos , Trítio
9.
J Biochem ; 88(3): 797-806, 1980 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-6252206

RESUMO

1. DNase I from porcine pancreas, if Mg2+ was present, hydrolyzed both sDNA and dDNA, whether free or bound to Sepharose. The hydrolysis rates were maximum at pH 7.5 with the bound DNAs and at pH 7.0 with the free DNAs negligible at pH 4.0 and pH 10.5 with the free and bound DNAs. The hydrolysis was completely inhibited by 50 mM sodium citrate. 2. With 50 mM citrate buffer (Ph 4.0), DNase I was effectively adsorbed on the DNA-Sepharoses in the absence of 5 mM Mg2+. The adsorbed enzyme was effectively eluated by the buffer containing 1 M KCl (eluate). The amounts of the eluated enzyme were approximately 1.5 X 10(5) units/mg DNA with sDNA-Sepharose and approximately 3.0 X 10(5) units/mg DNA with dDNA-Sepharose. This simple adsorption-elution of the pancreas extract resulted in approximately 300-fold purification of DNase I with a yield of 95%. In the elute, the ratios in activity of trypsin, chymotrypsin and RNase to DNase I were 1/(4.0 X 10(5)), 1/(5.3 X 10(3)), and 1/(4.1 X 10(2)) as low as in the extract, respectively. In addition, the eluate was not contaminated by kallikrein or carboxypeptidases A and B. 3. Upon repeating the adsorption-elution described above, the adsorbing capacities of DNA-Sepharoses gradually deteriorated with the whole pancreas extract, but not with the precipitate of the extract formed on 60% ammonium sulfate saturation, which contained 90% of the DNase I. With the precipitate, one dDNA-Sepharose solumn was repeatedly usable at least 20-times without deterioration. The DNase I preparation thus obtained was homogeneous on SDS-polyacrylamide gel electrophoresis. 4. Conceivably, the above-mentioned adsorption of DNase I on DNA-Sepharoses was mainly due to the steric and electrostatic affinity of a relatively large moiety of the DNA molecule to the substrate-binding site, but not to the catalytic site, of the enzyme.


Assuntos
Desoxirribonucleases/isolamento & purificação , Endonucleases/isolamento & purificação , Pâncreas/enzimologia , Animais , Cromatografia de Afinidade/métodos , Citratos , DNA , DNA de Cadeia Simples , Desoxirribonuclease I , Concentração de Íons de Hidrogênio , Concentração Osmolar , Sefarose , Suínos
10.
J Biochem ; 86(5): 1537-48, 1979 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-316432

RESUMO

1. All the porcine pancreas enzymes tested, regardless of their pI's were adsorbed on Amberlite CG-50 (a weakly acidic cation exchange resin) at pH 4, where the ion-exchange group (carboxyl group) is not dissociated. The adsorption is hardly influenced by ionic strength. 2. At pH 4, the adsorbed enzymes were partially eluted by organic solvents such as 50% propanol. 3. The adsorbed enzymes were effectively eluted by increasing the pH from 4 to 6. Trypsin (pI 10.5) was eluted before carboxypeptidase A (pI 4.5 AND 5.3) WITH 0.5 M acetate buffer, whereas the former enzyme was eluted after the latter enzyme with 0.2 M 3,3-dimethyl glutarate buffer. However, with either buffer, the elution order of enzymes was not always the same as the order of the pI's. 4. By a single Amberlite CG-50 column chromatography of porcine pancreas extracts, kallikrein, carboxypeptidase B, deoxyribonuclease, carboxypeptidase A, and trypsin were purified 100-fold, 16-fmately 13%. The purification procedures included treatment with protamine, ammonium sulfate fractionation, treatment with acid, DE-32 cellulose column chromatography, gel filtration on Sephadex G-100, preparative polyacrylamide gel electrophoresis, and affinity chromatography on 5' AMP-Sepharose 4B. The last procedure, affinity chromatography on 5' AMP-Sepharose 4B, was useful for the removal of other dehydrogenases. The enzyme which was homogeneous, as shown by polyacrylamide gel electrophoresis, had a molecular weight of about 92,000. The optimum pH was at 10.0 and isoelectric point at 5.2. The enzyme accepted both L-fucose and D-arabinose as substrate, but was specific for NAD+ as coenzyme. Km values were 0.15 mM, 1.4 mM, and 0.07 mM for L-fucose, D-arabinose, and NAD+, respectively. A single enzyme catalyzed the oxidation of L-fucose and D-arabinose, which had the same configurations of hydroxyl groups from C-2 to C-4. The reaction products obtained with L-fucose as substrate were L-fucono-lactone and L-fuconic acid. The L-fucono-lactone was an immediate product of oxidation and was hydrolyzed to L-fuconic acid spontaneously. This reaction was irreversible. Therefore, it is likely that L-fucose dehydrogenase is involved in the initial step of the catabolic pathway of L-fucose in rabbit liver.


Assuntos
Amilases/isolamento & purificação , Carboxipeptidases/isolamento & purificação , Desoxirribonucleases/isolamento & purificação , Calicreínas/isolamento & purificação , Lipase/isolamento & purificação , Pâncreas/enzimologia , Tripsina/isolamento & purificação , alfa-Amilases/isolamento & purificação , Animais , Cromatografia por Troca Iônica/métodos , Solventes , Suínos
11.
J Biochem ; 91(1): 211-7, 1982 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-7200090

RESUMO

Glycerol dehydrogenase [EC 1.1.1.6] (pI 5.9) from Geotrichum candidium is effectively adsorbed in the presence of 20 mM acute buffer (pH 6.0) on either octyl-Sepharose or 10-carboxydecyl-Sepharose, among ten different kinds of n-alkyl-Sepharose derivatives tested, some of which have an amino or a carboxyl group as a terminal residue. The enzyme adsorbed on 10-carboxydecyl-Sepharose is 95% eluted with 0.26 M NaCl. n-Propanol (10% and 15%, but not 5%), and various nucleotides such as NAD+, NADH, NADP+, NADPH, AMP, ADP, and ATP (1 mM) are also effective for elution. The elution with nucleotides is facilitated by 5% n-propanol. On the other hand, the enzyme adsorbed on octyl-Sepharose is not eluted under the conditions described above. These results suggest that the adsorption-elution of the enzyme on 10-carboxydecyl-Sepharose is due to a combination of hydrophobic interaction and electrostatic repulsion between a specific locus of the enzyme surface and the 10-carboxydecyl residue. Experimental conditions are described under which the enzyme can be purified 266-fold with a yield of 79% by a single chromatography of the cell extract on a 10-carboxydecyl-Sepharose column.


Assuntos
Cromatografia de Afinidade/métodos , Geotrichum/enzimologia , Fungos Mitospóricos/enzimologia , Polissacarídeos , Sefarose , Desidrogenase do Álcool de Açúcar/isolamento & purificação , Adsorção , NAD , Propranolol , Sefarose/análogos & derivados
12.
J Biochem ; 91(5): 1555-61, 1982 May.
Artigo em Inglês | MEDLINE | ID: mdl-6807971

RESUMO

Glucose oxidase from Aspergillus niger, hyaluronidase from Streptomyces hyalurolyticus, and cholesterol oxidase and cholesterol esterase from Pseudomonas fluorescens were effectively adsorbed on an Amberlite CG-50 column, when the cell-free cultured medium or the cultured medium with cell extract and without cell debris was applied without desalting but at pH less than or equal to 4.5. At the acidic pH, all the ion-exchange groups (-COOH) exist in the protonated form; the adsorption is not due to electrostatic attraction, but to hydrophobic interaction. The enzymes thus adsorbed were effectively eluted by increasing pH, at which the ion-exchange groups became dissociated. This type of adsorption-elution is called hydrophobic-ionic chromatography. By a single run of chromatography, glucose oxidase, hyaluronidase, cholesterol oxidase, and cholesterol esterase were purified 30-fold, 12-fold, 45-fold, and 20-fold with yields of 82%, 83%, 80%, and 90%, respectively. This indicates that hydrophobic-ionic chromatography on an Amberlite CG-50 column is effective for the purification of various enzymes, provided that they are stable at the acidic pH.


Assuntos
Bactérias/enzimologia , Proteínas de Bactérias/isolamento & purificação , Cromatografia/métodos , Aspergillus niger/enzimologia , Fenômenos Químicos , Química , Colesterol Oxidase/isolamento & purificação , Glucose Oxidase/isolamento & purificação , Hialuronoglucosaminidase/isolamento & purificação , Concentração de Íons de Hidrogênio , Pseudomonas fluorescens/enzimologia , Esterol Esterase/isolamento & purificação , Streptomyces/enzimologia
13.
J Biochem ; 91(4): 1411-7, 1982 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-6284726

RESUMO

1. It has been reported that DNase I can be highly purified from pancreas extract by affinity chromatography on a dDNA-Sepharose column under non-digestive conditions. In the present study, the adsorption-elution of other nucleases on the column under non-digestive conditions was studied. 2. All the seven kinds of nucleases tested were adsorbed when applied on a dDNA-Sepharose column under conditions which did not allow the enzymes to hydrolyze the DNA. The non-digestive conditions were as follows. i) For DNase II (pI=10.2), pH 3.0 in the presence of 50 mM sodium sulfate (inhibitor), ii) for micrococcal nuclease (pI=9.6), pH 4.0 in the absence of Ca2+ (activator), iii) for restriction endonucleases Eco RI (pI=5+1), Hind III (pI=5+1), and Bam HI (pI=5+1), pH 4.0 in the presence of 20% glycerol and 0.1% Neopeptone (stabilizers), and iv) for nucleases S1 (pI=5+1) and nuclease P1 (pI=4.5), pH 7.0. At the respective pH's, the enzymes other than nucleases S1 and P1 were cationic so as to exhibit electrostatic attraction to the anionic dDNA-Sepharose. Although S1 and P1 were anionic, they still adsorbed to the column. 3. All the adsorbed nucleases described above were eluted by a concentration gradient of KCl without changing pH. The ionic strengths required for elution were 0.19 for DNase II, 0.53 for micrococcal nuclease, 0.73 for Eco RI, 0.72 for Hind III, 0.37 for Bam HI, 0.17 for P1, and 0.13 for S1. The fact that the ionic strength required for the elution of DNase I (pI=5.0) was 0.39 at pH 4.0 indicates that the former five enzymes except DNase II can be chromatographed with almost the same or higher efficiency than DNase I, because the proteins adsorbed with no-specific affinity could be mostly eluted at lower ionic strength. On the other hand, the fact that nucleases P1 and S1 were adsorbed in spite of electrostatic repulsion suggests that these two enzymes can also be effectively chromatographed, especially when other cationic proteins are previously removed by an appropriate method such as adsorption to a typical cation exchanger.


Assuntos
Desoxirribonucleases/isolamento & purificação , Endodesoxirribonucleases , Animais , Cromatografia de Afinidade/métodos , DNA , Desoxirribonuclease I , Cães , Endonucleases/isolamento & purificação , Concentração de Íons de Hidrogênio , Técnicas In Vitro , Micrococcus/enzimologia , Sefarose
14.
Surgery ; 99(6): 728-34, 1986 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-3520915

RESUMO

The changes in gastric acid secretion and gut hormone release were investigated in 11 patients who underwent pancreaticoduodenectomy. The amount of acid output showed normoacidity before surgery and hypoacidity after surgery. No peptic ulcers were detectable after surgery. Plasma gastrin levels were markedly reduced after surgery both in the fasting state and after a test meal loading. Although fasting plasma levels of both gastric inhibitory polypeptide (GIP) and insulin after surgery were close to those before surgery, the response of these hormones to the meal was significantly reduced after surgery. On the other hand, blood glucose concentrations increased gradually after feeding, and the elevation was greatly prolonged after surgery compared with preoperative levels. From these results, it is concluded that peptic ulcer will not occur if subtotal gastrectomy is performed during Whipple's procedure. It is presumed that the diminished release of gut hormones such as gastrin, GIP, and insulin was due to the massive resection of the distal stomach, the upper small intestine, and the head of the pancreas and to the diversion of the stream of food from the duodenum to the jejunum. It is also assumed that the glucose-dependent insulinotropic action of GIP would be impaired by the procedure.


Assuntos
Duodeno/cirurgia , Ácido Gástrico/metabolismo , Mucosa Gástrica/metabolismo , Hormônios Gastrointestinais/metabolismo , Pâncreas/cirurgia , Adulto , Idoso , Glicemia/análise , Neoplasias do Sistema Digestório/cirurgia , Ingestão de Alimentos , Feminino , Gastrectomia , Determinação da Acidez Gástrica , Polipeptídeo Inibidor Gástrico/sangue , Gastrinas/sangue , Humanos , Insulina/sangue , Jejuno/cirurgia , Masculino , Pessoa de Meia-Idade , Ductos Pancreáticos/cirurgia
15.
Surgery ; 126(5): 918-24, 1999 11.
Artigo em Inglês | MEDLINE | ID: mdl-10568192

RESUMO

BACKGROUND: The herbal medicine Dai-Kenchu-To, composed of zanthoxylum fruit, ginseng root, and dried ginger rhizome, is clinically effective for uncomplicated postoperative adhesive intestinal obstruction. We investigated the effect of Dai-Kenchu-To and each ingredient on upper gastrointestinal motility and its mechanism of action. METHODS: Five mongrel dogs were equipped with 4-strain gauge-force transducers on the gastric body, antrum, duodenum, and jejunum to measure contractile activity of the circular muscle. Dai-Kenchu-To (1.5 g) or the separate ingredients zanthoxylum fruit, ginseng root, or dried ginger rhizome (1.0 g each) were administered by bolus into the gastric lumen. The effect of atropine, hexamethonium, phentolamine, propranolol, and ondansetron on intragastric Dai-Kenchu-To-induced contractions was studied. RESULTS: Intragastric Dai-Kenchu-To induced phasic contractions in the antrum, duodenum, and jejunum. Zanthoxylum fruit elicited phasic contractions mainly in the duodenum and jejunum, whereas dried ginger rhizome induced phasic contractions in the antrum. Ginseng root had no effect. Phasic contractions induced by intragastric Dai-Kenchu-To were inhibited by atropine and hexamethonium at all sites, although ondansetron inhibited these contractions in the antrum and duodenum. CONCLUSIONS: Intragastric Dai-Kenchu-To stimulates upper gastrointestinal motility through cholinergic and 5-hydroxytryptamine 3 receptors.


Assuntos
Motilidade Gastrointestinal/efeitos dos fármacos , Preparações Farmacêuticas , Extratos Vegetais/farmacologia , Receptores Colinérgicos/fisiologia , Receptores de Serotonina/fisiologia , Animais , Atropina/administração & dosagem , Atropina/farmacologia , Antagonistas Colinérgicos/administração & dosagem , Antagonistas Colinérgicos/farmacologia , Cães , Feminino , Zingiber officinale , Hexametônio/administração & dosagem , Hexametônio/farmacologia , Intubação Gastrointestinal , Masculino , Ondansetron/administração & dosagem , Ondansetron/farmacologia , Panax , Plantas Medicinais , Isoformas de Proteínas/fisiologia , Antagonistas da Serotonina/administração & dosagem , Antagonistas da Serotonina/farmacologia , Zanthoxylum , Zingiberaceae
16.
Surgery ; 123(3): 264-9, 1998 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-9526517

RESUMO

BACKGROUND: Our objective was to examine the accuracy of a 15 MHz ultrasound miniprobe in the pre-operative staging of colorectal cancer by assessing the depth of tumor infiltration and involvement of pericolonic lymph nodes. METHODS: Thirty-three patients with colorectal cancer who underwent ultrasonography with a miniprobe were studied prospectively. The results of this imaging were compared with the histologic findings of the resected specimens. RESULTS: The accuracy of the miniprobe for depth of invasion (T category) was 82% (27 of 33) for all tumors, 76% (13 of 17) in pT1 cases, and 88% (14 of 16) in pT2 to pT4 cases. The accuracy of the miniprobe for nodal staging (N category) was 87% (26 of 30) overall. The sensitivity was 63% (5 of 8), the specificity was 95% (21 of 22), the positive predictive value was 83% (5 of 6), and the negative predictive value was 88% (21 of 24). CONCLUSIONS: The miniprobe is an accurate method for the preoperative TN staging of colorectal cancer. We recommend its preoperative use because the results may influence the surgical approach.


Assuntos
Neoplasias Colorretais/diagnóstico por imagem , Metástase Linfática/diagnóstico por imagem , Estadiamento de Neoplasias/métodos , Idoso , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Invasividade Neoplásica , Ultrassonografia/instrumentação
17.
Neurosci Res ; 34(1): 55-8, 1999 May.
Artigo em Inglês | MEDLINE | ID: mdl-10413328

RESUMO

The effects of chronic L-dopa administration on antidromic excitability and the firing rate of nigrostriatal dopaminergic neurons were investigated in urethane-anesthetized rats. Rats that received daily L-dopa (100 mg/kg) and carbidopa (25 mg/kg) for 60 days showed a marked decrease in terminal excitability compared with the controls. There were no significant differences in the firing rates between the two groups. This finding may be related to impaired striatal dopamine release from exogenous L-dopa subsequent to chronic L-dopa treatment.


Assuntos
Antiparkinsonianos/farmacologia , Carbidopa/farmacologia , Núcleo Caudado/efeitos dos fármacos , Potenciais Evocados/efeitos dos fármacos , Levodopa/farmacologia , Neurônios/efeitos dos fármacos , Animais , Núcleo Caudado/química , Masculino , Ratos , Ratos Sprague-Dawley
18.
Regul Pept ; 79(1): 55-61, 1999 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-9930583

RESUMO

Recent successful synthesis of human glicentin prompted us to establish an immunoassay method for determination of human glicentin in plasma. Human glicentin in plasma was measured using a newly developed sandwich ELISA. The mean fasting levels of human glicentin were 18.6+/-2.4 and 19.7+/-2.1 pM in normal subjects and diabetic patients, respectively. In diabetic patients with renal failure, plasma glicentin was elevated, exceeding 100 pM. In normal subjects, plasma glicentin increased to a peak level of about 130 pM at 60 min after an oral glucose load, and then decreased. In patients who underwent gastrectomy, plasma glicentin rapidly increased to a peak of about 300 pM at 30 min after oral glucose load. In a patient with short bowel syndrome plasma glicentin did not change following an oral glucose load. These results correspond with previous findings for gut glucagon-like immunoreactive materials (GLI) or enteroglucagon. We conclude that glicentin is secreted from the small intestine in response to intraluminal glucose stimulation in humans.


Assuntos
Diabetes Mellitus/sangue , Gastrectomia , Glucagon/sangue , Fragmentos de Peptídeos/sangue , Precursores de Proteínas/sangue , Glicemia/análise , Glicentina , Peptídeos Semelhantes ao Glucagon , Humanos , Insulina/sangue
19.
Neurogastroenterol Motil ; 14(5): 543-51, 2002 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-12358683

RESUMO

The aim was to study the effect of intraduodenal capsaicin on interdigestive gastric contractions. Mongrel dogs were equipped with strain-gauge force transducers to measure gastroduodenal motility. The effects of intraduodenal capsaicin with or without pharmacological antagonists on spontaneous and motilin-induced interdigestive gastric contractions and on plasma motilin were studied in dogs with intact stomachs. The effect of intraduodenal capsaicin on gastric contractions was also studied in vagally denervated gastric (Heidenhain) pouch and vagally innervated antral pouch. Intraduodenal capsaicin inhibited spontaneous and motilin-induced gastric contractions. The spontaneous peak in plasma motilin was inhibited by intraduodenal capsaicin. The effect of intraduodenal capsaicin on motilin-induced gastric contractions was not affected by blockade of nitric oxide synthase, or by beta-adrenoceptor antagonist. Administration of alpha-adrenergic blocker inhibited basal interdigestive gastric motility. Intraduodenal capsaicin had no effect on contractions in the Heidenhain pouch but inhibited those in vagally innervated antral pouch. Duodenal afferent fibres stimulated by capsaicin inhibit gastric contractions via a nitric oxide-independent extrinsic neural reflex.


Assuntos
Capsaicina/administração & dosagem , Duodeno/efeitos dos fármacos , Complexo Mioelétrico Migratório/efeitos dos fármacos , Animais , Cães , Duodeno/fisiologia , Motilidade Gastrointestinal/efeitos dos fármacos , Motilidade Gastrointestinal/fisiologia , Motilina/sangue , Complexo Mioelétrico Migratório/fisiologia
20.
Pancreas ; 16(3): 370-8, 1998 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-9548681

RESUMO

An alteration of the enteroinsular axis (EIA) may be an important etiologic factor in postsurgical changes in gastrointestinal (GI) function. In this review, we present recent works, both from our laboratory and others, on how changes in the EIA function may be involved in postsurgical GI complications, especially late dumping syndrome (LDS). We found no or minimal direct role for vagal signals in the control of gastric inhibitory polypeptide (GIP) and enteroglucagon secretion, which regulate EIA function. In gastrectomized patients, it is suggested that the hypersecretion of glicentin and glucagon-like peptide-1 (GLP-1) induced by a rapid arrival of nutrients to the distal gut suppresses glucagon secretion and may be a cause of LDS. In patients who underwent proctocolectomy, we observed no significant postoperative changes in EIA function, although there are some conflicting reports. It seems unlikely that ordinary pancreaticobiliary diversion would cause a significant change in EIA function after an oral glucose load. Our experimental model of ileojejunal transposition produced marked hypersecretion of incretin secreted from the distal gut, which may alter EIA function. Further elucidation of the regulatory mechanism of EIA may provide a new strategy for the medical and surgical treatment of LDS.


Assuntos
Procedimentos Cirúrgicos do Sistema Digestório , Neurotransmissores/metabolismo , Pâncreas/fisiopatologia , Fragmentos de Peptídeos/metabolismo , Complicações Pós-Operatórias , Síndrome de Esvaziamento Rápido/etiologia , Síndrome de Esvaziamento Rápido/fisiopatologia , Glucagon , Peptídeo 1 Semelhante ao Glucagon , Peptídeos Semelhantes ao Glucagon , Humanos
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