ATP-ase activity of mitochondria isolated from needle-biopsy liver samples of diabetic subjects. 1985

A Duţu, and V Borza, and N Mosora, and M Motocu, and G Benga

ATP-ase activity in mitochondria isolated from liver needle-biopsy samples was measured in 5 diabetics, aged 30-63 years and in 4 control subjects of similar age. The mitochondrial fraction was isolated by differential centrifugation of the homogenate and the ATP-ase activity was determined in the optimal conditions previously described for human liver mitochondria. The basal and Mg-stimulated ATP-ase activities were higher, while the DNP-stimulated ATP-ase activity was lower in diabetics compared to controls. The ratio of DNP-ATP-ase/Mg2+-ATP-ase was between 1-2 in diabetics and above 5 in controls. This pattern of ATP-ase activity in diabetics is indicative of mitochondrial damage. No quantitative changes in the amount of mitochondria isolated from liver (expressed in micrograms mitochondrial protein/mg wet tissue) could be noticed in diabetics compared to controls. Consequently, the alterations of ATP-ase activity is probably reflective of impairments of functional integrity of liver mitochondria in diabetics.

UI MeSH Term Description Entries
D008297 Male Males
D008875 Middle Aged An adult aged 45 - 64 years. Middle Age
D008930 Mitochondria, Liver Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4) Liver Mitochondria,Liver Mitochondrion,Mitochondrion, Liver
D003920 Diabetes Mellitus A heterogeneous group of disorders characterized by HYPERGLYCEMIA and GLUCOSE INTOLERANCE.
D005260 Female Females
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000251 Adenosine Triphosphatases A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA. ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D000328 Adult A person having attained full growth or maturity. Adults are of 19 through 44 years of age. For a person between 19 and 24 years of age, YOUNG ADULT is available. Adults
D001707 Biopsy, Needle Removal and examination of tissue obtained through a transdermal needle inserted into the specific region, organ, or tissue being analyzed. Aspiration Biopsy,Puncture Biopsy,Aspiration Biopsies,Biopsies, Aspiration,Biopsies, Needle,Biopsies, Puncture,Biopsy, Aspiration,Biopsy, Puncture,Needle Biopsies,Needle Biopsy,Puncture Biopsies
D017301 Ca(2+) Mg(2+)-ATPase An enzyme that catalyzes the hydrolysis of ATP and is activated by millimolar concentrations of either Ca(2+) or Mg(2+). Unlike CA(2+)-TRANSPORTING ATPASE it does not require the second divalent cation for its activity, and is not sensitive to orthovanadate. (Prog Biophys Mol Biol 1988;52(1):1). A subgroup of EC 3.6.1.3. ATPase, Calcium Magnesium,ATPase, Magnesium,Adenosinetriphosphatase, Calcium, Magnesium,Adenosinetriphosphatase, Magnesium,Calcium Magnesium ATPase,Calcium Magnesium Adenosinetriphosphatase,Magnesium ATPase,Magnesium Adenosinetriphosphatase,Adenosine Triphosphatase, Calcium, Magnesium,Adenosine Triphosphatase, Magnesium,Ca Mg-ATPase,Ca2+-Mg2+ ATPase,Calcium Magnesium Adenosine Triphosphatase,Mg2+-ATPase,Mg2+-Dependent ATPase,ATPase, Ca2+-Mg2+,ATPase, Mg2+-Dependent,Adenosinetriphosphatase, Calcium Magnesium,Ca Mg ATPase,Ca2+ Mg2+ ATPase,Magnesium Adenosine Triphosphatase,Mg2+ ATPase,Mg2+ Dependent ATPase

Related Publications

A Duţu, and V Borza, and N Mosora, and M Motocu, and G Benga
March 1955, The Journal of biophysical and biochemical cytology,
A Duţu, and V Borza, and N Mosora, and M Motocu, and G Benga
September 1950, The Biochemical journal,
A Duţu, and V Borza, and N Mosora, and M Motocu, and G Benga
November 2010, Biochemical and biophysical research communications,
A Duţu, and V Borza, and N Mosora, and M Motocu, and G Benga
December 2002, Analytical biochemistry,
A Duţu, and V Borza, and N Mosora, and M Motocu, and G Benga
June 1973, Endokrinologie,
A Duţu, and V Borza, and N Mosora, and M Motocu, and G Benga
January 1969, Voprosy meditsinskoi khimii,
A Duţu, and V Borza, and N Mosora, and M Motocu, and G Benga
February 1984, Clinical science (London, England : 1979),
A Duţu, and V Borza, and N Mosora, and M Motocu, and G Benga
January 1965, Histochemie. Histochemistry. Histochimie,
A Duţu, and V Borza, and N Mosora, and M Motocu, and G Benga
September 1970, Biochemical and biophysical research communications,
Copied contents to your clipboard!