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1.
Saudi Medical Journal. 2011; 32 (5): 467-473
in English | IMEMR | ID: emr-109362

ABSTRACT

To identify renal clear cell carcinoma-associated marker proteins. Twelve patients with renal cell carcinoma [RCC] were collected and processed in the Department of Urology, Renmin Hospital, Wuhan University, China, between January 2008 and September 2009. Two-dimensional polyacrylamide gel electrophoresis and matrix assisted laser desorption ionisation time-of-flight mass spectrometry [MALDI-TOF-MS] were employed to investigate differentially expressed protein spots between RCC tissues and adjacent normal tissues, then reverse transcription polymerase chain reaction and western blot were employed to confirm the proteomic results. One protein spot was up regulated, 13 were downregulated, and 22 were absent in RCC tissues. Four of the absent proteins were L-arginine-glycine amidinotransferase [AGAT], Betaine-homocysteine S-methyltransferase [BHMT], Ketohexokinase [KHK], and Neuropolypeptide h3 [NPh3]. The reverse transcriptase-polymerase chain reaction analysis demonstrated mRNA expression of AGAT, BHMT, and Nph3 was significantly decreased in 12 RCC tissues. In addition, Western blot analysis showed AGAT protein was absent in 11/12, BHMT in 9/12, and Nph3 in 5/12 RCC tissues. Absence of AGAT, BHMT, and Nph3 is common events in clear cell RCC; hence, it may be involved in the development of RCC; therefore, they have the potential to be tumor markers for diagnosis, treatment, and prognosis of RCC patients


Subject(s)
Humans , Betaine-Homocysteine S-Methyltransferase , Amidinotransferases , Phosphatidylethanolamine Binding Protein , Electrophoresis, Polyacrylamide Gel , Electrophoresis, Gel, Two-Dimensional , Reverse Transcriptase Polymerase Chain Reaction , Blotting, Western
2.
Genet. mol. biol ; 28(1): 44-45, Jan.-Mar. 2005.
Article in English | LILACS | ID: lil-399614

ABSTRACT

The GATM gene encodes L-arginine:glycine amidinotransferase, which catalyzes the conversion of L-arginine into guanidinoacetate, the rate-limiting step in the synthesis of creatine. Since, deficiencies in creatine synthesis and transport lead to certain forms of mental retardation in human, the human GATM gene appears to be involved in brain development. Recently it has been demonstrated that the mouse Gatm is expressed during development and is imprinted with maternal expression in the placenta and yolk sac, but not in embryonic tissues. We investigated the imprinting status of the human GATM by analyzing its expression in four human placentas. GATM was biallelically expressed, thus suggesting that this gene escapes genomic imprinting in placentas, differently from what has been reported in mouse extra-embryonic tissues.


Subject(s)
Humans , Animals , Female , Amidinotransferases , Genomic Imprinting , Glycine , Creatinine , Placenta , Polymorphism, Genetic
3.
Indian J Exp Biol ; 2004 Sep; 42(9): 876-83
Article in English | IMSEAR | ID: sea-58211

ABSTRACT

Therapeutic efficacy of EGTA (ethylene glycol bis (2-aminoethyl ether) tetraacetic acid) against cerium intoxicated mice was studied. Administration of cerium showed significant decrease in haemoglobin percentage, RBC counts and blood glucose level with an increase in the activity of serum transaminases and WBC counts. Decrease in the activity of alkaline phosphatase and glycogen content was noted in liver and kidney after cerium exposure. Light and electron microscopical investigations showed that these changes were recouped considerably with the administration of EGTA suggesting its therapeutic efficacy against cerium toxicity.


Subject(s)
Alkaline Phosphatase/metabolism , Amidinotransferases/metabolism , Animals , Blood Glucose/metabolism , Cerium/administration & dosage , Chelating Agents/therapeutic use , Egtazic Acid/therapeutic use , Erythrocyte Count , Glycogen , Hemoglobins/metabolism , Kidney/drug effects , Leukocyte Count , Liver/drug effects , Male , Mice
4.
Hindustan Antibiot Bull ; 1994 Feb-May; 36(1-2): 30-3
Article in English | IMSEAR | ID: sea-2444

ABSTRACT

Intermediary enzymes of streptomycin biosynthesis-arginine amidinotransferase and alkaline phosphatase were located at the early fermentation stages. Their relationship with streptomycin production by Streptomyces griseus strains GX-19 and MR-20 was determined and the use of this relationship was made for the screening of streptomycin producing mutant strains.


Subject(s)
Alkaline Phosphatase/metabolism , Amidinotransferases/metabolism , Streptomyces griseus/enzymology , Streptomycin/biosynthesis
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