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1.
Ciênc. Saúde Colet. (Impr.) ; 20(2): 479-490, fev. 2015. tab
Article in Portuguese | LILACS | ID: lil-742228

ABSTRACT

O presente artigo tem por objetivo avaliar associação entre fatores de risco cardiovascular (FRCV) e indicadores antropométricos em amostra de base populacional de universitários de São Luís/MA. Estudo transversal com 968 universitários, mediana de 22 anos. Glicemia, triglicerídeos (TGL), HDL-c, tabagismo, consumo de álcool, sedentarismo, síndrome metabólica (SM–critérios do Joint Interim Statement) e resistência insulínica (RI), foram associados e correlacionados com os indicadores antropométricos Índice de Massa Corporal (IMC), Circunferência da Cintura (CC), Relação Cintura Quadril (RCQ) e Relação Cintura Altura (RCA). Encontraram-se associações entre TGL, HAS, SM e maiores valores de todas as variáveis antropométricas. RI associou-se a maiores valores IMC e RCA em homens e mulheres. Baixo HDL-c foi associado a maiores valores de todas as variáveis antropométricas em mulheres. Consumo de álcool associou-se a valores mais elevados de IMC e CC em mulheres e RCQ e RCA em homens. Fumo associou-se a maiores valores de RCA em ambos os sexos. Sedentarismo foi associado a maiores valores de RCQ apenas em homens. As correlações mais altas foram estabelecidas para mulheres entre TGL e IMC, CC, RCQ e RCA. Os indicadores que mais se associaram aos FRCV foram IMC, CC e RCA em mulheres e RCQ e RCA em homens.


The article aims to evaluate the relation between cardiovascular risk factors (CVRF) and anthropometric indicators in a sample of university students from São Luís-MA, Brazil. It is a cross-sectional study conducted with 968 university students, with median age of 22. Glycemia, triglycerides, HDL-c, smoking, alcohol consumption, physical inactivity, metabolic syndrome (Joint Interim Statement criteria) and insulin resistance (IR), were associated and correlated with anthropometric indicators such as BMI, WC, WHR and WHtR. Associations were found between TGL, SH, SM and higher values of all anthropometric variables. The RI was associated with higher BMI values and WHtR in men and women. The low HDL-c was associated with higher values of all anthropometric variables in women. Consumption of alcohol was associated with higher values of BMI and WC in women and WHR in men and WHtR. Smoking was associated with higher values of WHtR in both sexes. Physical inactivity was associated with higher values of WHR in men only. The highest correlations were established for women between TGL and BMI CC, WHR and WHtR. The indicators most associated with CVRF were BMI, WC and WHtR in females and WHR and WHtR in men.


Subject(s)
Cysteine Proteases/metabolism , Cysteine Proteinase Inhibitors/chemical synthesis , Cysteine Proteinase Inhibitors/pharmacology , Drug Design , Norwalk virus/enzymology , Chemistry Techniques, Synthetic , Crystallography, X-Ray , Cysteine Proteinase Inhibitors/chemistry , Dose-Response Relationship, Drug , Models, Molecular , Molecular Conformation , Stereoisomerism , Structure-Activity Relationship
2.
Braz. j. med. biol. res ; 47(6): 452-460, 06/2014. tab, graf
Article in English | LILACS | ID: lil-709442

ABSTRACT

It has been previously shown that dextran sulfate administered to diabetic rats accumulates in the liver and kidney, and this could be due to a malfunction of the lysosomal digestive pathway. The aim of the present study was to evaluate the expression and activities of lysosomal enzymes that act upon proteins and sulfated polysaccharides in the livers of diabetic rats. Diabetes mellitus was induced by streptozotocin in 26 male Wistar rats (12 weeks old), while 26 age-matched controls received only vehicle. The livers were removed on either the 10th or the 30th day of the disease, weighed, and used to evaluate the activity, expression, and localization of lysosomal enzymes. A 50-60% decrease in the specific activities of cysteine proteases, especially cathepsin B, was observed in streptozotocin-induced diabetes mellitus. Expression (mRNA) of cathepsins B and L was also decreased on the 10th, but not on the 30th day. Sulfatase decreased 30% on the 30th day, while glycosidases did not vary (or presented a transitory and slight decrease). There were no apparent changes in liver morphology, and immunohistochemistry revealed the presence of cathepsin B in hepatocyte granules. The decrease in sulfatase could be responsible for the dextran sulfate build-up in the diabetic liver, since the action of sulfatase precedes glycosidases in the digestive pathway of sulfated polysaccharides. Our findings suggest that the decreased activities of cathepsins resulted from decreased expression of their genes, and not from general lysosomal failure, because the levels of glycosidases were normal in the diabetic liver.


Subject(s)
Animals , Male , Cathepsin B/metabolism , Diabetes Mellitus, Experimental/enzymology , Liver/enzymology , Lysosomes/enzymology , Albumins/analysis , Blotting, Western , Blood Glucose/drug effects , Cathepsin L/metabolism , Creatinine/urine , Cysteine Proteases/metabolism , Dextran Sulfate/pharmacology , Diabetes Mellitus, Experimental/chemically induced , Gene Expression/drug effects , Glucuronidase/metabolism , Hexosaminidases/metabolism , Immunohistochemistry , Kidney/metabolism , Rats, Wistar , Real-Time Polymerase Chain Reaction , RNA , Sulfatases/metabolism
3.
Medicina (B.Aires) ; 59(supl.2): 7-10, 1999.
Article in Spanish | LILACS | ID: lil-242229

ABSTRACT

La cruzipaína es la cisteína proteinasa principal del parásito causante de la enfermedad de Chagas, Trypanosoma cruzi. La enzima está codificada por un número grande de genes (hasta 130 en la cepa Tul2) dispuestos en tandem cabeza-cola, y ubicados en dos a cuatro cromosomas diferenes, según el clon o cepa del parásito. La expresión simultánea de varios genes diferentes lleva a la producción de una mezcla compleja de isoformas. Las isoformas englobadas en el término "cruzipaína 1" difieren esencialmente en el dominio C-terminal, en su secuencia de aminoácidos y en su patrón de N-glicosilación. Se ha determinado la presencia de una forma que difiere más marcadamente, particularmente en la región catalítica, la cruzipaína 2.


Subject(s)
Animals , Cysteine Proteases/genetics , Trypanosoma cruzi/enzymology , Amino Acid Sequence , Cysteine Proteases/metabolism , Genome, Protozoan
4.
Braz. j. med. biol. res ; 27(12): 2831-42, Dec. 1994. tab
Article in English | LILACS | ID: lil-153282

ABSTRACT

1. A group of plant proteinases is present mainly in the unripe fruit of the papaya tree (Carica papaya), which is a member of the genus Carica. C. candamarcensis is another species that belongs to this group. Its latex contains several proteinases displaying high proteolytic activity. 2. We used several electrophoretic techniques to compare the protein composition of the latex from the two species. Acid electrophoresis followed by staining or Western blot revelated a total of 17 proteins in C. candamarcensis and 7 proteins in C. papaya. Some of the proteins observed in C. papaya have been previously reported in the literature. 3. Electrophoresis on denaturing gels, followed by staining or Western blot revealed the presence of 14 proteins in C. candamarcensis and 6 proteins in C. papaya. Non-equilibrium isoelectrofocusing of the latex from both species showed a larger array of proteins in C. candamarcensis. The analysis of esterase and proteolytic activities on gel fractions after electrophoresis revealed the presence of distinct areas presenting enzyme activity. Some proteins detected in C. candamarcensis have different mobilities when compared with from C. papaya. 4. These results support the view that latex from C. candamarcensis contains a wider diversity of proteins compared to C. papaya, and that some of the proteins not in C. papaya present esterase and proteolytic activity


Subject(s)
Cysteine Proteases/metabolism , Endopeptidases/metabolism , Latex , Peptide Hydrolases/metabolism , Plants/enzymology , Blotting, Western , Electrophoresis, Polyacrylamide Gel , Proteins/biosynthesis
5.
Ciênc. cult. (Säo Paulo) ; 45(5): 339-42, Sept.-Oct. 1993. ilus
Article in English | LILACS | ID: lil-200102

ABSTRACT

Cysteine proteinases have been found in a variety of organisms, and have been implicated in many processes related to pathogenesis in parasites. In this review we discuss cysteine proteinases of Leishmania, that may be involved in mechanisms of survival and growth of these parasites in the microbicidal environment of the macrophage.


Subject(s)
Animals , Cysteine Proteases , Leishmania/enzymology , Cysteine Proteases/physiology , Cysteine Proteases/isolation & purification , Cysteine Proteases/metabolism
6.
Biol. Res ; 26(1/2): 101-7, 1993. ilus, graf
Article in English | LILACS | ID: lil-228595

ABSTRACT

The major cysteine proteinase from Trypanosoma cruzi, cruzipain, can be obtained essentially homogeneous, starting from crude epimastigote extracts, in one step, by affinity chromatography on Cystatin-Sepharose (specific for cysteine proteinases) or ConA-Sepharose (specific for high mannose N-linked glycoproteins). The methods offer considerable potential for enzyme purification from scarce sources, such as other parasite stages or radioactively labelled material with high specific radioactivity


Subject(s)
Animals , Cysteine Proteases/isolation & purification , Trypanosoma cruzi/enzymology , Chromatography, Affinity/methods , Concanavalin A , Cystatins , Cysteine Proteases/metabolism , Sepharose
7.
Biol. Res ; 26(1/2): 151-7, 1993.
Article in English | LILACS | ID: lil-228602

ABSTRACT

Proteolysis of endogenous proteins may play a key role in the adaptation of T. cruzi to the different host environments to which it is exposed during its complex life cycle. For this reason, we have attempted to study the intracellular pathways of protein degradation in the non infective epimastigotes form (EP strain) of T. cruzi. Following intracellular proteolysis by pulse chase experiments with 35 S methionine, we observed a significant inhibition (50 percent) of the degradation of endogenous proteins in log phase parasites in the presence of inhibitors of lysosomal functions, such as chloroquine and E 64. A significant increase in proteolysis was observed in stationary phase parasites which was reverted to log phase values by supplementing the chase medium with 0.5 percent glucose or 10 percent serum, or in the presence of chloroquine. Under this condition of nutritional stress, we could observe an increase in the activity of acid proteases. A significant increase in the degradation rates was observed when abnormal proteins were induced in the parasite by amino acid analogs and puromycin. This increase was not affected by E 64, suggesting the participation of non lysosomal mechanisms in the degradation of rapidly degradable abnormal proteins. Under these conditions, we could observe an increase in high molecular weight conjugates of ubiquitin with respect to endogenous proteins. These results suggest the importance of lysosomal mechanisms in the degradation of cellular proteins in nutritional optimal conditions and during nutritional deprivation, and the possible involvement of the ubiquitin system in the degradation of high turnover proteins


Subject(s)
Animals , Peptide Hydrolases/metabolism , Protozoan Proteins/metabolism , Trypanosoma cruzi/metabolism , Chloroquine/pharmacology , Cysteine Proteases/metabolism , Hydrogen-Ion Concentration , Intracellular Membranes/metabolism , Leucine/analogs & derivatives , Leucine/pharmacology , Molecular Weight , Protease Inhibitors/pharmacology , Puromycin/pharmacology , Time Factors , Trypanosoma cruzi/enzymology , Trypanosoma cruzi/growth & development , Ubiquitin/metabolism
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