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1.
J Biomol Struct Dyn ; 38(10): 2884-2897, 2020 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-31345118

RESUMEN

In this study, we aimed to identify critical factors associated with superoxide dismutase 2 (SOD2) in human keratinocytes through gene and protein expression profiling approaches. After recombinant SOD2 was exogenously added to culture media, we conducted serial OMICS studies, which included RNA sequencing analysis, integrated antibody-chip arrays, and the implementation of bioinformatics algorithms, in order to reveal genes and proteins that are possibly associated with SOD2 in keratinocytes. These approaches identified several novel genes and proteins in keratinocytes that are associated with exogenous SOD2. These novel genes included DCT, which was up-regulated, and CD38, GPR151, HCK, KIT, and AFP, which were down-regulated. Among them, CD38 and KIT were also predicted as hub proteins in PPI mappings. By integrating the datasets obtained from these complementary high-throughput OMICS studies and utilizing the strengths of each method, we obtained new insights into the functional role of externally added SOD2 in skin cells and into several critical genes that are thought to play important roles in SOD2-associated skin function. The approach used here could help contribute to our clinical understanding of SOD2-associated applications and may be broadly applicable to a wider range of diseases. AbbreviationsSOD2superoxide dismutase 2DAVIDthe database for annotation, visualization and integrated discoveryKEGGKyoto Encyclopedia of Genes and GenomesPPIprotein-protein interactionsHTSHigh-throughput screeningCommunicated by Ramaswamy H. Sarma.


Asunto(s)
Biología Computacional , Superóxido Dismutasa , Humanos , Queratinocitos , Análisis de Secuencia de ARN , Superóxido Dismutasa/genética
2.
Zhongguo Zhong Yao Za Zhi ; 38(12): 1915-8, 2013 Jun.
Artículo en Chino | MEDLINE | ID: mdl-24066583

RESUMEN

The dried Whitmania pigra is used for the treatment of cardiovascular and cerebrovascular diseases in traditional Chinese medicine. Bellamya purificata is widely distributed in the Chang Jiang River basin, it is natural diets of W. pigra. Current study was conducted to compare and analyze the nutritional ingredient in W. pigra, body fluid and flesh of B. purificata. Results showed that the contents of protein, crude fat and total sugar in W. pigra, body fluid and flesh of B. purificata were significantly different (P < 0.05). Protein content in W. pigra accounts up to 65.01%. The contents of inorganic elements and amino acid were abundant in W. pigra, body fluid and flesh of B. purificata. The content of essential amino acids in them were 32.6, 221.59, 40.78 mg x g(-1), respectively. The content of flavor amino acid in them were 27.51, 14.5, 32.03 mg x g(-1), while the coresponding content of antioxidant amino acid were 8.81, 5.91, 9.73 mg x g(-1), respectively. The individual amino acids of high content in them were Glu, Asp and Leu. Macro elements Ca, P, Mg and trace elements Zn, Si, Fe were abundant. It could be speculated that W. pigra may be a promising novel food, and the present results provide a foundation to develop artificial feed for W. Pigra.


Asunto(s)
Gastrópodos/química , Sanguijuelas/química , Aminoácidos/análisis , Animales , Medicina Tradicional China
3.
J Enzyme Inhib Med Chem ; 24(1): 234-40, 2009 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-18608781

RESUMEN

The present work focused on the kinetics of the inhibitory effects of the leaf extract of Siberian Crabapple, named Shan jingzi in China, on chicken liver fatty acid synthase. The results showed that this extract had much stronger inhibitory ability on fatty acid synthase than that from green teas described in many previous reports. The inhibitory ability of this extract is closely related to the extracting solvent, and the time of extraction was also an important influencing factor. The inhibitory types of this extract on diffeerent substrates of chicken liver fatty acid synthase, acetyl-CoA, malonyl-CoA and NADPH, were found to be noncompetitive, uncompetitive and mixed, respectively. The studies here shed a new light on the exploration for inhibitors of fatty acid synthase.


Asunto(s)
Ácido Graso Sintasas/antagonistas & inhibidores , Malus/química , Extractos Vegetales/aislamiento & purificación , Animales , Pollos , Cinética , Extractos Vegetales/farmacología , Hojas de la Planta/química , Solventes
4.
Int J Biochem Cell Biol ; 36(3): 447-59, 2004 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-14687923

RESUMEN

The thermostability of an enzyme that exhibits phytase and acid phosphatase activities was studied. Kinetics of inactivation and unfolding during thermal denaturation of the enzyme were compared. The loss of phytase activity on thermal denaturation is most suggestive of a reversible process. As for acid phosphatase activities, an interesting phenomenon was observed; there are two phases in thermal inactivation: when the temperature was between 45 and 50 degrees C, the thermal inactivation could be characterized as an irreversible inactivation which had some residual activity and when the temperature was above 55 degrees C, the thermal inactivation could be characterized as an irreversible process which had no residual activity. The microscopic rate constants for the free enzyme and substrate-enzyme complex were determined by Tsou's method [Adv. Enzymol. Relat. Areas Mol. Biol. 61 (1988) 381]. Fluorescence analyses indicate that when the enzyme was treated at temperatures below 60 degrees C for 60 min, the conformation of the enzyme had no detectable change; when the temperatures were above 60 degrees C, some fluorescence red-shift could be observed with a decrease in emission intensity. The inactivation rates (k(+0)) of free enzymes were faster than those of conformational changes during thermal denaturation at the same temperature. The rapid inactivation and slow conformational changes of phytase during thermal denaturation suggest that inactivation occurs before significant conformational changes of the enzyme, and the active site of this enzyme is situated in a relatively fragile region which makes the active site more flexible than the molecule as a whole.


Asunto(s)
6-Fitasa/química , Fosfatasa Ácida/química , Conformación Proteica , 6-Fitasa/antagonistas & inhibidores , 6-Fitasa/metabolismo , Fosfatasa Ácida/antagonistas & inhibidores , Fosfatasa Ácida/metabolismo , Compuestos de Anilina/química , Alimentación Animal/normas , Aditivos Alimentarios/normas , Calor , Cinética , Compuestos Organofosforados/química , Fósforo/química , Desnaturalización Proteica , Espectrometría de Fluorescencia
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