The Effects of Starvation on Lipogenesis in Human Adipose Tissue
Autor: | David J. Galton, J. P. D. Wilson |
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Rok vydání: | 1970 |
Předmět: |
Adult
Male medicine.medical_specialty Adolescent Biopsy Glyceride Coenzyme A Clinical Biochemistry Phospholipid Adipose tissue Palmitic Acids White adipose tissue Fatty Acids Nonesterified Biology Biochemistry Glycerides Fluorides chemistry.chemical_compound Internal medicine medicine Humans Phospholipids Aged chemistry.chemical_classification Carbon Isotopes Fatty Acids Fatty acid Lipid metabolism General Medicine Middle Aged Lipid Metabolism Lipids Phosphoric Monoester Hydrolases Glucose Endocrinology Adipose Tissue chemistry Starvation Lipogenesis Female lipids (amino acids peptides and proteins) Acyltransferases |
Zdroj: | European Journal of Clinical Investigation. 1:94-98 |
ISSN: | 1365-2362 0014-2972 |
Popis: | 1. The effects of starvation on glyceride synthesis have been studied in biopsies of human adipose tissue. After a week's fast glyceride synthesis from glucose (8.3 and 14 mM) was reduced by about 70% in intact adipose tissue; this occurred within 5 days of starting the fast.—2. A method has been devised to follow the simultaneous incorporation of 14C-l-palmitate into acyl-CoA, phospholipid and neutral lipid in homogenates of human adipose tissue. This system was sensitive to fluoride which produced an accumulation of radioactivity in phospholipid and a reduction in neutral lipid.— 3. Starvation also reduced the incorporation of 14C-l-palmitate into neutral lipid in a similar incubation system, but radio-activity now accumulated in long chain acyl-CoA. This suggests that fasting is accompanied by an inhibition of L-glycerol 3-phosphate acyl transferase (E.C. 2.3.1.15).—4. Oleate (600 μM), which is similar to concentrations found in homogenates of fasting adipose tissue, was found to inhibit the activity of acyl transferase by about 80%. The possibility was therefore considered that the reduction of lipogenesis during fasting is mediated by free fatty acid inhibiting the acyl transferase. |
Databáze: | OpenAIRE |
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