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1.
Diabetes Res Clin Pract ; 104(1): e5-7, 2014 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-24565212

RESUMO

Post-absorptive glucose lowering (PALG) is observed in individuals with glucose intolerance and in healthy individuals. We report a prevalence of about 23% among healthy Asian Indians. Individuals with PALG are characterized by leaner phenotype, low body fat percentage, increased insulin sensitivity and higher fasting glucose levels.


Assuntos
Glicemia/metabolismo , Intolerância à Glucose/epidemiologia , Glucose/farmacocinética , Hiperinsulinismo/epidemiologia , Resistência à Insulina , Adolescente , Adulto , Jejum , Feminino , Intolerância à Glucose/sangue , Intolerância à Glucose/diagnóstico , Teste de Tolerância a Glucose , Humanos , Hiperinsulinismo/sangue , Hiperinsulinismo/diagnóstico , Incidência , Índia/epidemiologia , Insulina/sangue , Masculino , Prevalência , Adulto Jovem
2.
Indian J Biochem Biophys ; 28(5-6): 389-94, 1991.
Artigo em Inglês | MEDLINE | ID: mdl-1812072

RESUMO

Candida 107 (NCYC 911) accumulates up to 45% of the biomass as triglycerides under conditions of nitrogenous substrate limitation in the medium. In oilseeds and adipocytes, lipid accumulation is preceded and accompanied by increased activity of key enzymes such as pyruvate dehydrogenase. However, in Candida 107, the activity of this complex was greatly reduced during lipogenesis. The initial velocity patterns were in accordance with a Hexa Uni Ping Pong mechanism. The Km values for the various substrates were similar to those found for the yeast Saccharomyces cerevisiae, but much higher than those reported for the mammalian enzyme. Product inhibition studies indicated that the Ki for acetyl coenzyme A and NADH were higher than those reported for other yeasts. The values for Ki were similar to those found for the liver enzyme, whereas the enzyme complex from heart had much lower Ki values for products. It has been suggested that in the heart and kidney, pyruvate dehydrogenase is regulated by product inhibition whereas in the liver this does not appear to be the mechanism. Therefore, it is probable, that like the liver enzyme, pyruvate dehydrogenase from Candida 107 may not be regulated by product inhibition.


Assuntos
Complexo Piruvato Desidrogenase/metabolismo , Acetilcoenzima A/farmacologia , Candida/metabolismo , Cinética , Metabolismo dos Lipídeos , NAD/farmacologia , Complexo Piruvato Desidrogenase/antagonistas & inibidores
3.
Int J Cosmet Sci ; 7(1): 9-14, 1985 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-19460009

RESUMO

Synopsis Chemical microbial inhibitors compatible with formulations of soaps and deodorant perfumes are more effective if they are substantive to the skin. However, highly effective inhibitors are toxic and their substantivity on skin may accentuate the toxicity. Natural compounds such as short to medium chain fatty acids and their derivatives, which are known to be germicidal, offer a viable alternative to chemical inhibitors. We report here the synthesis of sodium 2-lauroyloxy propionate and an in vivo method to test its substantivity on skin following its incorporation in soaps. Among several compounds tested, sodium 2-lauroyloxy propionate was found to be highly substantive in soap formulation.

6.
Proc Natl Acad Sci U S A ; 75(12): 6115-9, 1978 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-282629

RESUMO

A cell surface component from quiescent BALB/c 3T3 mouse cells that inhibits DNA synthesis and cell division when added to a culture of growing 3T3 cells has been detected. The inhibition of DNA synthesis by this factor was dependent on concentration and time of incubation; a transient exposure of cells to the factor followed by incubation in its absence for 20 hr was sufficient to elicit its inhibitory effect. The active component appears to be protein in nature, as judged by heat inactivation and trypsin sensitivity. Extracts obtained in an identical manner from quiescent 3T3 cells that had been preincubated in situ with uridine diphosphate N-acetyl-D-glucosamine (UDP-GlcNAc) did not inhibit DNA synthesis. The effect was specific for UDP-GlcNAc: incubation with three other nucleotide sugars yielded active component. Incubation of the inactive component from UDP-GlcNAc-treated cells with purified N-acetyl-beta-D-glucosaminidase in vitro restored its inhibitory property. Extracts from growing cells failed to inhibit DNA synthesis. These results suggest that reversible glycosylation with N-acetyl-D-glucosamine residues may serve as a regulatory signal for the conversion of the active factor to its inactive form. We propose that the onset of quiescence of 3T3 cells is due to a casual relationship between depletion of growth factors in the culture medium and the presence of the active regulatory factor on the cell surface that inhibits DNA synthesis; conversion of the regulatory factor to its inactive form under favorable nutritional status may be viewed as a switch that allows DNA synthesis to resume.


Assuntos
DNA/biossíntese , Glicoproteínas/metabolismo , Substâncias de Crescimento/farmacologia , Acetilglucosamina/metabolismo , Linhagem Celular , Fibroblastos/fisiologia , Glicoproteínas/farmacologia , Cinética , Proteínas de Membrana/fisiologia
7.
Proc Natl Acad Sci U S A ; 75(8): 3859-62, 1978 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-279000

RESUMO

Preincubation of quiescent BALB/C3T3 cells with uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) in conditioned medium resulted in a time- and concentration-dependent stimulation of uptake of 2-deoxyglucose, uridine, and alpha-aminoisobutyric acid over that seen in conditioned medium alone. The apparent Km values for 2-deoxyglucose and uridine uptake were the same for cells incubated with or without UDP-GlcNAc, whereas the Vmax values were higher for cells pretreated with the nucleotide sugar. The stimulation of uptake was specific for UDP-GlcNAc, and the other nucleotide sugars tested were ineffective; incubation of UDP-GlcNAc-pretreated cells with N-acetylglucosaminidase abolished the stimulatory effect. In all cases, the extent of stimulation of nutrient uptake was comparable to that seen with serum-stimulated cells. Incubation of quiescent cells in situ with UDP-[3H]GlcNAc led to incorporation of radioactive N-acetylglucosamine into the acid-precipitable fraction; a large fraction of the labeled amino sugar was found on the cell surface acceptors. We interpret these data to mean that the cellular acceptors of quiescent cells are "under-glycosylated," at least in terms of N-acetylglucosamine, and that stimulation of uptake of nutrients may be a consequence of restoration of the amino sugar residues on the oligosaccharide chains of acceptors on the cell surface.


Assuntos
Ácidos Aminoisobutíricos/metabolismo , Desoxiaçúcares/metabolismo , Desoxiglucose/metabolismo , Uridina Difosfato N-Acetilglicosamina/farmacologia , Açúcares de Uridina Difosfato/farmacologia , Uridina/metabolismo , Acetilglucosamina/metabolismo , Sítios de Ligação , Membrana Celular/metabolismo , Células Cultivadas
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