Fatty acids pathological concentrations

The metabolism of CLA in peroxisomes shows interesting aspects in terms of a possible role in the formation and concentration of eicosanoids, especially as effected in different pathologic conditions. By either competing with linoleic acid for desaturation and elongation, or via peroxisomal P-oxidation, CLA may interfere with eicosanoid production and degradation. It is likely however that its action may depend on its incorporation and thereby its concentration in different tissues. The different rate of peroxisomal P-oxidation between t 0,c 2 and c9,tll, may also explain the different biological activities of the two isomers. Also, enhanced fatty acid oxidation... 

In normal liver, only relatively small amounts of ketone bodies are formed. Their concentration in the blood is 0.5-D.8 mg per 100 ml plasma. The acetoacetate produced by this physiological K. is degraded in the peripheral musculature. Coenzyme A from succi-nyl-CoA is transferred to the acetoacetate by aceto-acetate succinyl-CoA transferase. Direct activation of acetoacetate by coenzyme A and ATP can also occur (Fig, 2). The acetoacetyl-CoA produced in either case is thioclastically cleaved into two molecules of acetyl-CoA, consuming a CoA molecule in the process. In carbohydrate deficiency (starvation, ketone-mia in ruminants), or deficient carbohydrate utilization (diabetes mellitus), K. is greatly increased. The cause of this pathological K. is a disturbance of the equilibrium between the degradation of fatty acids to acetyl-CoA and its utilization in the tricarboxylic acid cycle. The several-fold increase in the oxidation of the fatty acids leads under these conditions to an increase in the intracellular acetyl-CoA concentration. This leads to the condensation of 2 molecules of... 

Murine Hsp25 and human Hsp27 act as molecular chaperones and are constitutively expressed in several mammalian cells, particularly in pathological conditions Short-chain fatty acids, such as butyrate, induce a time- and concentration-dependent increase in Hsp25 protein expression in rat intestinal epithelial cells Small heat-shock proteins share functions as diverse as protection against toxicity mediated by aberrantly folded proteins or oxidative-inflammation conditions These proteins can have... 

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