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Fatty acids resources:

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Int J Pharm. 1999 Mar 25;180(1):31-9.
Enzymatic degradation of SLN-effect of surfactant and surfactant mixtures.

Olbrich C, Muller RH.

Department of Pharmaceutics, Biopharmaceutics and Biotechnology, The Free University of Berlin, Kelchstr. 31, D-12169, Berlin, Germany.

Solid lipid nanoparticles (SLN) show different degradation velocities by the lipolytic enzyme pancreatic lipase as a function of their composition (lipid matrix, stabilizing surfactant). In combination with pancreatic colipase a degradation assay has been developed for studying the degradation behavior. As a measure to follow the degradation the formed free fatty acids have been analyzed using an enzymatic test. In the studies SLN degradation showed dependencies in relation to the length of the fatty acid chains in the triglycerides and the surfactants used for SLN production. The longer the fatty acid chains in the glycerides, the slower the degradation. The influence of surfactants can be degradation accelerating (e.g. cholic acid sodium salt) or a hindering, degradation slowing down effect due to steric stabilization (e.g. Poloxamer 407). As a second steric stabilizer, Tween 80 has been used and the results showed a less pronounced effect on hindering the degradation process than for Poloxamer 407. This result seems to be correlated to the number of ethyleneoxide chains in the molecule. The longer the ethyleneoxide chains are in the molecule, the more hindered is the anchoring of the lipase/colipase complex and consequently the degradation of the SLN. The result can be used to adjust degradation of SLN and consequently drug release in a controlled way.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10089289&dopt=Abstract

Biochem Biophys Res Commun. 1999 Feb 5;255(1):34-9.
Identification of caveolin-1 as a fatty acid binding protein.

Trigatti BL, Anderson RG, Gerber GE.

Department of Biochemistry, McMaster University, Hamilton, Ontario, L8N 3Z5, Canada.

In an attempt to identify high affinity, fatty acid binding proteins present in 3T3-L1 adipocytes plasma membranes, we labeled proteins in purified plasma membranes with the photoreactive fatty acid analogue, 11-m-diazirinophenoxy[11-3H]undecanoate. A single membrane protein of 22 kDa was covalently labeled after photolysis. This protein fractionated with caveolin-1 containing caveolae and was immunoprecipitated by an anti-caveolin-1 monoclonal antibody. Furthermore, 2D-PAGE analysis revealed that both the alpha and beta isoforms of caveolin-1 could be labeled by the photoreactive fatty acid upon photolysis, indicating that both bind fatty acids. The saturable binding of the photoreactive fatty acid suggests caveolin-1 has a lipid binding site that may either operate during intracellular lipid traffic or regulate caveolin-1 function. 1999 Academic Press.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10082651&dopt=Abstract

Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):3165-70.
Induced mutant mouse lines that express lipoprotein lipase in cardiac muscle, but not in skeletal muscle and adipose tissue, have normal plasma triglyceride and high-density lipoprotein-cholesterol levels.

Levak-Frank S, Hofmann W, Weinstock PH, Radner H, Sattler W, Breslow JL, Zechner R.

Spezialforschungsbereich Biomembrane Research Center, Karl-Franzens University, A-8010 Graz, Austria.

The tissue-specific expression of lipoprotein lipase (LPL) in adipose tissue (AT), skeletal muscle (SM), and cardiac muscle (CM) is rate-limiting for the uptake of triglyceride (TG)-derived free fatty acids and decisive in the regulation of energy balance and lipoprotein metabolism. To investigate the tissue-specific metabolic effects of LPL, three independent transgenic mouse lines were established that expressed a human LPL (hLPL) minigene predominantly in CM. Through cross-breeding with heterozygous LPL knockout mice, animals were generated that produced hLPL mRNA and enzyme activity in CM but lacked the enzyme in SM and AT because of the absence of the endogenous mouse LPL gene (L0-hLPL). LPL activity in CM and postheparin plasma of L0-hLPL mice was reduced by 34% and 60%, respectively, compared with control mice. This reduced LPL expression was sufficient to rescue LPL knockout mice from neonatal death. L0-hLPL animals developed normally with regard to body weight and body-mass composition. Plasma TG levels in L0-hLPL animals were increased up to 10-fold during the suckling period but normalized after weaning and decreased in adult animals. L0-hLPL mice had normal plasma high-density lipoprotein (HDL)-cholesterol levels, indicating that LPL expression in CM alone was sufficient to allow for normal HDL production. The absence of LPL in SM and AT did not cause detectable morphological or histopathological changes in these tissues. However, the lipid composition in AT and SM exhibited a marked decrease in polyunsaturated fatty acids. From this genetic model of LPL deficiency in SM and AT, it can be concluded that CM-specific LPL expression is a major determinant in the regulation of plasma TG and HDL-cholesterol levels.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10077655&dopt=Abstract

Xenobiotica. 2002 Dec;32(12):1079-91.
Binding of brominated diphenyl ethers to male rat carrier proteins.

Hakk H, Larsen G, Bergman A, Orn U.

US Department of Agriculture, Agricultural Research Service, Biosciences Research Laboratory, PO Box 5674-University Station, Fargo, ND 58105, USA. hakkargo.ars.usda.gov

1. Two [(14)C]-labelled brominated diphenyl ethers, 2,2',4,4',5-pentabromodiphenyl ether (BDE-99) and decabromodiphenyl ether (BDE-209), were separately administered to the male Sprague-Dawley rat as a single oral dose (2.2 mg kg(-1) body weight and 3.0 mg kg(-1), respectively). 2. Very low [(14)C] urine excretion was observed for both congeners (<1% of the dose), and cumulative biliary excretion was approximately 4% for BDE-99 and 9% for BDE-209. 3. More than 6% of the pooled urine from the BDE-99-treated rat was protein-bound to an 18-kDa protein characterized by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and Western immunoblot analysis as alpha(2u)-globulin. Eighteen per cent of the radioactivity from the pooled urine from the BDE-209 treated rat was bound to albumin; no binding to alpha(2u)-globulin was detected. 4. In bile, 27-39% of the radioactivity from the BDE-99-dosed rat was bound to an unidentified 79-kDa protein, whereas essentially all (>87%) of the biliary radioactivity from BDE-209 was bound to the 79-kDa protein. Both parent BDE-99 and-209 and their metabolites were detected by thin layer chromatography in the extracted fraction of this bile protein. 5. By differential centrifugation, the subcellular localization of the (14)C derived from each congener in selected tissues was quantified. The cytosolic [(14)C] from livers of the BDE-209-treated rat was bound to a 14-kDa protein, which was characterized as a fatty acid-binding protein.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12593757&dopt=Abstract

Like developmental biology of any part of our body, hair growth is a complicated process. Hence the homework for modern science to yet unravel the process and mechanism to a completion. There exist a number of traditional and alternative therapeutic methods that include drugs, surgery, suppelements, and even snake oils that have been developed and used for those who lose hair. No understanding, and there is no solution. Of course, none of these approaches are perfect for all hair loss problems, especially due to the heterogeneity of the causes underlying hair losses. Most of chemical drugs and hair transplantation surgeries are accompanied by undesirable side effects.

DHEA is a natural hormone, and it is produced in our body by the adrenal glands. DHEA has been suggested to provide numerous potential benefits. DHEA (or dehydroepiandrosterone) is converted into androgens (male hormones) or estrogens (female hormones) in the cells. Our bodies produce decreasing amount of DHEA as we get older. various health benefits: To deter aging, improve sexual function/erectile dysfunction, treat cognitive decline, enhance athletic performance, facilitate weight loss, improve strength, prevent osteoporosis, enhance immunomodulation for rheumatic conditions, and treat depression.

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