Metabolic changes in the quadriceps femoris muscle of obese people. Enzyme activity patterns of energy-supplying metabolism. 1975

A Bass, and K Vondra, and R Rath, and V Vítek, and T Havránek

1. In biopsy samples of the lateral part of m. quadriceps femoris of 49 obese and 14 lean persons the activities of the following enzymes were investigated: triosephosphate dehydrogenase (TPDH), glycerolphosphate: nad dehydrogenase (GPDH), lactate dehydrogenase (LDH), hexokinase (HK), malate: NAD dehydrogenase (MDH), citrate synthase (CS) and hydroxyacyl-CoA dehydrogenase (HOADH). 2. The muscles of obese had an increased activity ratio of TPDH to CS and to HK, respectively, caused in muscles of female obese subjects by an increase of TPDH activity, in those of obese men rather by a decrease of CS and HK activities. 3. Cluster analysis brough to light the existence of three major groups. Group 1 (low activity-low LDH group), consisting of muscles of female obese subjects only, exhibited low activities of all enzymes investigated, that of LDH being so low as to possibly induce a serious deficiency of anerobic metabolism under working conditions. Group 2 (medium enzyme activity group) was characterized by medium enzyme activities, similar to that of lean controls (included in this group). This consisted of subjects of both sex. Group 3 (high enzyme activity group) consisted of obese of both sex. It was distinguished by high enzyme activities, especially of LDH. It is suggested that the groups of similar enzyme activity patterns might reflect different stages, types and/or genesis of obesity.

UI MeSH Term Description Entries
D007770 L-Lactate Dehydrogenase A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist. Lactate Dehydrogenase,Dehydrogenase, L-Lactate,Dehydrogenase, Lactate,L Lactate Dehydrogenase
D008291 Malate Dehydrogenase An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37. Malic Dehydrogenase,NAD-Malate Dehydrogenase,Dehydrogenase, Malate,Dehydrogenase, Malic,Dehydrogenase, NAD-Malate,NAD Malate Dehydrogenase
D008297 Male Males
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009765 Obesity A status with BODY WEIGHT that is grossly above the recommended standards, usually due to accumulation of excess FATS in the body. The standards may vary with age, sex, genetic or cultural background. In the BODY MASS INDEX, a BMI greater than 30.0 kg/m2 is considered obese, and a BMI greater than 40.0 kg/m2 is considered morbidly obese (MORBID OBESITY).
D002950 Citrate (si)-Synthase Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7. Citrate Synthase,Synthase, Citrate
D003065 Coenzyme A CoA,CoASH
D004734 Energy Metabolism The chemical reactions involved in the production and utilization of various forms of energy in cells. Bioenergetics,Energy Expenditure,Bioenergetic,Energy Expenditures,Energy Metabolisms,Expenditure, Energy,Expenditures, Energy,Metabolism, Energy,Metabolisms, Energy
D005260 Female Females
D005987 Glyceraldehyde-3-Phosphate Dehydrogenases Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD. GAPD,Glyceraldehyde-3-Phosphate Dehydrogenase,Glyceraldehydephosphate Dehydrogenase,Phosphoglyceraldehyde Dehydrogenase,Triosephosphate Dehydrogenase,Dehydrogenase, Glyceraldehyde-3-Phosphate,Dehydrogenase, Glyceraldehydephosphate,Dehydrogenase, Phosphoglyceraldehyde,Dehydrogenase, Triosephosphate,Dehydrogenases, Glyceraldehyde-3-Phosphate,Glyceraldehyde 3 Phosphate Dehydrogenase

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