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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
Plant Physiol. 1994 Dec;106(4):1547-1553.
Release of Photosynthetic Protein Catabolites by Blebbing from Thylakoids.
Ghosh S, Hudak KA, Dumbroff EB, Thompson JE.
Department of Biology, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada (K.A.H., E.B.D., J.E.T.).
Thylakoid proteins and their catabolites have been detected in lipid-protein particles isolated from the stroma of intact chloroplasts obtained from primary leaves of 2-week-old bean seedlings (Phaseolus vulgaris L. cv Kinghorn). The lipid-protein particles bear morphological resemblance to plastoglobuli seen in the chloroplasts of senescing leaves, but they are much smaller. They range from 10 to 320 nm in radius, are uniformly stained in thin sections visualized by transmission electron microscopy, and are discernible in the stroma of chloroplasts in corresponding thin-sectioned leaf tissue. The lipid-protein particles contain thylakoid lipids and are enriched in free fatty acids. Specifically, the free-to-esterified fatty acid ratio is about 1:1 in the particles compared to only 1:18 for corresponding thylakoid membranes. Western blot analyses indicate that these particles also contain thylakoid proteins and, in some cases, catabolites of these proteins including the CF1 [beta] and [gamma] subunits of ATPase, cytochrome f, and the 31- and 33-kD proteins of PSII. Lipid-protein particles with similar properties were generated in vitro from isolated, light-stressed thylakoids. Collectively, these data suggest that blebbing of lipid-protein particles may be a means of removing potentially destabilizing macromolecular catabolites from thylakoid membrane bilayers.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12232430&dopt=Abstract [PubMed - as supplied by publisher]
Plant Physiol. 1994 Dec;106(4):1609-1614.
A Mutation at the fad8 Locus of Arabidopsis Identifies a Second Chloroplast [omega]-3 Desaturase.
McConn M, Hugly S, Browse J, Somerville C.
Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340 (M.M., J.B.).
Two independently isolated mutations at the fad7 locus in Arabidopsis produced plants with a temperature-conditional phenotype. Leaves of fad7 mutants grown at 28[deg]C contained less than 30% of wild-type levels of trienoic fatty acids (16:3 plus 18:3) compared with more than 70% of wild-type levels for plants grown at 15[deg]C. Screening of an M2 population derived from the fad7-1 line led to the identification of a line, SH1, in which the proportion of trienoic acids was much less than in fad7 plants. The segregation pattern of F2 progeny from a cross between SH1 and wild type indicated that the additional fatty acid mutation in SH1 is at a new locus, designated fad8. In a genetic background that was wild type at the FAD7 locus, the fad8 mutation had no detectable effect on overall leaf fatty acid composition irrespective of the temperature at which plants were grown. However, fatty acid analyses of individual leaf lipids revealed small decreases in the levels of 18:3 in two chloroplast lipids. In fad8 plants grown at 22[deg]C, phospha-tidylglycerol contained 22.5% 18:3 compared with 33.5% in wild-type Arabidopsis. For sulfoquinovosyldiacylglycerol, the values were 31.4 and 44.5%, respectively. Together with information from studies of the cloned FAD8 gene (S. Gibson, V. Arondel, K. Iba, C. Somerville [1994] Plant Physiol 106: 1615-1621), these results indicate that the FAD8 locus encodes a chloroplast-localized 16:2/18:2 desaturase that has a substrate specificity similar to the FAD7 gene product but that is induced by low temperature.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12232435&dopt=Abstract [PubMed - as supplied by publisher]
Curr Microbiol. 2002 Nov;45(5):340-5.
Amino acid deamination by ruminal Megasphaera elsdenii strains.
Rychlik JL, LaVera R, Russell JB.
Section of Microbiology, Wing Hall, Cornell University, Ithaca, NY 14853, USA.
When ruminal fluid from a cow fed timothy hay was serially diluted (10-fold increments into anaerobic broth containing 15 mg ml(-1) Trypticase), the low dilutions (< or =10(-6)) had optical densities greater than 2.0 and ammonia concentrations greater than 100 m M. The optical densities and ammonia concentrations of the 10(-8) and 10(-9) dilutions were very low, but large cocci were observed in the 10(-8) dilution. The large cocci were isolated and identified by 16S rDNA sequencing as Megasphaera elsdenii. The freshly isolated strain (JL1) grew well on Trypticase, but less than 4% of the amino acid nitrogen in Trypticase was converted to ammonia. Optical density and ammonia production were twice as great if Casamino acids were provided, and similar results were obtained with seven other strains (B159, AW106, YT91, LC1, T81, J1, and YZ70). Specific activities of deamination (based on Casamino acids) of the eight strains ranged from 100 (strain JL1) to 325 (strain B159) nmol mg protein(-1) min(-1). None of the strains could utilize branched-chain amino acids as an energy source for growth, but specific activities of branched-chain amino acid deamination ranged from 15 to 65 nmol mg protein(-1) min(-1). All eight of the M. elsdenii strains grew well in the presence of 5 micro M monensin, and only two of the strains were strongly inhibited by 20 micro M monensin. On the basis of these results, it appears that M. elsdenii is deficient in peptidase activity and can utilize only a few amino acids. Some M. elsdenii strains produced ammonia and branched-chain volatile fatty acids nearly as fast as obligate amino acid-fermenting ruminal bacteria, but the extent of this production was at least fourfold lower. Because all of the strains could tolerate 5 micro M monensin, it is unlikely that this feed additive would significantly inhibit M. elsdenii in vivo.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12232664&dopt=Abstract
Am J Physiol. 1999 Apr;276(4 Pt 1):E650-7.
Plasma leptin levels and triglyceride secretion rates in VMH-lesioned obese rats: a role of adiposity.
Suga A, Hirano T, Inoue S, Tsuji M, Osaka T, Namba Y, Miura M, Adachi M.
First Department of Internal Medicine, Showa University School of Medicine, Tokyo 142-8666, Japan.
To explore the role of adiposity on hypertriglyceridemia associated with obesity, we examined the relation between triglyceride secretion rate (TGSR) and plasma leptin, insulin, or insulin resistance in ventromedial hypothalamus (VMH)-lesioned rats in the dynamic and static phases (2 and 14 wk after lesions, respectively). VMH-lesioned rats gained body weight (BW) at fivefold higher rates in the dynamic phase compared with sham-operated control (sham) rats, and BW gain reached a plateau in the static phase. Parametrial fat pad mass was increased 2.5-fold in VMH-lesioned rats compared with sham rats in both phases. Leptin levels were sixfold higher in VMH-lesioned rats of the dynamic phase and even higher in the static phase. Insulin levels were twofold higher in VMH-lesioned rats than in sham rats in both phases. In the dynamic phase, VMH-lesioned rats had 2-fold higher plasma triglyceride (TG) levels and 2.6-fold higher TGSRs, whereas steady-state plasma glucose (SSPG) values, an indicator of insulin resistance, were lower. SSPG values became significantly higher in VMH-lesioned rats in the static phase, but TGSR was not further accelerated. TGSR was significantly associated with leptin, independent of insulin. Leptin was highly correlated with BW, fat mass, and nonesterified fatty acids (NEFA). These results suggest that adiposity itself plays a critical role in TGSR probably through increased NEFA flux from enlarged adipose tissues. Insulin resistance is not associated with the overproduction of TG in this animal model for obesity.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10198300&dopt=Abstract
The average human scalp is covered by approximatey 100,000 hair follicles. Each hair undergoes
hair cycle and normally 50-100 hairs randomly fall out a day, which is unnoticeable because lost hair is replaced by as many new hairs springing up daily. Hair loss results from the fall out of hair from the hair follicle. Alopecia or excessive, premature hair loss is the condition caused by many factors.
Loss of hair itself does not pose critical health problems because biological role of human hair is relatively marginal. Hair on our scalp protects the head from mechanical shock, heat loss, and exposure to UV-light. The eyelashes and eyebrowes protect the eyes, and hair in the ear canal or the nasal passages help filter out particles and pathogens, thus protecting our internal organs.
However, hair does play important social role: it is one of the major determinants of our appearance and identity in daily life. Fullness of hair also implicates or manifests physical integrity and youthfulness of the person. Losing hair could have more than just emotional impacts on individuals.
The hair is a unique organ that goes through a characteristic cycle consisting of an immature phase, a growing phase called anagen, a transitional phase between the growing phase and the resting phase called catagen, and finally a resting phase called telogen in which the hair stops growing, waiting to fall out. 85-90% of hairs on our body are in anagen phase or growing phase, which lasts anywhere from two to five years. This phase is followed by a short regression phase, or catagen, which lasts 2-3 weeks. Approximately 1% of hair follicles are in catagen. Approximately 10-15% of hair follicles are in the resting phase, the telogen, which lasts about 3-5 months. Hair follicles typically goes through 10-20 asynchronous cycles during the lifetime.
Persistent loss of more than 150 hairs would consist a state of hair loss, or alopecia, albeit it could be temporary.
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