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Fatty acids resources:

Fatty acids research abs 1 || Fatty acids research abs 2 || Fatty acids research abs 3 || Fatty acids research abs 4

J Lipid Res. 2001 Feb;42(2):225-34.
Diacylglycerol transport in the insect fat body: evidence of involvement of lipid droplets and the cytosolic fraction.

Arrese EL, Gazard JL, Flowers MT, Soulages JL, Wells MA.

Department of Biochemistry and Center for Insect Science, University of Arizona, Tucson 85721, USA. esteliochem.okstate.edu

In this report we show the existence of a distinct pool of fat body diacylglycerol (DG) that can be distinguished from the bulk DG. This is a dynamic pool of DG that uses FA entering the fat body from the hemolymph, whereas the bulk DG uses the fatty acids stored in the fat body fat droplets. Using a dual labeling technique, it was possible to compare the effect of hormone-stimulated DG synthesis and secretion on the distribution of radiolabeled FA among the lipids of the dynamic pool (short-term radiolabeling), with the hormonal effect on the total complement of fat body lipids (long-term radiolabeling). We observed that, whereas DG represents 2% to 3% of the fat body lipid mass, about 20% of the short-term radiolabeled lipids are represented by DG. Stimulation of lipolysis produces a fast decrease in the fraction of short-term radiolabeled DG, whereas there is an increase in the mass of fat body DG. The subcellular distribution of bulk DG showed that its majority (62%) was in the fat cake whereas only 2.9% was in the cytosol. On lipolysis stimulation, the largest changes in specific activities of newly synthesized DG were detected in the cytosol and the fat cake, suggesting that newly synthesized DG localized in the lipid droplets and the cytosol is preferentially mobilized.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11181752&dopt=Abstract

J Lipid Res. 2001 Feb;42(2):241-8.
ApoA-II expression in CETP transgenic mice increases VLDL production and impairs VLDL clearance.

Escola-Gil JC, Julve J, Marzal-Casacuberta A, Ordonez-Llanos J, Gonzalez-Sastre F, Blanco-Vaca F.

Servei de Bioquimica, de l'Hospital de la Santa Creu i Sant Pau, 08025 Barcelona, Spain.

Apolipoprotein (apo)A-II is a major high density lipoprotein (HDL) protein; however, its role in lipoprotein metabolism is largely unknown. Transgenic (Tg) mice that overexpress human apoA-II present functional lecithin: cholesterol acyltransferase deficiency, HDL deficiency, hypertriglyceridemia and, when fed an atherogenic diet, increased non-HDL cholesterol and increased susceptibility to atherosclerosis. In contrast to humans, mice do not present cholesteryl ester transfer protein (CETP) activity in plasma. To study the in vivo interaction of these two proteins, we crossbred human apoA-II and CETP-Tg mice. CETP x apoA-II-Tg mice fed an atherogenic diet, compared with CETP-Tg mice presented a 2-fold decrease in HDL cholesterol and a quantitatively similar increase in total plasma cholesterol and percentage of free cholesterol, non-HDL cholesterol, and free fatty acids, together with a remarkable 112-fold increase in plasma triglycerides. Plasma triglycerides in CETP x apoA-II-Tg mice were mainly associated with very low density lipoproteins (VLDL), which were also enriched in protein content, and resulted from a combination of higher production rate compared with both of their progenitors and non-Tg control mice, and decreased catabolism compared only with CETP-Tg mice. These results show CETP x apoA-II-Tg mice to be a good model with which to study mechanisms leading to VLDL overproduction and suggest that CETP and, in particular apoA-II, may play a role in the regulation of VLDL metabolism.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11181754&dopt=Abstract

Lab Invest. 2003 Mar;83(3):397-408.
Abnormal expression of the novel epidermal enzyme, glucosylceramide deacylase, and the accumulation of its enzymatic reaction product, glucosylsphingosine, in the skin of patients with atopic dermatitis.

Ishibashi M, Arikawa J, Okamoto R, Kawashima M, Takagi Y, Ohguchi K, Imokawa G.

Department of Dermatology, Tokyo Women's Medical University, Tokyo, Japan.

To clarify mechanisms underlying acylceramide deficiency as an causative factor of the permeability barrier disruption seen in the skin of patients with atopic dermatitis (AD), we hypothesized and then demonstrated the presence of a novel epidermal enzyme, termed glucosylceramide (GC) deacylase. This enzyme hydrolyzes (acyl)GC at the N-acyl site to yield its lysoform, glucosylsphingosine (GS), instead of the formation of (acyl)ceramides by beta-glucocerebrosidase. Assays of enzymatic activity using [palmitic acid-(14)C] GC as a substrate revealed that extracts from the stratum corneum and from the epidermis (but not from the dermis) of patients with AD have the significantly higher potential to hydrolyze GC at the N-acyl site to release (14)C-labeled free fatty acid than of healthy controls. To determine the in vivo physiologic function of this novel enzyme, we measured the metabolic product GS in the upper stratum corneum. In both the involved and the uninvolved stratum corneum from patients with AD, there were significant increases in the amounts of GS compared with healthy controls and there was a significant inverse correlation with the decreased content of ceramides or ceramide-1 (acylceramide). Thus, collectively these results strongly suggest the physiologic relevance of GC deacylase to the acylceramide deficiency seen in the stratum corneum of patients with AD.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12649340&dopt=Abstract

J Neurochem. 2001 Feb;76(4):1129-41.
Chemical deacylation reduces the adhesive properties of proteolipid protein and leads to decompaction of the myelin sheath.

Bizzozero OA, Bixler HA, Davis JD, Espinosa A, Messier AM.

Department of Cell Biology and Physiology, University of New Mexico-Health Sciences Center, Albuquerque, New Mexico, USA. obizzozeralud.unm.edu

Myelin proteolipid protein (PLP) contains thioester-bound, long-chain fatty acids which are known to influence the structure of the molecule. To gain further insights into the role of this post-translational modification, we studied the effect that chemical deacylation of PLP had on the morphology of myelin and on the protein's ability to mediate the clustering of lipid vesicles. Incubation of rat optic nerves in isoosmotic solutions containing 100 mM hydroxylamine (HA) pH 7.4 led to deacylation of PLP and decompaction of myelin lamellae at the level of the intraperiod line. Incubation of nerves with milder nucleophilic agents (Tris and methylamine) or diluted HA, conditions that do not remove protein-bound fatty acids, caused no alterations in myelin structure. Other possible effects of HA which could have affected myelin compaction indirectly were ruled out. Incubation of optic nerves with 50 mM dithioerythritol (DTE) also led to the splitting of the myelin intraperiod line and this change again coincided with the removal of fatty acids. In addition, the apparently compacted CNS myelin in the PLP-less myelin-deficient rat, like that in tissue containing deacylated PLP, was readily decompacted upon incubation in isoosmotic buffers, suggesting that the function of PLP as a stabilizer of the interlamellar attachment is, at least in part, mediated by fatty acylation. Furthermore, in contrast to the native protein, PLP deacylated with either HA or DTE failed to induce the clustering of phosphatidylcholine/cholesterol vesicles in vitro. This phenomenon is not due to side-effects of the deacylation procedure since, upon partial repalmitoylation, the protein recovered most of its original vesicle-clustering activity. Collectively, these findings suggest that palmitoylation, by influencing the adhesive properties of PLP, is important for stabilizing the multilamellar structure of myelin.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11181833&dopt=Abstract

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