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Relevant bibliographies by topics / Apolipoproteine saa

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Academic literature on the topic 'Apolipoproteine saa'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Apolipoproteine saa"

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Shephard, E. G., F. C. de Beer, M. C. de Beer, M. S. Jeenah, G. A. Coetzee, and D. R. van der Westhuyzen. "Neutrophil association and degradation of normal and acute-phase high-density lipoprotein 3." Biochemical Journal 248, no. 3 (December 15, 1987): 919–26. http://dx.doi.org/10.1042/bj2480919.

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The interaction of normal and acute-phase high-density lipoproteins of the subclass 3 (N-HDL3 and AP-HDL3) with human neutrophils and the accompanying degradation of HDL3 apolipoproteins have been studied in vitro. The chemical composition of normal and acute-phase HDL3 was similar except that serum amyloid A protein (apo-SAA) was a major apolipoprotein in AP-HDL3 (approx. 30% of total apolipoproteins). 125I-labelled AP-HDL3 was degraded 5-10 times faster than 125I-labelled N-HDL3 during incubation with neutrophils or neutrophil-conditioned medium. Apo-SAA, like apolipoprotein A-II (apo-A-II), was more susceptible than apolipoprotein A-I (apo-A-I) to the action of proteases released from the cells. The amounts of cell-associated AP-HDL3 apolipoproteins at saturation were up to 2.8 times greater than N-HDL3 apolipoproteins; while apo-A-I was the major cell-associated apolipoprotein when N-HDL3 was bound, apo-SAA constituted 80% of the apolipoproteins bound in the case of AP-HDL3. The associated intact apo-SAA was mostly surface-bound as it was accessible to the action of exogenous trypsin. alpha 1-Antitrypsin-resistant (alpha 1-AT-resistant) cellular degradation of AP-HDL3 apolipoproteins also occurred; experiments in which pulse-chase labelling was performed or lysosomotropic agents were used indicated that insignificant intracellular degradation occurred which points to the involvement of cell-surface proteases in this degradation.

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Nel, A. E., M. C. De Beer, E. G. Shephard, A. F. Strachan, M. L. Vandenplas, and F. C. De Beer. "Phosphorylation of human serum amyloid A protein by protein kinase C." Biochemical Journal 255, no. 1 (October 1, 1988): 29–34. http://dx.doi.org/10.1042/bj2550029.

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Monokine-induced hepatic secretion of serum amyloid A protein (apo-SAA), an acute-phase reactant, is followed by rapid association with high-density lipoprotein (HDL) in plasma. Plasma clearance of apo-SAA is more rapid than any of the other HDL apolipoproteins. It has been shown that, of the acute-phase HDL3 apolipoproteins, apo-SAA preferentially associates with neutrophil membranes. HDL apolipoproteins have been shown to activate protein kinase C in endothelial cells. We therefore investigated potential phosphorylation of HDL3 apolipoproteins by protein kinase C. Apo-SAA was the only apolipoprotein phosphorylated (Km = 12 mM). Phosphorylation of the apo-SAA-containing HDL3 particle was selective for the more basic isoforms of apo-SAA (pI 7.0, 7.4, 7.5 and 8.0), with more acidic isoforms being phosphorylated when delipidated acute-phase apolipoproteins were used as substrate. However, phosphorylation was not in itself responsible for the establishment of the apo-SAA isoforms.

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Lepedda, Antonio J., Gabriele Nieddu, Elisabetta Zinellu, Pierina De Muro, Franco Piredda, Anna Guarino, Rita Spirito, Franco Carta, Francesco Turrini, and Marilena Formato. "Proteomic Analysis of Plasma-Purified VLDL, LDL, and HDL Fractions from Atherosclerotic Patients Undergoing Carotid Endarterectomy: Identification of Serum Amyloid A as a Potential Marker." Oxidative Medicine and Cellular Longevity 2013 (2013): 1–11. http://dx.doi.org/10.1155/2013/385214.

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Apolipoproteins are very heterogeneous protein family, implicated in plasma lipoprotein structural stabilization, lipid metabolism, inflammation, or immunity. Obtaining detailed information on apolipoprotein composition and structure may contribute to elucidating lipoprotein roles in atherogenesis and to developing new therapeutic strategies for the treatment of lipoprotein-associated disorders. This study aimed at developing a comprehensive method for characterizing the apolipoprotein component of plasma VLDL, LDL, and HDL fractions from patients undergoing carotid endarterectomy, by means of two-dimensional electrophoresis (2-DE) coupled with Mass Spectrometry analysis, useful for identifying potential markers of plaque presence and vulnerability. The adopted method allowed obtaining reproducible 2-DE maps of exchangeable apolipoproteins from VLDL, LDL, and HDL. Twenty-three protein isoforms were identified by peptide mass fingerprinting analysis. Differential proteomic analysis allowed for identifying increased levels of acute-phase serum amyloid A protein (AP SAA) in all lipoprotein fractions, especially in LDL from atherosclerotic patients. Results have been confirmed by western blotting analysis on each lipoprotein fraction using apo AI levels for data normalization. The higher levels of AP SAA found in patients suggest a role of LDL as AP SAA carrier into the subendothelial space of artery wall, where AP SAA accumulates and may exert noxious effects.

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Djurec, Magdolna, Osvaldo Graña, Albert Lee, Kevin Troulé, Elisa Espinet, Lavinia Cabras, Carolina Navas, et al. "Saa3 is a key mediator of the protumorigenic properties of cancer-associated fibroblasts in pancreatic tumors." Proceedings of the National Academy of Sciences 115, no. 6 (January 19, 2018): E1147—E1156. http://dx.doi.org/10.1073/pnas.1717802115.

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Pancreatic ductal adenocarcinoma (PDAC) is characterized by the presence of abundant desmoplastic stroma primarily composed of cancer-associated fibroblasts (CAFs). It is generally accepted that CAFs stimulate tumor progression and might be implicated in drug resistance and immunosuppression. Here, we have compared the transcriptional profile of PDGFRα+ CAFs isolated from genetically engineered mouse PDAC tumors with that of normal pancreatic fibroblasts to identify genes potentially implicated in their protumorigenic properties. We report that the most differentially expressed gene, Saa3, a member of the serum amyloid A (SAA) apolipoprotein family, is a key mediator of the protumorigenic activity of PDGFRα+ CAFs. Whereas Saa3-competent CAFs stimulate the growth of tumor cells in an orthotopic model, Saa3-null CAFs inhibit tumor growth. Saa3 also plays a role in the cross talk between CAFs and tumor cells. Ablation of Saa3 in pancreatic tumor cells makes them insensitive to the inhibitory effect of Saa3-null CAFs. As a consequence, germline ablation of Saa3 does not prevent PDAC development in mice. The protumorigenic activity of Saa3 in CAFs is mediated by Mpp6, a member of the palmitoylated membrane protein subfamily of the peripheral membrane-associated guanylate kinases (MAGUK). Finally, we interrogated whether these observations could be translated to a human scenario. Indeed, SAA1, the ortholog of murine Saa3, is overexpressed in human CAFs. Moreover, high levels of SAA1 in the stromal component correlate with worse survival. These findings support the concept that selective inhibition of SAA1 in CAFs may provide potential therapeutic benefit to PDAC patients.

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Saïle, R., C. Delpierre, P. Puchois, G. Hocke, C. Cachera, J. C. Gesquiere, A. Steinmetz, A. Tartar, and J. C. Fruchart. "Enzyme-linked immunosorbent assay for serum amyloid A apolipoprotein with use of specific antibodies against synthetic peptides." Clinical Chemistry 34, no. 9 (September 1, 1988): 1767–71. http://dx.doi.org/10.1093/clinchem/34.9.1763.

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Abstract We describe a noncompetitive enzyme-linked immunosorbent assay for amyloid A apolipoprotein in human serum (apo SAA) in which specific antibodies against synthetic peptides are used. Microtiter plates were used as solid phase and coated with affinity-purified antibodies raised against SAA1-(95-104) peptide. After incubation with delipidated plasmas, the bound apo SAA was revealed by labeled antibodies raised against SAA1-(58-69) peptide. The assay offers several advantages over existing techniques: sensitivity, specificity, simplicity, and non-use of radioisotopes. Results correlate well with those by a nephelometric method in which polyclonal antibodies are used.

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Beach, C. M., M. C. De Beer, J. D. Sipe, L. D. Loose, and F. C. De Beer. "Human serum amyloid A protein. Complete amino acid sequence of a new variant." Biochemical Journal 282, no. 2 (March 1, 1992): 615–20. http://dx.doi.org/10.1042/bj2820615.

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Serum amyloid A protein (SAA), an acute-phase reactant and apolipoprotein of high-density lipoprotein, is a polymorphic protein with six reported isoforms. These are the products of three genes, i.e., cDNA pA1, cDNA pSAA82 and genomic DNA SAAg9, the last two being allelic variants at a single locus. We have identified an individual with additional novel SAA isoforms on isoelectric-focusing analysis. By using 3-bromo-3-methyl-2-(2′-nitrophenylsulphenyl)-indolenine (BNPS-skatole) cleavage of the protein at tryptophan residues we obtained the complete amino acid sequence of a novel isoform. Additional cleavage by endoproteinase Asp-N allowed verification of the tryptophan residues and complete amino acid sequence of both isoforms. The suitability of this approach to the rapid sequencing of SAA was demonstrated. Sequence analysis and quantification suggest that these isoforms are the result of the first confirmed allelic variation at the SAA1 locus. We designate the protein products of this allele SAA1 beta (pI 6.1) and SAA1 beta des-Arg (pI 5.6).

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Jayaraman, Shobini, Donald L. Gantz, Christian Haupt, and Olga Gursky. "Serum amyloid A forms stable oligomers that disrupt vesicles at lysosomal pH and contribute to the pathogenesis of reactive amyloidosis." Proceedings of the National Academy of Sciences 114, no. 32 (July 25, 2017): E6507—E6515. http://dx.doi.org/10.1073/pnas.1707120114.

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Serum amyloid A (SAA) is an acute-phase plasma protein that functions in innate immunity and lipid homeostasis. SAA is a protein precursor of reactive AA amyloidosis, the major complication of chronic inflammation and one of the most common human systemic amyloid diseases worldwide. Most circulating SAA is protected from proteolysis and misfolding by binding to plasma high-density lipoproteins. However, unbound soluble SAA is intrinsically disordered and is either rapidly degraded or forms amyloid in a lysosome-initiated process. Although acidic pH promotes amyloid fibril formation by this and many other proteins, the molecular underpinnings are unclear. We used an array of spectroscopic, biochemical, and structural methods to uncover that at pH 3.5–4.5, murine SAA1 forms stable soluble oligomers that are maximally folded at pH 4.3 with ∼35% α-helix and are unusually resistant to proteolysis. In solution, these oligomers neither readily convert into mature fibrils nor bind lipid surfaces via their amphipathic α-helices in a manner typical of apolipoproteins. Rather, these oligomers undergo an α-helix to β-sheet conversion catalyzed by lipid vesicles and disrupt these vesicles, suggesting a membranolytic potential. Our results provide an explanation for the lysosomal origin of AA amyloidosis. They suggest that high structural stability and resistance to proteolysis of SAA oligomers at pH 3.5–4.5 help them escape lysosomal degradation, promote SAA accumulation in lysosomes, and ultimately damage cellular membranes and liberate intracellular amyloid. We posit that these soluble prefibrillar oligomers provide a missing link in our understanding of the development of AA amyloidosis.

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Fleischer, Jacklyn G., Dan Rossignol, Gordon A. Francis, Teddy Chan, Melvyn Lynn, and Kishor M. Wasan. "Deactivation of the lipopolysaccharide antagonist eritoran (E5564) by high-density lipoprotein-associated apolipoproteins." Innate Immunity 18, no. 1 (March 7, 2011): 171–78. http://dx.doi.org/10.1177/1753425910394395.

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Lipid A, the active moiety of LPS, exerts its effects through interaction with TLR4, triggering a signalling cascade that results in the release of pro-inflammatory cytokines. Eritoran is a lipid A analogue that competes with LPS for binding to TLR4; however, after intravenous administration, it undergoes a time-dependent deactivation as a consequence of binding to high-density lipoproteins (HDLs). The site of eritoran association with HDL remains unknown. Therefore the aim of this study was to determine if HDL-associated apolipoproteins A1, A2, serum amyloid A (SAA) and C1, inhibit the ability of eritoran to block LPS-induced TNF-α release from whole blood. Eritoran activity after LPS stimulation in human whole blood was assessed in the presence of reconstituted HDL (rHDL) containing different apos. In rHDL, the major apolipoproteins in both the healthy and septic state, A1 and SAA, caused a significant reduction in eritoran antagonistic activity and had a greater effect than minor apolipoproteins A2 and C1. Apolipoproteins associated with HDL are likely to facilitate eritoran deactivation. Apolipoproteins A1 and SAA should be of particular focus as they are the major apos found on HDL in both the healthy and septic state. Further evaluation of the physical association between apolipoproteins and eritoran should be explored.

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Marsche, Gunther, Sǎsa Frank, John G. Raynes, Karen F. Kozarsky, Wolfgang Sattler, and Ernst Malle. "The lipidation status of acute-phase protein serum amyloid A determines cholesterol mobilization via scavenger receptor class B, type I." Biochemical Journal 402, no. 1 (January 25, 2007): 117–24. http://dx.doi.org/10.1042/bj20061406.

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During the acute-phase reaction, SAA (serum amyloid A) replaces apoA-I (apolipoprotein A-I) as the major HDL (high-density lipoprotein)-associated apolipoprotein. A remarkable portion of SAA exists in a lipid-free/lipid-poor form and promotes ABCA1 (ATP-binding cassette transporter A1)-dependent cellular cholesterol efflux. In contrast with lipid-free apoA-I and apoE, lipid-free SAA was recently reported to mobilize SR-BI (scavenger receptor class B, type I)-dependent cellular cholesterol efflux [Van der Westhuyzen, Cai, de Beer and de Beer (2005) J. Biol. Chem. 280, 35890–35895]. This unique property could strongly affect cellular cholesterol mobilization during inflammation. However, in the present study, we show that overexpression of SR-BI in HEK-293 cells (human embryonic kidney cells) (devoid of ABCA1) failed to mobilize cholesterol to lipid-free or lipid-poor SAA. Only reconstituted vesicles containing phospholipids and SAA promoted SR-BI-mediated cholesterol efflux. Cholesterol efflux from HEK-293 and HEK-293[SR-BI] cells to lipid-free and lipid-poor SAA was minimal, while efficient efflux was observed from fibroblasts and CHO cells (Chinese-hamster ovary cells) both expressing functional ABCA1. Overexpression of SR-BI in CHO cells strongly attenuated cholesterol efflux to lipid-free SAA even in the presence of an SR-BI-blocking IgG. This implies that SR-BI attenuates ABCA1-mediated cholesterol efflux in a way that is not dependent on SR-BI-mediated re-uptake of cholesterol. The present in vitro experiments demonstrate that the lipidation status of SAA is a critical factor governing cholesterol acceptor properties of this amphipathic apolipoprotein. In addition, we demonstrate that SAA mediates cellular cholesterol efflux via the ABCA1 and/or SR-BI pathway in a similar way to apoA-I.

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SCHREIBER, Barbara M., Mara VEVERBRANTS, Richard E. FINE, Jan K. BLUSZTAJN, Mario SALMONA, Apurva PATEL, and Jean D. SIPE. "Apolipoprotein serum amyloid A down-regulates smooth-muscle cell lipid biosynthesis." Biochemical Journal 344, no. 1 (November 8, 1999): 7–13. http://dx.doi.org/10.1042/bj3440007.

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The addition of acute-phase apolipoprotein serum amyloid A (SAA) to cultured aortic smooth-muscle cells caused a decrease in the incorporation of [14C]acetate into lipids. Optimal inhibition of lipid biosynthesis was achieved with 2 μM SAA, and the effect was maintained for up to 1 week when SAA was included in the culture medium. Lipid extracts were subjected to TLC and it was determined that the SAA-induced decrease in [14C]acetate incorporation into lipids was attributable to decreases in cholesterol, phospholipid and triglyceride levels. The accumulated mass of cholesterol and phospholipid in SAA-treated cultures was significantly less than that of controls, with no change in the accumulated protein. Moreover, SAA had no effect on either protein synthesis or DNA synthesis, suggesting that SAA specifically alters lipid synthesis. By using a peptide corresponding to the cholesterol-binding domain of acute-phase SAA (amino acids 1-18), it was shown that this region of the molecule was as effective as the full-length protein in decreasing lipid synthesis and the accumulation of cholesterol and phospholipid. The implications of these findings for atherosclerosis and Alzheimer's disease are discussed.

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Dissertations / Theses on the topic "Apolipoproteine saa"

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SAILE, RACHID. "L'apolipoproteine serique amyloide a : methodologie de dosage utilisant des peptides synthetiques, applications cliniques." Lille 2, 1989. http://www.theses.fr/1989LIL2P252.

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Book chapters on the topic "Apolipoproteine saa"

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Malmendier, C. L., and J.-F. Lontie. "Protein S and SAA: Genetics, Structure and Metabolism are they Apolipoproteins and Identical." In Advances in Experimental Medicine and Biology, 203–12. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-0733-4_25.

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Chehade, JOE M., Rosalyn Alcade, Emad Naem, Senan Sultan, Abdul-Razzak Alamir, Michael J. Haas, Norman C. Wong, and Arshag D. Mooradian. "Induction of Apolipoprotein A-I Gene Expression by Glucagon-Like Peptide-1 and Exendin-4." In The Endocrine Society's 92nd Annual Meeting, June 19–22, 2010 - San Diego, OR06–5—OR06–5. Endocrine Society, 2010. http://dx.doi.org/10.1210/endo-meetings.2010.part1.or.or06-5.

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Stanhope, KL, AA Bremer, NL Keim, GX Chen, T. Fong, VI Lee, RI Menorca, K. Nakajima, and PJ Havel. "Consuming Fructose-, or HFCS-, but Not Glucose-Sweetened Beverages for 2 Weeks Increases Nighttime Triglyceride and Fasting LDL and Apolipoprotein-B (apoB) Concentrations in Young Men and Women." In The Endocrine Society's 92nd Annual Meeting, June 19–22, 2010 - San Diego, OR06–3—OR06–3. Endocrine Society, 2010. http://dx.doi.org/10.1210/endo-meetings.2010.part1.or.or06-3.

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Conference papers on the topic "Apolipoproteine saa"

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Shin, Esther, Kent E. Pinkerton, Christel TeeSy, and Niharika Gupta. "Cardiopulmonary Changes Of Apolipoprotein (Apo/E) Deficient Mice With Inhalation Of Nano Fe2O3/Soot Particles." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1195.

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Umar, Soban, Rangarajan D. Nadadur, Kaveh Navab, Greg Hough, David Ross, Alan Fogelman, Mohamad Navab, and Mansoureh Eghbali. "Apolipoprotein-A1 Mimetic Peptide 4F Rescues Pre-Existing Severe Pulmonary Hypertension And Right Ventricular Dysfunction." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1249.

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Iorga, Andrea, Rod Partow-Navid, Soban Umar, Marjan Amjedi, and Mansoureh Eghbali. "Exogenous Estrogen Therapy Of Aging Female Apolipoprotein E-Deficient Mice Rescues Pulmonary Hypertension And Right Ventricular Dysfunction." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1240.

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Chung, Eunjoo, Jason Horton, Ayla White, Bradly Scroggins, Kathryn Hudak, and Deborah Citrin. "Abstract 852: Enhanced expression of secretory clusterin/apolipoprotein J (sCLU) in pulmonary alveolar stem cells after ionizing radiation exposure." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-852.

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Anjum, Fatima, Jason Lazar, and Raj Wadgaonkar. "Identification Of Altered Patterns Of Ubiquitin-Proteasome Pathway And Apolipoprotein A In Sickle Cell Disease Related Pulmonary Arterial Hypertension." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1892.

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Elbahrawy, Ali I., Abdelmetalab Tarhuni, Amarjit S. Naura, Youssef Errami, Mohamed Alwan, Samar Hammad, Jimena Trillo-Tinoco, et al. "Abstract LB-3: Apolipoprotein (E) is a determinant of colon carcinogenesis potentially by regulating inflammation and β-catenin independently of its role in lipid metabolism." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-lb-3.

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Burkart, Kristin M., Ani Manichaikul, Gregory L. Burke, Eric A. Hoffman, Joel D. Kaufman, Jerome I. Rotter, Michael Tsai, Karol E. Watson, Stephen S. Rich, and R. G. Barr. "Single Nucleotide Polymorphisms In The Apolipoprotein M Gene Are Associated With Percent Emphysema, HDL And HDL Subfractions Among European- And African-Americans: The MESA Lung And SNP Health Association Resource (SHARe) Studies." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a3809.

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