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Relevant bibliographies by topics / Human Liver Fatty Acid Binding Protein

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Academic literature on the topic 'Human Liver Fatty Acid Binding Protein'

Author: Grafiati

Published: 11 March 2023

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Journal articles on the topic "Human Liver Fatty Acid Binding Protein"

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Sharma, Ashwani, and Amit Sharma. "Fatty Acid Induced Remodeling within the Human Liver Fatty Acid-binding Protein." Journal of Biological Chemistry 286, no. 36 (July 8, 2011): 31924–28. http://dx.doi.org/10.1074/jbc.m111.270165.

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Cai, Jun, Christian Lücker, Zhongjing Chen, Elena Klimtchuk, Ye Qiao, and James A. Hamilton. "Human Liver Fatty Acid Binding Protein: Solution Structure and Ligand Binding." Biophysical Journal 96, no. 3 (February 2009): 600a. http://dx.doi.org/10.1016/j.bpj.2008.12.3140.

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Sheng, Nan, Juan Li, Hui Liu, Aiqian Zhang, and Jiayin Dai. "Interaction of perfluoroalkyl acids with human liver fatty acid-binding protein." Archives of Toxicology 90, no. 1 (November 5, 2014): 217–27. http://dx.doi.org/10.1007/s00204-014-1391-7.

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Cai, Jun, Christian Lücke, Zhongjing Chen, Ye Qiao, Elena Klimtchuk, and James A. Hamilton. "Solution Structure and Backbone Dynamics of Human Liver Fatty Acid Binding Protein: Fatty Acid Binding Revisited." Biophysical Journal 102, no. 11 (June 2012): 2585–94. http://dx.doi.org/10.1016/j.bpj.2012.04.039.

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Thumser, A. E., J. E. Voysey, and D. C. Wilton. "The binding of lysophospholipids to rat liver fatty acid-binding protein and albumin." Biochemical Journal 301, no. 3 (August 1, 1994): 801–6. http://dx.doi.org/10.1042/bj3010801.

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The binding of lysophospholipids to rat liver fatty acid-binding protein (FABP) and to BSA and human serum albumin was investigated by using competitive displacement fluorescence assays by monitoring the displacement of the fluorescent fatty acid probe 11-(dansylamino)undecanoic acid (DAUDA). In addition, direct binding assays using changes in tryptophan fluorescence were possible with albumin. Liver FABP was able to bind a range of lysophospholipids, oleoyl-lysophosphatidic acid (lysoPA), oleoyl-lysophosphatidylcholine (lysoPC), oleoyl-lysophosphatidylethanolamine (lysoPE) and oleoyl-lysophosphatidylglycerol, with similar affinity and a Kd of about 1 microM. Liver FABP was also able to bind lysophospholipids generated by the action of phospholipase A2 or phospholipase A1 (triacylglycerol lipase) on phospholipid vesicles. A possible physiological role for liver FABP in lysophospholipid metabolism within the cell is discussed. Albumin was shown to bind lysoPA with higher affinity than either lysoPC or lysoPE, and the initial minimal DAUDA displacement by lysoPA indicated that lysoPA was binding to the primary high-affinity fatty acid-binding sites on albumin and that, like oleic acid, about 3 mol of ligand/mol was bound to these sites. Kd values in the microM range were indicated for lysoPC and lysoPE, whereas, by comparison with oleic acid, the Kd for lysoPA was significantly lower and high-affinity binding in the nM range was indicated. Overall, the data suggest that, because of structural similarity, lysoPA binds to albumin in a similar manner to long-chain fatty acids.

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Favretto, Filippo, Carlo Santambrogio, Mariapina D'Onofrio, Henriette Molinari, Rita Grandori, and Michael Assfalg. "Bile salt recognition by human liver fatty acid binding protein." FEBS Journal 282, no. 7 (February 18, 2015): 1271–88. http://dx.doi.org/10.1111/febs.13218.

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Pietro, Santiago M. Di, and José A. Santomé. "Presence of two new fatty acid binding proteins in catfish liver." Biochemistry and Cell Biology 74, no. 5 (September 1, 1996): 675–80. http://dx.doi.org/10.1139/o96-073.

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A basic fatty acid binding protein (FABP), closely related to that of chicken liver, was isolated and characterized from catfish (Rhamdia sapo) liver in a previous work. Results herein show the presence of another two FABPs in which partial amino acid sequences reveal great similarity with the corresponding sequences of other already known FABPs belonging to the heart type. The purification procedures for both proteins involve gel filtration, anion-exchange chromatography, and sodium dodecyl sulfate – polyacrylamide gel electrophoresis (as a last step). Because both FABP N-termini were blocked, they were submitted to in-gel tryptic digestion and the resulting peptides were separated by high performance liquid chromatography, and sequenced by Edman degradation. One of these proteins presented the highest identity percentage when compared with those of the human and bovine heart and bovine brain (81%), and the other when compared with those of chicken retina (75%) and mouse and bovine heart FABP (70%). The presence of several FABPs plus the fact that they belong to different types, as found in the Rhamdia sapo liver, is unusual in mammals, which express a characteristic liver-type member of this protein family.Key words: fatty acid binding protein, liver, catfish, Rhamdia sapo.

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González, Javier M., and S. Zoë Fisher. "Structural analysis of ibuprofen binding to human adipocyte fatty-acid binding protein (FABP4)." Acta Crystallographica Section F Structural Biology Communications 71, no. 2 (January 28, 2015): 163–70. http://dx.doi.org/10.1107/s2053230x14027897.

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Inhibition of human adipocyte fatty-acid binding protein (FABP4) has been proposed as a treatment for type 2 diabetes, fatty liver disease and atherosclerosis. However, FABP4 displays a naturally low selectivity towards hydrophobic ligands, leading to the possibility of side effects arising from cross-inhibition of other FABP isoforms. In a search for structural determinants of ligand-binding selectivity, the binding of FABP4 towards a group of small molecules structurally related to the nonsteroidal anti-inflammatory drug ibuprofen was analyzed through X-ray crystallography. Several specific hydrophobic interactions are shown to enhance the binding affinities of these compounds, whereas an aromatic edge-to-face interaction is proposed to determine the conformation of bound ligands, highlighting the importance of aromatic interactions in hydrophobic environments.

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Velkov, Tony. "Interactions between Human Liver Fatty Acid Binding Protein and Peroxisome Proliferator Activated Receptor Selective Drugs." PPAR Research 2013 (2013): 1–14. http://dx.doi.org/10.1155/2013/938401.

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Fatty acid binding proteins (FABPs) act as intracellular shuttles for fatty acids as well as lipophilic xenobiotics to the nucleus, where these ligands are released to a group of nuclear receptors called the peroxisome proliferator activated receptors (PPARs). PPAR mediated gene activation is ultimately involved in maintenance of cellular homeostasis through the transcriptional regulation of metabolic enzymes and transporters that target the activating ligand. Here we show that liver- (L-) FABP displays a high binding affinity for PPAR subtype selective drugs. NMR chemical shift perturbation mapping and proteolytic protection experiments show that the binding of the PPAR subtype selective drugs produces conformational changes that stabilize the portal region of L-FABP. NMR chemical shift perturbation studies also revealed that L-FABP can form a complex with the PPAR ligand binding domain (LBD) of PPARα. This protein-protein interaction may represent a mechanism for facilitating the activation of PPAR transcriptional activity via the direct channeling of ligands between the binding pocket of L-FABP and the PPARαLBD. The role of L-FABP in the delivery of ligands directly to PPARαvia this channeling mechanism has important implications for regulatory pathways that mediate xenobiotic responses and host protection in tissues such as the small intestine and the liver where L-FABP is highly expressed.

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Cai, Jun, Christian Lücke, Ye Qiao, Elena Klimtchuk, and James A. Hamilton. "Solution Structure and Backbone Dynamics of Human Liver Fatty Acid Binding Protein." Biophysical Journal 98, no. 3 (January 2010): 238a. http://dx.doi.org/10.1016/j.bpj.2009.12.1288.

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Dissertations / Theses on the topic "Human Liver Fatty Acid Binding Protein"

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Evans, Carol. "Studies on rat liver fatty acid-binding protein." Thesis, University of Southampton, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.385122.

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Hagan, Robert Mark. "Liver fatty acid binding protein : relating structure to function." Thesis, University of Southampton, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.437109.

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Wilkinson, T. C. I. "A study of the fatty acid-binding protein of rat liver." Thesis, University of Southampton, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.374448.

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Wong, Yue-ling, and 黃愉鈴. "The role of adipocyte fatty acid binding protein in the pathogenesis of non-alcoholic fatty liver disease." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2010. http://hub.hku.hk/bib/B45164873.

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Chan, Cangel Pui Yee. "A superior early myocardial infarction marker : human heart-type fatty acid-binding protein /." View Abstract or Full-Text, 2002. http://library.ust.hk/cgi/db/thesis.pl?CHEM%202002%20CHAN.

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Thesis (Ph. D.)--Hong Kong University of Science and Technology, 2002.
Includes bibliographical references (leaves 139-166). Also available in electronic version. Access restricted to campus users.

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Iwen, Alexander. "Molecular mechanisms of action of thyroid hormone the liver fatty acid binding protein as a model /." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972186670.

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Davies, Joanna Kay. "Rat liver fatty acid binding protein structure and function : the targeting of FABP-bound ligands to anionic interfaces." Thesis, University of Southampton, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.393911.

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Gutiérrez, González Luis Horacio. "Structural and dynamical studies on human epidermal-type fatty acid binding protein using high resolution NMR spectroscopy." [S.l.] : [s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=964395630.

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Spann, Nathanael J. "Transcriptional modulation of hepatic lipoprotein assembly and secretion coordinate regulation of the liver-fatty acid binding protein and microsomal triglyceride transfer protein genes /." Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2006. http://wwwlib.umi.com/cr/ucsd/fullcit?p3215280.

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Thesis (Ph. D.)--University of California, San Diego and San Diego State University, 2006.
Title from first page of PDF file (viewed July 21, 2006). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 123-155).

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Jakobsson, Emma. "Structural Studies of Echinococcus granulosus Fatty-acid-binding Protein 1 and Human Semicarbazide-sensitive Amine Oxidase." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis: Univ.-bibl. [distributör], 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-5884.

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Books on the topic "Human Liver Fatty Acid Binding Protein"

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Dworatzek, Paula Darlene Nesbitt. Cross sectional and postprandial phenotypes of human subjects with the T54 variant of fatty acid-binding protein 2 (FABP2) gene and the effect of different fat sources. 2004.

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Book chapters on the topic "Human Liver Fatty Acid Binding Protein"

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Vergani, Lodovica, Marina Fanin, Andrea Martinuzzi, Andrea Galassi, Andrea Appi, Rosalba Carrozzo, Maurizio Rosa, and Corrado Angelini. "Liver fatty acid-binding protein in two cases of human lipid storage." In Cellular Fatty Acid-binding Proteins, 225–30. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-3936-0_28.

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Storch, Judith, Jacques H. Veerkamp, and Kuo-Tung Hsu. "Similar mechanisms of fatty acid transfer from human anal rodent fatty acid-binding proteins to membranes: Liver, intestine, heart muscle, and adipose tissue FABPs." In Cellular Lipid Binding Proteins, 25–33. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4419-9270-3_4.

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Kaikaus, Raja M., William K. Chan, Paul R. Ortiz de Montellano, and Nathan M. Bass. "Mechanisms of regulation of liver fatty acid-binding protein." In Cellular Fatty Acid-Binding Proteins II, 93–100. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-3096-1_12.

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Scapin, Giovanna, Paola Spadon, Mario Mammi, Giuseppe Zanotti, and Hugo L. Monaco. "Crystal structure of chicken liver basic fatty acid-binding protein at 2.7 Å resolution." In Cellular Fatty Acid-binding Proteins, 95–99. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-3936-0_12.

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Iseki, Shoichi, Hisatake Kondo, Masahiro Hitomi, and Teruo Ono. "Localization of liver fatty acid-binding protein and its mRNA in the liver and jejunum of rats: an immunohistochemical and in situ hybridization study." In Cellular Fatty Acid-binding Proteins, 27–33. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-3936-0_4.

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Börchers, Torsten, Peter Højrup, Søren U. Nielsen, Peter Roepstorff, Friedrich Spener, and Jens Knudsen. "Revision of the amino acid sequence of human heart fatty acid-binding protein." In Cellular Fatty Acid-binding Proteins, 127–33. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-3936-0_16.

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Bass, Nathan M. "Fatty acid-binding protein expression in the liver: its regulation and relationship to the zonation of fatty acid metabolism." In Cellular Fatty Acid-binding Proteins, 167–76. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-3936-0_21.

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Nielsen, Søren U., Anders O. Pedersen, Henrik Vorum, and Rolf Brodersen. "Fatty acid-binding protein from human heart localized in native and denaturing two-dimensional gels." In Cellular Fatty Acid-binding Proteins, 119–25. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-3936-0_15.

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Kleine, Appie H., Jan F. C. Glatz, Frans A. van Nieuwenhoven, Monique I. J. Vallinga, Martin H. L. Salden, Fré T. Bosman, Wim J. A. Boersma, Netty D. Zegers, and Ger J. van der Vusse. "Type-specific immunodetection of human heart fatty acid-binding protein with polyclonal anti-peptide antibodies." In Cellular Fatty Acid-binding Proteins, 41–48. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-3936-0_6.

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Evans, Carol, and David C. Wilton. "The chemical modification of cysteine-69 of rat liver fatty acid-binding protein (FABP): a fluorescence approach to FABP structure and function." In Cellular Fatty Acid-binding Proteins, 135–40. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-3936-0_17.

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Conference papers on the topic "Human Liver Fatty Acid Binding Protein"

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Zelencova-Gopejenko, Diana, Rimants Metlans, and Kristaps Jaudzems. "Insights into binding specificity of human heart-type fatty-acid binding protein." In 7th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/ecmc2021-11480.

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Sanati, A., R. Siavash Moakhar, K. Raeissi, F. Karimzadeh, H. Vali, and S. Mahshid. "Detection of heart-fatty acid binding protein in human serum using gold nano/micro-islands and molecularly imprinted polymers." In 2021 IEEE 21st International Conference on Nanotechnology (NANO). IEEE, 2021. http://dx.doi.org/10.1109/nano51122.2021.9514337.

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Sumi, Y., Y. Nakamura, M. Sakai, M. Muramatsu, and N. Aoki. "STRUCTURE OF HUMAN α2-PLASMIN INHIBITOR DEDUCED FROM THAT OF cDNA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644371.

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The complete amino acid sequence of α2-plasmin inhibitor (α2PI) was determined by cDNA cloning. A Agt 10 cDNA library was prepared from poly(A)+mRNA isolated from cultured human liver cells. The labeled oligonucleotides, corresponding to the reported partial amino acid sequences of α2PI, were used as probes to screen the library. One of the positive clones was subcloned into plasmid pUC8. A 2.2 kilobase cDNA clone thus isolated contains a region coding for a portion of a leader sequence, the mature protein, a stop codon (TGA), a 3' noncoding region (733 nucleotides), and a poly(A)tail (37 nucleotides). The amino acid sequence deduced from the cDNA is composed of 452 amino acids starting with an amino-terminal sequence of Asn-Gln-Glu-Gln and ending with a carboxyl-terminal sequence of Gly-Ser-Pro-Lys. The sequence shows approximately 30% homology with those of other plasma serine protease inhibitors. However, α2PI extends 50-52 amino acids beyond the carboxyl-terminal ends of the other inhibitors. This 50-52 carboxyl-terminal amino acid sequence is therefore specific to α2PI, and contains the sequence that is exactly the same as that of the peptide containing the plasminogen binding site. There are three lysine residues possibly involved in the binding to plasminogen in this region. From the homology with the other inhibitors, the inhibitor's reactive-site peptide bond was suggested to be Met-Ser and the same as that of ai-antitrypsin. The Met residue is located at the 362 position from the amino-terminal end.

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Broekman, M. J. "METABOLISM OF ARACHIDONATE RELEASED FROM THROMBIN-STIMULATED PLATELETS TO THROMBOXANE, 12-HYDROXYHEPTADECATRIENATE AND 12-HYDROXYEICOSATETRAENATE IS REGULATED BY ALBUMIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644623.

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Stimulation with high-dose thrombin of human platelets leads to release of arachidonate from phosphatidylethanolamine and phosphatidylcholine via a phosholipase A2 mechanism. Released arachidonate is subsequently reincorporated into cellular lipid, or oxygenated by cyclooxygenase or lipoxygenase of the cell which originally released the arachidonate, or of another cell in the local environment. Albumin is the major fatty acid-binding protein in plasma, where it is present at 600 uM. In addition, albumin binds and stabilizes labile eicosanoid intermediates. Albumin could therefore profoundly influence the pattern and time course of eicosanoid formation. The effects of added albumin (fatty acid-free) on accumulation of free arachidonate, measured by GLC, formation of 12-hydroxyhepta-decatrienoate (12HHT) and 12-hydroxyeicosatetraenoate (12HETE), measured by HPLC, were studied in washed platelets stimulated with thrombin (15 U/5×109 cells). Addition of 150 uM albumin increased free arachidonate accumulation from 3-5 nmol to 44 nmol 300 s following thrombin stimulation. In the presence of 150 uM albumin, aspirin-pretreatment did not further increase free arachidonate accumulation. Albumin dose-dependently inhibited arachidonate cyclooxygenation: 150 uM albumin reduced 12HHT formation by >55%, but arachidonate lipoxygenation (12HETE production) decreased by only 26%. Aspirin-treated platelets, in the absence of albumin, produced more than double the quantity of 12HETE of untreated platelets. Addition of 15 uM albumin to aspirin-treated platelets increased 12HETE production slightly, but higher levels of albumin (150 uM) led to a 60% decrease in 12HETE formation. This decrease was similar to the decrease in 12HHT induced by albumin in aspirin-free platelets. Albumin also increased the lag in onset of 12HETE formation caused by aspirin. These data demonstrate that eicosanoid production by thrombin-stimulated platelets is greatly down-regulated by comparatively very small quantities of albumin due to sequestration of released arachidonate.

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