L-Carnitine (C) is required for intramitochondrial transport of FFA to the sites of beta-oxidation: in muscle the oxidation of long chain fatty acids is mostly C dependent. It is also accepted that C may shuttle acetyl-groups from the mytochondrial matrix to the cytosol for FFA synthesis and, in liver, TG synthesis.

La L-carnitine plasmatique est abaissee chez les patients en hemodialyse. La supplementation stimule l'oxydation des acides gras a chaine longue. Paradoxalement, l'administration de carnitine i.v., pendant la dialyse augmente la triglyceridemie, l'acetate sanguine et abaisse les tricarbonates. L'etude de l'effet de l'ajout de carnitine au liquide de dialyse permet de formuler l'hypothese suivante: la carnitine stimulerait l'oxydation du pyruvate en acetyl CoA, et diminuerait le Coenzyme A disponible pour la conversion de l'acetate et des acides gras en acetyl CoA. L'ajout de carnitine au liquide de dialyse n'entraine pas d'elevation des taux de triglycerides et d'acetate plasmatiques

The effects of nutrition and disease state on whole body protein metabolism have been widely studied in recent years, but the distribution of changes among the various body tissues is less known. It is, therefore, important to establish the contribution made by skeletal muscle to whole body protein metabolism in disease state, because skeletal muscle is quantitatively and metabolically the most important body protein “store”1 and remains a good marker of protein-energy malnutrition (PEM) when the protein pools of other tissues and organs become metabolically una vailable 1-3.

Journal of Parenteral and Enteral NutritionVolume 11, Issue 5S p. 55S-63S Direct Biochemical Analysis of Human Muscle Tissue in Hospital Malnutrition G.F. Guarnieri, G.F. Guarnieri Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this authorG. Toigo, G. Toigo Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this authorR. Situlin, R. Situlin Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this authorM.A. Del Bianco, M.A. Del Bianco Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this authorL. Crapesi, L. Crapesi Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this authorA. Zanettovich, A. Zanettovich Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this author G.F. Guarnieri, G.F. Guarnieri Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this authorG. Toigo, G. Toigo Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this authorR. Situlin, R. Situlin Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this authorM.A. Del Bianco, M.A. Del Bianco Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this authorL. Crapesi, L. Crapesi Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this authorA. Zanettovich, A. Zanettovich Institute of Medical Pathology, University of Trieste, ItalySearch for more papers by this author First published: 01 September 1987 https://doi.org/10.1177/014860718701100507Citations: 12AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Citing Literature Volume11, Issue5SSeptember 1987Pages 55S-63S RelatedInformation

Malnutrition is a common finding in chronic pancreatitis and its pathogenesis is multifactorial. In 14 patients with chronic pancreatitis we assessed the dietary intake, some anthropometric indices and the concentration of some serum proteins. In muscle specimens obtained by needle biopsy we examined the DNA, RNA and non-collagen alkali-soluble protein (ASP) content. In muscle we determined also the activity of cathepsin D, an enzyme involved in intracellular myofibrillar catabolism. Protein and energy intake were lower than in the normal healthy population. Plasma protein content (an index of liver protein synthesis) was generally in the normal range, whereas anthropometry and the biochemical muscle indices were generally subnormal, suggesting a depressed muscle protein content and synthesis (evaluated, respectively, by the ASP: DNA and RNA: DNA ratios). Cathepsin D activity was lower than in controls, and the percentage of 'free' activity tended to be higher but not significantly. This study suggests that muscle protein content and synthesis are reduced in patients with chronic pancreatitis, whereas liver protein synthesis is generally preserved. Possibly as a consequence of metabolic abnormalities and/or of an inadequate protein and energy intake, the nutritional status was often abnormal in our patients and a nutritional support therapy was needed.