Host Species:	Rabbit
Concentration:	1 mg/ml (OD 1.35 / 280 nm)
Antigen:	MDA-KLH
Purification:	Affinity purified
Buffer:	75 mM Sodium Phosphate, 75 mM NaCl, 0.5 mM EDTA, 0.02% NaN3, pH 7.2
Specificity	Specifically binds to MDA-LDL and other MDA modified proteins. Dilution for immunoblot and ELISA range: 1,000 to 20,000. (A slight amount of precipitation may have occurred during storage due to the natural properties of these antibodies; please centrifuge before use.)
Use:	The antibody can be used for detection of MDA in plasma, lipoproteins and other MDA modified proteins, immunoassays, immunoblots, enzyme conjugation, or biotinylation.
Storage:	-20°C for long-term storage, 4°C for short- term storage. Aliquot to avoid repeated freezing and thawing.

 

*These products are for research or manufacturing use only, not for use in human therapeutic or diagnostic applications.

Importance

Oxidative damage includes oxidative modification of cellular macromolecules, induction of cell death by apoptosis or necrosis, as well as structural tissue damage. Of the many biological targets of oxidative stress, lipids are the most involved class of biomolecules. Lipid oxidation gives rise to a number of secondary products of polyunsaturated fatty acid peroxidation. Malondialdehyde (MDA) is the principal and most studied product. Consistent evidence reveals the reaction between MDA and cellular macromolecules such as proteins, RNA and DNA (Valenzuela, 1991).

Numerous experiments have shown that MDA readily modifies proteins (Nair, 1986). MDA reacts with DNA to form adducts to deoxyguanosine and deoxyadenosine which may be mutagenic and these can be quantified in several human tissues (Marnett, 1999).This aldehyde is a highly toxic molecule and should be considered as a marker of lipid peroxidation. The interaction with DNA and proteins has often been referred to as potentially mutagenic and atherogenic (Rio et al., 2005).

L.J. Marnett, Lipid peroxidation‐DNA damage by malondialdehyde, Mutat Res, 424 (1999), pp. 83–95

V. Nair, C.S. Cooper, D.E. Vietti, G.A. Turner, The chemistry of lipid peroxidation metabolites: crosslinking reactions of malondialdehyde, Lipids, 21 (1986), pp. 6–10

Rio, Daniele Del, Amanda J. Stewart, and Nicoletta Pellegrini. "A Review of Recent Studies on Malondialdehyde as Toxic Molecule and Biological Marker of Oxidative Stress." Nutrition, Metabolism and Cardiovascular Diseases 15.4 (2005): 316-28.

A. Valenzuela, The biological significance of malondialdehyde determination in the assessment of tissue oxidative stress, Life Sci, 48 (1991), pp. 301–309

 

Citations

[A16][A17]	2020	Busquets, Sílvia; Pérez-Peiró, Maria; Salazar-Degracia, Anna; Argilés, Josep M.; Serpe, Roberto; Rojano-Toimil, Alba et al. (2020): Differential structural features in soleus and gastrocnemius of carnitine-treated cancer cachectic rats. Journal of Cellular Physiology 235 (1), pp. 526–537. DOI: 10.1002/jcp.28992.
[A16][A17]	2019	Himori, Koichi; Tatebayashi, Daisuke; Ashida, Yuki; Yamada, Takashi (2019): Eccentric training enhances the αB-crystallin binding to the myofibrils and prevents skeletal muscle weakness in adjuvant-induced arthritis rat. Journal of Applied Physiology 127 (1), pp. 71–80. DOI: 10.1152/japplphysiol.00102.2019.
[A16][A17]	2019	Oniki, Takahiro; Teshima, Yasushi; Nishio, Satoru; Ishii, Yumi; Kira, Shintaro; Abe, Ichitaro et al. (2019): Hyponatraemia aggravates cardiac susceptibility to ischaemia/reperfusion injury. International Journal of Experimental Pathology 100 (5-6), pp. 350–358. DOI: 10.1111/iep.12338.
[A16][A17]	2019	Rahman, Mizanur; Steuer, Johnny; Gillgren, Peter; Végvári, Ákos; Liu, Anquan; Frostegård, Johan (2019): Malondialdehyde Conjugated With Albumin Induces Pro-Inflammatory Activation of T Cells Isolated From Human Atherosclerotic Plaques Both Directly and Via Dendritic Cell-Mediated Mechanism. JACC. Basic to Translational Science 4 (4), pp. 480–494. DOI: 10.1016/j.jacbts.2019.03.009.
[A16][A17]	2019	Barreiro, Esther; Salazar‐Degracia, Anna; Sancho‐Muñoz, Antonio; Gea, Joaquim (2019): Endoplasmic reticulum stress and unfolded protein response profile in quadriceps of sarcopenic patients with respiratory diseases. In Journal of cellular physiology 234 (7), pp. 11315–11329. DOI: 10.1002/jcp.27789.
[A16][A17]	2018	Barreiro, Esther; Puig-Vilanova, Ester; Salazar-Degracia, Anna; Pascual-Guardia, Sergi; Casadevall, Carme; Gea, Joaquim (2018): The phosphodiesterase-4 inhibitor roflumilast reverts proteolysis in skeletal muscle cells of patients with COPD cachexia. In Journal of Applied Physiology 125 (2), pp. 287–303. DOI: 10.1152/japplphysiol.00798.2017.
[A16][A17]	2018	Yamada, Ryotaro; Himori, Koichi; Tatebayashi, Daisuke; Ashida, Yuki; Ikezaki, Kazumi; Miyata, Hirohumi et al. (2018): Preconditioning contractions prevent the delayed onset of myofibrillar dysfunction after damaging eccentric contractions. In J Physiol 596 (18), pp. 4427–4442. DOI: 10.1113/JP276026.
[A16][A17]	2017	Salazar-Degracia, Anna; Busquets, Sílvia; Argilés, Josep M.; López-Soriano, Francisco J.; Barreiro, Esther (2017): Formoterol attenuates increased oxidative stress and myosin protein loss in respiratory and limb muscles of cancer cachectic rats. In PeerJ 5 (Suppl 1), e4109. DOI: 10.7717/peerj.4109.
[A16][A17]	2016	Salazar-Degracia, Anna; Blanco, David; Vilà-Ubach, Mònica; Biurrun, Gabriel de; Solórzano, Carlos Ortiz de; Montuenga, Luis M.; Barreiro, Esther (2016): Phenotypic and metabolic features of mouse diaphragm and gastrocnemius muscles in chronic lung carcinogenesis: influence of underlying emphysema. In Journal of Translational Medicine 14 (1), p. 244. DOI: 10.1186/s12967-016-1003-9.
[A16][A17]	2015	Aoki, Kohei; Teshima, Yasushi; Kondo, Hidekazu; Saito, Shotaro; Fukui, Akira; Fukunaga, Naoya et al. (2015): Role of Indoxyl Sulfate as a Predisposing Factor for Atrial Fibrillation in Renal Dysfunction. In Journal of the American Heart Association 4 (10), e002023. DOI: 10.1161/JAHA.115.002023.
[A16][A17]	2015	El-Mas, Mahmoud M.; Abdel-Rahman, Abdel A. (2015): Estrogen modulation of the ethanol-evoked myocardial oxidative stress and dysfunction via DAPK3/Akt/ERK activation in male rats. In Toxicology and Applied Pharmacology 287 (3), pp. 284–292. DOI: 10.1016/j.taap.2015.06.015.
[A16][A17]	2015	Yamada, Takashi; Abe, Masami; Lee, Jaesik; Tatebayashi, Daisuke; Himori, Koichi; Kanzaki, Keita et al. (2015): Muscle dysfunction associated with adjuvant-induced arthritis is prevented by antioxidant treatment. In Skeletal Muscle 5, p. 20. DOI: 10.1186/s13395-015-0045-7.
[A16][A17]	2014	El-Mas, Mahmoud M.; Abdel-Rahman, Abdel A. (2014): Nongenomic effects of estrogen mediate the dose-related myocardial oxidative stress and dysfunction caused by acute ethanol in female rats. In American journal of physiology. Endocrinology and Metabolism 306 (7), E740-7. DOI: 10.1152/ajpendo.00465.2013.
[A16][A17]	2014	Ibrahim, Badr M.; Fan, Ming; Abdel-Rahman, Abdel A. (2014): Oxidative Stress and Autonomic Dysregulation Contribute to the Acute Time-Dependent Myocardial Depressant Effect of Ethanol in Conscious Female Rats. In Alcoholism, Clinical and Experimental Research 38 (5), pp. 1205–1215. DOI: 10.1111/acer.12363.
[A16][A17]	2014	Okutsu, Mitsuharu; Call, Jarrod A.; Lira, Vitor A.; Zhang, Mei; Donet, Jean A.; French, Brent A. et al. (2014): Extracellular superoxide dismutase ameliorates skeletal muscle abnormalities, cachexia, and exercise intolerance in mice with congestive heart failure. In Circulation. Heart failure 7 (3), pp. 519–530. DOI: 10.1161/CIRCHEARTFAILURE.113.000841.
[A16][A17]	2014	Saito, Shotaro; Teshima, Yasushi; Fukui, Akira; Kondo, Hidekazu; Nishio, Satoru; Nakagawa, Mikiko et al. (2014): Glucose fluctuations increase the incidence of atrial fibrillation in diabetic rats. In Cardiovascular Research 104 (1), pp. 5–14. DOI: 10.1093/cvr/cvu176.
[A16][A17]	2014	Sáyago-Ayerdi, Sonia G.; Mateos, Raquel; Ortiz-Basurto, Rosa I.; Largo, Carlota; Serrano, José; Granado-Serrano, Ana Belén et al. (2014): Effects of consuming diets containing Agave tequilana dietary fibre and jamaica calyces on body weight gain and redox status in hypercholesterolemic rats. In Food Chemistry 148, pp. 54–59. DOI: 10.1016/j.foodchem.2013.10.004.
[A16][A17]	2014	Slot, Ilse G. M.; van den Borst, Bram; Hellwig, Valéry A. C. V.; Barreiro, Esther; Schols, Annemie M. W. J.; Gosker, Harry R. (2014): The muscle oxidative regulatory response to acute exercise is not impaired in less advanced COPD despite a decreased oxidative phenotype. In PLoS ONE 9 (2), e90150. DOI: 10.1371/journal.pone.0090150.
[A16][A17]	2014	Yang, Tzu-Ching; Chen, Yi-Jie; Chang, Shwu-Fen; Chen, Chu-Huang; Chang, Po-Yuan; Lu, Shao-Chun (2014): Malondialdehyde mediates oxidized LDL-induced coronary toxicity through the Akt-FGF2 pathway via DNA methylation. In Journal of Biomedical Science 21, p. 11. DOI: 10.1186/1423-0127-21-11.
[A16][A17]	2014	Zhu, Xinmei; Ng, Hang Pong; Lai, Yen-Chun; Craigo, Jodi K.; Nagilla, Pruthvi S.; Raghani, Pooja; Nagarajan, Shanmugam (2014): Scavenger Receptor Function of Mouse Fcγ Receptor III Contributes to Progression of Atherosclerosis in Apolipoprotein E Hyperlipidemic Mice. In J.I. 193 (5), pp. 2483–2495. DOI: 10.4049/jimmunol.1303075.
[A16][A17]	2013	Arashiki, Nobuto; Kimata, Naoki; Manno, Sumie; Mohandas, Narla; Takakuwa, Yuichi (2013): Membrane peroxidation and methemoglobin formation are both necessary for band 3 clustering: mechanistic insights into human erythrocyte senescence. In Biochemistry 52 (34), pp. 5760–5769. DOI: 10.1021/bi400405p.
[A16][A17]	2013	Serrano, José C. E.; Gonzalo-Benito, Hugo; Jové, Mariona; Fourcade, Stéphane; Cassanyé, Anna; Boada, Jordi et al. (2013): Dietary intake of green tea polyphenols regulates insulin sensitivity with an increase in AMP-activated protein kinase α content and changes in mitochondrial respiratory complexes. In Molecular Nutrition & Food Research 57 (3), pp. 459–470. DOI: 10.1002/mnfr.201200513.
[A16][A17]	2013	van den Borst, Bram; Slot, Ilse G. M.; Hellwig, Valéry A. C. V.; Vosse, Bettine A. H.; Kelders, Marco C. J. M.; Barreiro, Esther et al. (2013): Loss of quadriceps muscle oxidative phenotype and decreased endurance in patients with mild-to-moderate COPD. In Journal of Applied Physiology 114 (9), pp. 1319–1328. DOI: 10.1152/japplphysiol.00508.2012.
[A16][A17]	2012	Barreiro, Esther; del Puerto-Nevado, Laura; Puig-Vilanova, Ester; Pérez-Rial, Sandra; Sánchez, Francisco; Martínez-Galán, Lourdes et al. (2012): Cigarette smoke-induced oxidative stress in skeletal muscles of mice. In Respiratory Physiology & Neurobiology 182 (1), pp. 9–17. DOI: 10.1016/j.resp.2012.02.001.
[A16][A17]	2012	Fukunaga, Naoya; Takahashi, Naohiko; Hagiwara, Satoshi; Kume, Osamu; Fukui, Akira; Teshima, Yasushi et al. (2012): Establishment of a model of atrial fibrillation associated with chronic kidney disease in rats and the role of oxidative stress. In Heart Rhythm 9 (12), pp. 2023–2031. DOI: 10.1016/j.hrthm.2012.08.019.
[A16][A17]	2011	Andersson, Daniel C.; Fauconnier, Jérémy; Yamada, Takashi; Lacampagne, Alain; Zhang, Shi-Jin; Katz, Abram; Westerblad, Håkan (2011): Mitochondrial production of reactive oxygen species contributes to the β-adrenergic stimulation of mouse cardiomycytes. In J Physiol 589 (7), pp. 1791–1801. DOI: 10.1113/jphysiol.2010.202838.
[A16][A17]	2011	André, Lucas; Gouzi, Fares; Thireau, Jérôme; Meyer, Gregory; Boissiere, Julien; Delage, Martine et al. (2011): Carbon monoxide exposure enhances arrhythmia after cardiac stress: involvement of oxidative stress. In Basic Res Cardiol 106 (6), pp. 1235–1246. DOI: 10.1007/s00395-011-0211-y.
[A16][A17]	2011	Ferrer, Isidro; Carmona, Margarita; Blanco, Rosa; Recio, Maria; San Segundo, R. (2011): Gerstmann-Straüssler-Scheinker PRNP P102L-129V mutation. In Translational Neuroscience 2 (1), p. 1197. DOI: 10.2478/s13380-011-0001-x.
[A16][A17]	2011	Tolfsen, C. C.; Baker, N.; Kreibich, C.; Amdam, G. V. (2011): Flight restriction prevents associative learning deficits but not changes in brain protein-adduct formation during honeybee ageing. In Journal of Experimental Biology 214 (8), pp. 1322–1332. DOI: 10.1242/jeb.049155.
[A16][A17]	2010	Casós, Kelly; Zaragozá, María C.; Zarkovic, Neven; Zarkovic, Kamelija; Andrisic, Luka; Portero-Otín, Manuel et al. (2010): A fish-oil-rich diet reduces vascular oxidative stress in apoE(-/-) mice. In Free Radical Research 44 (7), pp. 821–829. DOI: 10.3109/10715762.2010.485992.
[A16][A17]	2010	Cholewa, Jill; Nikolic, Dejan; Post, Steven R. (2010): Regulation of class A scavenger receptor-mediated cell adhesion and surface localization by PI3K: identification of a regulatory cytoplasmic motif. In Journal of Leukocyte Biology 87 (3), pp. 443–449. DOI: 10.1189/jlb.0509318.
[A16][A17]	2010	Yamada, Takashi; Zhang, Shi-Jin; Westerblad, Hakan; Katz, Abram (2010): {beta}-Hydroxybutyrate inhibits insulin-mediated glucose transport in mouse oxidative muscle. In American Journal of Physiology-Endocrinology and Metabolism 299 (3), E364-73. DOI: 10.1152/ajpendo.00142.2010.
[A16][A17]	2009	Aydin, Jan; Andersson, Daniel C.; Hänninen, Sandra L.; Wredenberg, Anna; Tavi, Pasi; Park, Chan Bae et al. (2009): Increased mitochondrial Ca2+ and decreased sarcoplasmic reticulum Ca2+ in mitochondrial myopathy. In Human Molecular Genetics 18 (2), pp. 278–288. DOI: 10.1093/hmg/ddn355.
[A16][A17]	2009	Kichev, Anton; Ilieva, Ekaterina V.; Piñol-Ripoll, Gerard; Podlesniy, Petar; Ferrer, Isidro; Portero-Otín, Manuel et al. (2009): Cell Death and Learning Impairment in Mice Caused by in Vitro Modified Pro-NGF Can Be Related to Its Increased Oxidative Modifications in Alzheimer Disease. In The American Journal of Pathology 175 (6), pp. 2574–2585. DOI: 10.2353/ajpath.2009.090018.
[A16][A17]	2009	Woltjer, Randall L.; Sonnen, Joshua A.; Sokal, Izabela; Rung, Lisa G.; Yang, Wan; Kjerulf, John D. et al. (2009): Quantitation and Mapping of Cerebral Detergent-Insoluble Proteins in the Elderly. In Brain Pathology 19 (3), pp. 365–374. DOI: 10.1111/j.1750-3639.2008.00190.x.
[A16][A17]	2009	Yamada, Takashi; Place, Nicolas; Kosterina, Natalia; Östberg, Therese; Zhang, Shi-Jin; Grundtman, Cecilia et al. (2009): Impaired myofibrillar function in the soleus muscle of mice with collagen-induced arthritis. In Arthritis & Rheumatism 60 (11), pp. 3280–3289. DOI: 10.1002/art.24907.
[A16][A17]	2008	Bustamante, Víctor; Casanova, Juan; López de Santamaría, Elena; Mas, Sandra; Sellarés, Jacobo; Gea, Joaquim et al. (2008): Redox balance following magnetic stimulation training in the quadriceps of patients with severe COPD. In Free Radical Research 42 (11-12), pp. 939–948. DOI: 10.1080/10715760802555569.
[A16][A17]	2008	Choksi, Kashyap B.; Papaconstantinou, John (2008): Age-related alterations in oxidatively damaged proteins of mouse heart mitochondrial electron transport chain complexes. In Free Radical Biology and Medicine 44 (10), pp. 1795–1805. DOI: 10.1016/j.freeradbiomed.2008.01.032.
[A16][A17]	2008	Wallace, Sunny; Vaughn, Katherine; Stewart, Bradford W.; Viswanathan, Tito; Clausen, Edgar; Nagarajan, Shanmugam; Carrier, Danielle Julie (2008): Milk Thistle Extracts Inhibit the Oxidation of Low-Density Lipoprotein (LDL) and Subsequent Scavenger Receptor-Dependent Monocyte Adhesion. In J. Agric. Food Chem. 56 (11), pp. 3966–3972. DOI: 10.1021/jf703694u.
[A16][A17]	2007	Barreiro, Esther; Nowinski, Adam; Gea, Joaquim; Sliwinski, Pawel (2007): Oxidative stress in the external intercostal muscles of patients with obstructive sleep apnoea. In Thorax 62 (12), pp. 1095–1101. DOI: 10.1136/thx.2006.069963.
[A16][A17]	2007	Choksi, Kashyap B.; Nuss, Jonathan E.; Boylston, William H.; Rabek, Jeffrey P.; Papaconstantinou, John (2007): Age-related increases in oxidatively damaged proteins of mouse kidney mitochondrial electron transport chain complexes. In Free Radical Biology and Medicine 43 (10), pp. 1423–1438. DOI: 10.1016/j.freeradbiomed.2007.07.027.
[A16][A17]	2007	Janué, Anna; Olivé, Montse; Ferrer, Isidre (2007): Oxidative stress in desminopathies and myotilinopathies: a link between oxidative damage and abnormal protein aggregation. In Brain Pathology 17 (4), pp. 377–388. DOI: 10.1111/j.1750-3639.2007.00087.x.
[A16][A17]	2007	Nagarajan, Shanmugam (2007): Anti-OxLDL IgG blocks OxLDL interaction with CD36, but promotes FcgammaR, CD32A-dependent inflammatory cell adhesion. In Immunology Letters 108 (1), pp. 52–61. DOI: 10.1016/j.imlet.2006.09.008.
[A16][A17]	2007	Nikolic, Dejan M.; Cholewa, Jill; Gass, Cecelia; Gong, Ming C.; Post, Steven R. (2007): Class A scavenger receptor-mediated cell adhesion requires the sequential activation of Lyn and PI3-kinase. In American journal of physiology. Cell Physiology 292 (4), C1450-8. DOI: 10.1152/ajpcell.00401.2006.
[A16][A17]	2007	Nikolic, Dejan M.; Gong, Ming C.; Turk, John; Post, Steven R. (2007): Class A scavenger receptor-mediated macrophage adhesion requires coupling of calcium-independent phospholipase A(2) and 12/15-lipoxygenase to Rac and Cdc42 activation. In J. Biol. Chem. 282 (46), pp. 33405–33411. DOI: 10.1074/jbc.M704133200.
[A16][A17]	2007	Ping, Xiao-Du; Harris, Frank L.; Brown, Lou Ann S.; Gauthier, Theresa W. (2007): In vivo dysfunction of the term alveolar macrophage after in utero ethanol exposure. In Alcoholism, Clinical and Experimental Research 31 (2), pp. 308–316. DOI: 10.1111/j.1530-0277.2006.00306.x.
[A16][A17]	2007	Sellares, Jacobo; Mas, Sandra; Melo, Esther; Sánchez, Francesc; Marin, Judith; Gea, Joaquim; Barreiro, Esther (2007): Oxidative stress time course in the rat diaphragm after freezing-thawing cycles. In Respiratory Physiology & Neurobiology 155 (2), pp. 156–166. DOI: 10.1016/j.resp.2006.05.008.
[A16][A17]	2007	Toroser, Dikran; Orr, William C.; Sohal, Rajindar S. (2007): Carbonylation of mitochondrial proteins in Drosophila melanogaster during aging. In Biochemical and Biophysical Research Communications 363 (2), pp. 418–424. DOI: 10.1016/j.bbrc.2007.08.193.
[A16][A17]	2006	Barreiro, Esther; Coronell, Carlos; Laviña, Barbara; Ramírez-Sarmiento, Alba; Orozco-Levi, Mauricio; Gea, Joaquim (2006): Aging, sex differences, and oxidative stress in human respiratory and limb muscles. In Free Radical Biology and Medicine 41 (5), pp. 797–809. DOI: 10.1016/j.freeradbiomed.2006.05.027.
[A16][A17]	2006	Freixes, M.; Rodríguez, A.; Dalfó, E.; Ferrer, I. (2006): Oxidation, glycoxidation, lipoxidation, nitration, and responses to oxidative stress in the cerebral cortex in Creutzfeldt-Jakob disease. In Neurobiology of Aging 27 (12), pp. 1807–1815. DOI: 10.1016/j.neurobiolaging.2005.10.006.
[A16][A17]	2005	Barreiro, Esther; La Puente, Beatriz de; Busquets, Sílvia; López-Soriano, Francisco J.; Gea, Joaquim; Argilés, Josep M. (2005): Both oxidative and nitrosative stress are associated with muscle wasting in tumour-bearing rats. In FEBS Letters 579 (7), pp. 1646–1652. DOI: 10.1016/j.febslet.2005.02.017.
[A16][A17]	2005	Dalfó, Esther; Portero-Otín, Manuel; Ayala, Victoria; Martínez, Anna; Pamplona, Reinald; Ferrer, Isidre (2005): Evidence of oxidative stress in the neocortex in incidental Lewy body disease. In Journal of Neuropathology and Experimental Neurology 64 (9), pp. 816–830. DOI: 10.1097/01.jnen.0000179050.54522.5a.
[A16][A17]	2005	Gauthier, Theresa W.; Ping, Xiao-Du; Harris, Frank L.; Wong, Michael; Elbahesh, Husni; Brown, Lou Ann S. (2005): Fetal alcohol exposure impairs alveolar macrophage function via decreased glutathione availability. In Pediatric Research 57 (1), pp. 76–81. DOI: 10.1203/01.PDR.0000149108.44152.D3.
[A16][A17]	2005	Pamplona, Reinald; Dalfó, Esther; Ayala, Victòria; Bellmunt, Maria Josep; Prat, Joan; Ferrer, Isidre; Portero-Otín, Manuel (2005): Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets. In J. Biol. Chem. 280 (22), pp. 21522–21530. DOI: 10.1074/jbc.M502255200.
[A16][A17]	2005	Pamplona, Reinald; Portero-Otín, Manuel; Sanz, Alberto; Ayala, Victoria; Vasileva, Ekaterina; Barja, Gustavo (2005): Protein and lipid oxidative damage and complex I content are lower in the brain of budgerigar and canaries than in mice. Relation to aging rate. In Age (Dordrecht, Netherlands) 27 (4), pp. 267–280. DOI: 10.1007/s11357-005-4562-x.
[A16][A17]	2005	Yarian, Connie S.; Rebrin, Igor; Sohal, Rajindar S. (2005): Aconitase and ATP synthase are targets of malondialdehyde modification and undergo an age-related decrease in activity in mouse heart mitochondria. In Biochemical and Biophysical Research Communications 330 (1), pp. 151–156. DOI: 10.1016/j.bbrc.2005.02.135.
[A16][A17]	2004	Wen, Jian-Jun; Vyatkina, Galina; Garg, Nisha (2004): Oxidative damage during chagasic cardiomyopathy development: role of mitochondrial oxidant release and inefficient antioxidant defense. In Free Radical Biology and Medicine 37 (11), pp. 1821–1833. DOI: 10.1016/j.freeradbiomed.2004.08.018.
[A16][A17]	2004	Ye, Gang; Metreveli, Naira S.; Donthi, Rajakumar V.; Xia, Shen; Xu, Ming; Carlson, Edward C.; Epstein, Paul N. (2004): Catalase protects cardiomyocyte function in models of type 1 and type 2 diabetes. In Diabetes 53 (5), pp. 1336–1343. DOI: 10.2337/diabetes.53.5.1336.

academy biomed产品信息-载脂蛋白脂蛋白和载脂蛋白的一般信息血浆脂蛋白类别可以根据其分离的密度来定义，包括高（HDL），低（LDL），中间（IDL），极低密度脂蛋白（VLDL）和乳糜微粒。通常，脂蛋白颗粒的大小范围为10至1000 nm。它们由含有胆固醇酯，甘油三酸酯，脂肪酸和脂溶性维生素的疏水核组成。周围的亲水层由各种载脂蛋白，磷脂和胆固醇组成。载脂蛋白可以通过从脂蛋白脱脂而分离，并且已经建立了许多制备方法，例如凝胶过滤或DEAE色谱法。 脂蛋白 载脂蛋白高密度脂蛋白apoAI，AII，AIV，apoCI，CII，CIII，apoD和apoE低密度脂蛋白载脂蛋白B-100极低密度脂蛋白apoB-100，apoCI，CII，CIII和apoE乳糜微粒apoAI，AII，AIV，apoB-48，apoCI，CII，CIII，apoE和apoH 1.载脂蛋白AI（ApoAI）ApoAI约占HDL中蛋白质部分的70％。它是一条单链多肽，由243个氨基酸组成，没有二硫键结合，谷氨酸为C末端残基，天冬氨酸为N末端残基。据报道分子量为28kDa（Brewer等，1978）。ApoAI激活卵磷脂-胆固醇（LCAT）酰基转移酶，该酶负责血浆中的胆固醇酯化。ApoAI水平可能与冠状动脉疾病的风险成反比。 2.载脂蛋白AII（ApoAII）ApoAII在HDL中占ApoAI的25％。它在人血浆中以77条氨基酸残基的2条相同链的二聚体形式存在，并通过二硫键连接。据报道，单链的分子量为8.7kDa（Brewer等，1972）。对小鼠的研究报道，apoAII可能具有促动脉粥样硬化作用（Warden等，1993）。然而，大型欧洲前瞻性研究中的病例对照研究表明，血浆apoAII浓度与冠心病事件密切相关（Birjmohun等，2007）。 3.载脂蛋白B（ApoB）ApoB在人血浆中以两种亚型存在，即ApoB-48（Chen等，1987）和ApoB-100（Wei等，1985，Yang等，1986a; 1989a，b; 1990; Chen等，1990）。 1986； Yang等，1990； Yang和Pownall，1992）。ApoB-100是LDL受体的主要生理配体。ApoB100是一种大型单体蛋白，包含4536个氨基酸（分子量515 kDa，Yang等，1986b）。ApoB-100在肝脏中合成，是VLDL组装所必需的。在去除apoA，E和C后，在LDL和VLDL中发现了它。乳糜微粒及其残留物中存在ApoB-48。它对于膳食脂质的肠道吸收至关重要。ApoB水平与冠心病的风险相关。ApoB-48在小肠中合成。 4.载脂蛋白CI（ApoCI）ApoCI包含57个氨基酸残基，mw为6.6 kDa（Jackson等，1974）。已经发现ApoCI可以激活LCAT（Liu和Subbaiah 1993）并抑制胆固醇酯转移酶，该酶可能调节几种脂肪酶（Poensgen，1990; Conde-Knape等，2002; Berbee等，2005）。 5.载脂蛋白CII（ApoCII）ApoCII包含78个氨基酸残基。mw为8.5 kDa（Jackson等，1977）。ApoCII激活脂蛋白脂肪酶，该酶水解乳糜微粒中三酰基甘油中的脂肪酸。 6.载脂蛋白CIII（ApoCIII）ApoCIII包含79个氨基酸残基。mw为8.7 kDa（Brewer等，1974）。它可能会抑制apoCIII激活脂蛋白脂肪酶。ApoCIII是循环中含apoB和含apoAI的脂蛋白的组成部分。ApoCIII在调节VLDL，IDL和LDL的血浆代谢中起着关键作用，主要是通过抑制受体介导的肝脏对这些脂蛋白的摄取（Sehayek和Eisenberg 1991，Aalto-Setala等人，1992，Zheng等人。 ，2007） 7.载脂蛋白E（ApoE）ApoE包含299个氨基酸残基。它是一种34-37 kDa的糖基化蛋白（Rall等，1983）。ApoE与甘油三酸酯，磷脂，胆固醇酯和胆固醇在细胞内外的转运有关，并且是LDL受体的配体。ApoE也与免疫和神经变性有关。已经发现抑制淋巴细胞增殖。已发现晚期家族性和偶发性阿尔茨海默病患者的三种常见ApoE亚型之一ApoE4发生率更高。已在阿尔茨海默氏病患者的老年斑和神经原纤维缠结中检测到ApoE4亚型。ApoE4与乳糜微粒残留的快速清除和总胆固醇水平升高有关。 8.载脂蛋白（a）[载脂蛋白（a）]人脂蛋白[a]，Lp [a]的血浆浓度与冠状动脉疾病高度相关。Lp [a]的蛋白质部分apoLp [a]由两个载脂蛋白apo [a]和apoB-100组成，它们通过一个或多个二硫键连接。Apo [a]是Lp [a]特有的蛋白质，以多态性形式存在，其表观分子量从419 kDa到838 kDa不等（Gaubatz等，1983； 1990，1993）。 9.纤溶酶原纤溶酶原包含810个氨基酸残基。它是分子量为90 kDa的单链糖蛋白（Robbins等，1967），可溶于水。由经认证测试显示对HBsAg以及HIV和HCV抗体呈阴性的血浆制备。纤溶酶原是蛋白酶纤溶酶的无活性前体。纤溶酶原通过组织纤溶酶原激活物（tPA）的作用被激活，后者主要激活纤溶酶的纤溶活性（血栓溶解），而尿激酶纤溶酶原激活物（uPA）与细胞外基质重塑和细胞迁移有关。 10. C反应蛋白（CRP）人C反应蛋白（CRP）是预测未来心血管事件（如心脏病和中风）的重要生物标志物（Koenig等，1999； Jenny等，2007； Kabagambe等。2011）。CRP是肝脏产生的急性期蛋白。它是五味素蛋白家族的成员，具有五个相同的非糖基化亚基，每个亚基具有206个氨基酸（mw 23 kDa）（Agrawal等，2009）。在炎症的其他标志物中，CRP与心血管事件之间的关联最强（Marsik等，2008； Kones等，2010）。临床研究表明，不稳定型心绞痛和CRP升高的患者的冠心病死亡率明显高于CRP升高的患者。它是检测处于斑块性高风险的个体的重要生物标志物。 11.伊里辛运动诱导型肌动蛋白鸢尾素（Boström等人，2012）是通过从跨膜前体FNDC5裂解而分泌的。循环鸢尾素控制着与褐变，血管生成，伤口愈合，骨量和新陈代谢有关的多种细胞过程。