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Journal articles on the topic 'Homocysteinylation'

Author: Grafiati

Published: 6 September 2023

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1

Bełtowski, Jerzy, Grażyna Wójcicka, and Hieronim Jakubowski. "Modulation of paraoxonase 1 and protein N-homocysteinylation by leptin and the synthetic liver X receptor agonist T0901317 in the rat." Journal of Endocrinology 204, no. 2 (November 2, 2009): 191–98. http://dx.doi.org/10.1677/joe-09-0298.

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The adipose tissue hormone leptin and homocysteine (Hcy)-thiolactone are linked to the pathogenesis of atherosclerosis through their interactions with the anti-atherogenic enzyme paraoxonase 1 that has the ability to hydrolyze Hcy-thiolactone and minimizes protein N-homocysteinylation. Here we examined the relationships between hyperleptinemia, Hcy-thiolactonase, and protein N-homocysteinylation in rats. Hyperleptinemia was induced in adult rats by administration of leptin for 7 days (0.25 mg/kg twice daily s.c). We found that serum Hcy-thiolactonase was lower in hyperleptinemic than in control animals (−41.0%, P<0.001). Leptin administration increased the level of N-linked Hcy in plasma proteins (+92.9%, P<0.01), but had no effect on plasma total Hcy. These effects were not reproduced by pair-feeding. We also found that the synthetic liver X receptor (LXR) agonist, T0901317 (1 mg/kg per day) normalized Hcy-thiolactonase and protein N-homocysteinylation levels in leptin-treated rats. However, leptin-induced increase in plasma isoprostane levels (a marker of oxidative stress) was not normalized by T0901317. The NADPH oxidase inhibitor apocynin prevented leptin-induced increase in isoprostane levels but did not normalize Hcy-thiolactonase and protein N-homocysteinylation levels. These results suggest that the decreased capacity to metabolize Hcy-thiolactone and concomitant increase in protein N-homocysteinylation contribute to pro-atherogenic effect of chronic hyperleptinemia, independently of oxidative stress. LXR agonists normalize Hcy-thiolactonase levels and decrease protein N-homocysteinylation, especially under conditions associated with excess leptin such as metabolic syndrome.

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2

Chen, Nan, Zeyu Qiao, and Chu Wang. "A chemoselective reaction between protein N-homocysteinylation and azides catalyzed by heme(ii)." Chemical Communications 55, no. 25 (2019): 3654–57. http://dx.doi.org/10.1039/c9cc00055k.

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3

Chen, Nan, Jinmin Liu, Zeyu Qiao, Yuan Liu, Yue Yang, Changtao Jiang, Xian Wang, and Chu Wang. "Chemical proteomic profiling of proteinN-homocysteinylation with a thioester probe." Chemical Science 9, no. 10 (2018): 2826–30. http://dx.doi.org/10.1039/c8sc00221e.

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4

Xu, Leilei, Jiajia Chen, Jun Gao, Hongxiu Yu, and Pengyuan Yang. "Crosstalk of homocysteinylation, methylation and acetylation on histone H3." Analyst 140, no. 9 (2015): 3057–63. http://dx.doi.org/10.1039/c4an02355b.

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5

Jakubowski, H. "Protein N-homocysteinylation: implications for atherosclerosis." Biomedicine & Pharmacotherapy 55, no. 8 (October 2001): 443–47. http://dx.doi.org/10.1016/s0753-3322(01)00085-3.

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6

Jakubowski, Hieronim. "Protein N-Homocysteinylation and Colorectal Cancer." Trends in Cancer 5, no. 1 (January 2019): 7–10. http://dx.doi.org/10.1016/j.trecan.2018.10.006.

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7

Perna, A. F., E. Satta, F. Acanfora, C. Lombardi, D. Ingrosso, and N. G. De Santo. "Increased plasma protein homocysteinylation in hemodialysis patients." Kidney International 69, no. 5 (March 2006): 869–76. http://dx.doi.org/10.1038/sj.ki.5000070.

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8

Colgan, Stephen M., and Richard C. Austin. "Homocysteinylation of Metallothionein Impairs Intracellular Redox Homeostasis." Arteriosclerosis, Thrombosis, and Vascular Biology 27, no. 1 (January 2007): 8–11. http://dx.doi.org/10.1161/01.atv.0000254151.00086.26.

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9

Balint, Brittany, Sébastien Hergalant, Jean-Michel Camadro, Sébastien Blaise, Laetitia Vanalderwiert, Laurent Lignières, Rosa-Maria Guéant-Rodriguez, and Jean-Louis Guéant. "Fetal Programming by Methyl Donor Deficiency Produces Pathological Remodeling of the Ascending Aorta." Arteriosclerosis, Thrombosis, and Vascular Biology 41, no. 6 (June 2021): 1928–41. http://dx.doi.org/10.1161/atvbaha.120.315587.

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Objective: Deficiency in vitamin B12/folate (methyl donor deficiency [MDD]) produces cardiovascular outcomes during aging and fetal programming effects in newborns of MDD mothers. Whether fetal programming provokes long-term effects on aorta remains largely unknown. Approach and Results: We investigated the impact of fetal programming on ascending aorta of aged rats born from mothers subjected to MDD during gestation/lactation. We performed morphological and molecular examinations of ascending aortas in 21 days- and 400 days-aged rats with initial MDD fetal programming (iMDD) compared with control matched rats. iMDD induces remodeling of the ascending aorta in aged rats, with collagen deposition ( P =0.0008), decreased thickness of elastin ( P <0.0001), and 8.7-fold increase of elastin breaks ( P =0.0002). Proteomic analyses, Western blotting, and immunohistochemical examination revealed decreased expression of α-smooth muscle actin, vinculin, SM22α (smooth muscle 22α), and N-cadherin and increased expression of TGF (transforming growth factor) β1. Elastin breaks were correlated to increased neutrophil elastase ( P =0.0002), cathepsin-K ( P =0.0002), cathepsin-S ( P <0.0001), MMP (matrix metalloproteinase) 9, and MMP2 ( P <0.0001 and P =0.02). Proximity Duolink ligation assay showed homocysteinylation of actin-associated and extracellular matrix proteins, including SM22α ( P =0.01), N-cadherin ( P =0.0008), and vinculin ( P =0.001), which was associated with elastin breaks ( P =0.002) and increased expression of MARS (methionyl-tRNA synthetase; involved in irreversible protein homocysteinylation). Furthermore, we observed an inverse relationship between elastin breaks and blood pressure (systolic, P =0.004 and diastolic, P =0.0007). Conclusions: MDD fetal programming produced altered integrity and remodeling of ascending aorta during aging and irreversible MARS-associated homocysteinylation of key proteins of extracellular matrix and elastin homeostasis. This contributes to understanding why homocysteine-lowering vitamin B supplementation fails to relieve vascular complications in adulthood.

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10

Jamroz-Wiśniewska, A., J. Bełtowski, H. Bartosik-Psujek, G. Wójcicka, and K. Rejdak. "Processes of plasma proteinN-homocysteinylation in multiple sclerosis." International Journal of Neuroscience 127, no. 8 (October 14, 2016): 709–15. http://dx.doi.org/10.1080/00207454.2016.1241782.

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11

Zinellu, Angelo, Elisabetta Zinellu, Salvatore Sotgia, Marilena Formato, Gian Mario Cherchi, Luca Deiana, and Ciriaco Carru. "Factors Affecting S-Homocysteinylation of LDL Apoprotein B." Clinical Chemistry 52, no. 11 (November 1, 2006): 2054–59. http://dx.doi.org/10.1373/clinchem.2006.071142.

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Abstract Background: Hyperhomocysteinemia is an important risk factor for vascular disease and atherosclerosis, but the mechanisms by which homocysteine exerts its deleterious effects are not known. Because oxidation and/or homocysteinylation may increase atherogenicity of LDL, we investigated S-homocysteinylation of LDL as a possible contributor to atherosclerosis pathogenesis. Methods: We used capillary electrophoresis to measure LDL-bound thiols [homocysteine, cysteine (Cys), cysteinylglycine, glutathione, and glutamylcysteine] in 104 healthy study participants We also assessed total plasma thiol concentrations and lipid profiles. Results: Our data suggest that apoprotein B (apoB)-cysteinylglycine (CysGly), apoB-Hcy, and apoB-Cys concentrations are markedly higher in men than in women. The percentage of CysGly and glutathione on apoB was higher than that of the same thiols in plasma, whereas the other thiols were markedly less prevalent in lipoprotein than in plasma. Pearson correlation showed that among all thiols, only total plasma Hcy is related to apoB-Hcy concentrations. Multiple correlation analysis confirmed that total Hcy was the most important determinant of apoB-Hcy. Age and LDL cholesterol also showed positive associations, but Cys and, mainly, CysGly were negatively associated with apoB-Hcy concentrations. Conclusions: apoB-Hcy derivative formation is mainly dependent on total homocysteine concentration. Increased cholesterol concentrations are related to increased apoB-Hcy. CysGly seems to compete with Hcy for binding to LDL apoprotein, suggesting that CysGly may protect against atherosclerosis by decreasing the concentrations of Hcy transferred by LDL from plasma to endothelial and subendothelial spaces.

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12

Sharma, Gurumayum Suraj, Tarun Kumar, Tanveer Ali Dar, and Laishram Rajendrakumar Singh. "Protein N-homocysteinylation: From cellular toxicity to neurodegeneration." Biochimica et Biophysica Acta (BBA) - General Subjects 1850, no. 11 (November 2015): 2239–45. http://dx.doi.org/10.1016/j.bbagen.2015.08.013.

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13

Sikora, Marta, Łukasz Marczak, Jolanta Kubalska, AŁŁa Graban, and Hieronim Jakubowski. "Identification of N-homocysteinylation sites in plasma proteins." Amino Acids 46, no. 1 (November 30, 2013): 235–44. http://dx.doi.org/10.1007/s00726-013-1617-7.

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14

Zhloba, Alexandr A., and Tatiana F. Subbotina. "Homocysteinylation score of high-molecular weight plasma proteins." Amino Acids 46, no. 4 (December 25, 2013): 893–99. http://dx.doi.org/10.1007/s00726-013-1652-4.

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15

Deslandes, Jordan, Jessy-Carol Ntunzwenimana, Laurane Forestier, Vincent Lacasse, Richard J. Wagner, and Klaus Klarskov. "Dehydroascorbate-Induced Peptide S-Glutathionylation and S-Homocysteinylation." Free Radical Biology and Medicine 87 (October 2015): S53. http://dx.doi.org/10.1016/j.freeradbiomed.2015.10.139.

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16

Jakubowski, Hieronim. "Homocysteine Thiolactone: Metabolic Origin and Protein Homocysteinylation in Humans." Journal of Nutrition 130, no. 2 (February 1, 2000): 377S—381S. http://dx.doi.org/10.1093/jn/130.2.377s.

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17

Gates, Arther T., Leonard Moore, Monica R. Sylvain, Christina M. Jones, Mark Lowry, Bilal El-Zahab, James W. Robinson, Robert M. Strongin, and Isiah M. Warner. "Mechanistic Investigation ofN-Homocysteinylation-Mediated Protein−Gold Nanoconjugate Assembly." Langmuir 25, no. 16 (August 18, 2009): 9346–51. http://dx.doi.org/10.1021/la900798q.

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18

Perla‐Kaján, Joanna, and Hieronim Jakubowski. "Paraoxonase 1 protects against protein N ‐homocysteinylation in humans." FASEB Journal 24, no. 3 (October 30, 2009): 931–36. http://dx.doi.org/10.1096/fj.09-144410.

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19

Jakubowski, Hieronim, Li Zhang, Arlene Bardeguez, and Abram Aviv. "Homocysteine Thiolactone and Protein Homocysteinylation in Human Endothelial Cells." Circulation Research 87, no. 1 (July 7, 2000): 45–51. http://dx.doi.org/10.1161/01.res.87.1.45.

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20

Leri, Manuela, Paola Rebuzzini, Anna Caselli, Simone Luti, Antonino Natalello, Sofia Giorgetti, Loredana Marchese, et al. "S-Homocysteinylation effects on transthyretin: worsening of cardiomyopathy onset." Biochimica et Biophysica Acta (BBA) - General Subjects 1864, no. 1 (January 2020): 129453. http://dx.doi.org/10.1016/j.bbagen.2019.129453.

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21

Huang, An, John T. Pinto, Ghezal Froogh, Sharath Kandhi, Jun Qin, Michael S. Wolin, Thomas H. Hintze, and Dong Sun. "Role of homocysteinylation of ACE in endothelial dysfunction of arteries." American Journal of Physiology-Heart and Circulatory Physiology 308, no. 2 (January 15, 2015): H92—H100. http://dx.doi.org/10.1152/ajpheart.00577.2014.

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The direct impact of de novo synthesis of homocysteine (Hcy) and its reactive metabolites, Hcy-S-S-Hcy and Hcy thiolactone (HCTL), on vascular function has not been fully elucidated. We hypothesized that Hcy synthesized within endothelial cells affects activity of angiotensin-converting enzyme (ACE) by direct homocysteinylation of its amino- and/or sulfhydryl moieties. This covalent modification enhances ACE reactivity toward angiotensin II (ANG II)-NADPH oxidase-superoxide-dependent endothelial dysfunction. Mesenteric and coronary arteries isolated from normal rats were incubated for 3 days with or without exogenous methionine (Met, 0.1–0.3 mM), a precursor to Hcy. Incubation of arteries in Met-free media resulted in time-dependent decreases in vascular Hcy formation. By contrast, vessels incubated with Met produced Hcy in a dose-dependent manner. There was a notably greater de novo synthesis of Hcy from endothelial than from smooth muscle cells. Enhanced levels of Hcy production significantly impaired shear stress-induced dilation and release of nitric oxide, events that are associated with elevated production of vascular superoxide. Each of these processes was attenuated by ANG II type I receptor blocker or ACE and NADPH oxidase inhibitors. In addition, in vitro exposure of purified ACE to Hcy-S-S-Hcy/HCTL resulted in formation of homocysteinylated ACE and an enhanced ACE activity. The enhanced ACE activity was confirmed in isolated coronary and mesenteric arteries that had been exposed directly to Hcy-S-S-Hcy/HCTL or after Met incubation. In conclusion, vasculature-derived Hcy initiates endothelial dysfunction that, in part, may be mediated by ANG II-dependent activation of NADPH oxidase in association with homocysteinylation of ACE.

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22

Ferretti, Gianna, Tiziana Bacchetti, Simona Masciangelo, and Virginia Bicchiega. "Effect of homocysteinylation on high density lipoprotein physico-chemical properties." Chemistry and Physics of Lipids 163, no. 2 (February 2010): 228–35. http://dx.doi.org/10.1016/j.chemphyslip.2009.11.008.

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23

Zinellu, Angelo, Giacomina Loriga, Bastianina Scanu, Elisabetta Pisanu, Manuela Sanna, Luca Deiana, Andrea Ercole Satta, and Ciriaco Carru. "Increased Low-Density Lipoprotein S-Homocysteinylation in Chronic Kidney Disease." American Journal of Nephrology 32, no. 3 (2010): 242–48. http://dx.doi.org/10.1159/000319012.

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24

Stroylova, Yulia Y., Jean-Marc Chobert, Vladimir I. Muronetz, Hieronim Jakubowski, and Thomas Haertlé. "N-homocysteinylation of ovine prion protein induces amyloid-like transformation." Archives of Biochemistry and Biophysics 526, no. 1 (October 2012): 29–37. http://dx.doi.org/10.1016/j.abb.2012.06.008.

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25

Miyazaki, Akari, Nozomi Sagae, Yoko Usami, Megumi Sato, Takahiro Kameda, Akira Yoshimoto, Nau Ishimine, et al. "N-homocysteinylation of apolipoprotein A-I impairs the protein’s antioxidant ability but not its cholesterol efflux capacity." Biological Chemistry 395, no. 6 (June 1, 2014): 641–48. http://dx.doi.org/10.1515/hsz-2013-0262.

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Abstract A high homocysteine (Hcy) level is a risk factor for atherosclerosis. Hcy can be added to proteins through a process known as N-homocysteinylation. This is thought to be a potential cause of atherosclerosis induction. We previously reported that N-homocysteinylated apolipoprotein A-I (N-Hcy-apoA-I) was identified in normal human plasma. In this study, the effect of N-homocysteinylation on the functions of apoA-I was examined. A kinetic study using dimyristoyl phosphatidylcholine (DMPC) liposomes indicated that N-Hcy-apoA-I showed increased lipid-binding activity compared to wild-type apoA-I. Two reconstituted high-density lipoprotein (rHDL) particles of different sizes (approximately 8.2 nm and 7.6 nm in diameter) were produced by mixing apoA-I and 1-palmitoyl-2-oleoyl phosphatidylcholine (POPC). However, an increased ratio of large to small particles was found in rHDL prepared with N-Hcy-apoA-I. The normal apoA-I antioxidant ability, estimated by the suppression of conjugated diene formation in low-density lipoprotein (LDL) induced by copper sulfate oxidation, was considerably impaired when using N-Hcy-apoA-I. Although N-Hcy-apoA-I functioned as an oxidant, no significant difference was observed in the cholesterol efflux capacity from THP-1 macrophages between wild-type apoA-I and N-Hcy-apoA-I. These results suggest that N-Hcy-apoA-I might be proatherogenic due to its oxidative behavior but not an attenuation of cholesterol efflux capacity.

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26

Perl̷a-Kaján, Joanna, Agata Malinowska, Jarosl̷aw Zimny, Dominik Cysewski, Joanna Suszyńska-Zajczyk, and Hieronim Jakubowski. "Proteome-Wide Analysis of Protein Lysine N-Homocysteinylation in Saccharomyces cerevisiae." Journal of Proteome Research 20, no. 5 (April 2, 2021): 2458–76. http://dx.doi.org/10.1021/acs.jproteome.0c00937.

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27

JAKUBOWSKI, HIERONIM. "Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels." FASEB Journal 13, no. 15 (December 1999): 2277–83. http://dx.doi.org/10.1096/fasebj.13.15.2277.

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28

Genoud, Valeria, Paula G. Quintana, Silvana Gionco, Alicia Baldessari, and Irene Quintana. "Structural changes of fibrinogen molecule mediated by the N-homocysteinylation reaction." Journal of Thrombosis and Thrombolysis 45, no. 1 (October 26, 2017): 66–76. http://dx.doi.org/10.1007/s11239-017-1574-1.

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29

Paoli, Paolo, Francesca Sbrana, Bruno Tiribilli, Anna Caselli, Barbara Pantera, Paolo Cirri, Alina De Donatis, et al. "Protein N-Homocysteinylation Induces the Formation of Toxic Amyloid-Like Protofibrils." Journal of Molecular Biology 400, no. 4 (July 2010): 889–907. http://dx.doi.org/10.1016/j.jmb.2010.05.039.

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30

Parada-Turska, Jolanta, Grażyna Wójcicka, and Jerzy Beltowski. "Paraoxonase 1 Phenotype and Protein N-Homocysteinylation in Patients with Rheumatoid Arthritis: Implications for Cardiovascular Disease." Antioxidants 9, no. 9 (September 21, 2020): 899. http://dx.doi.org/10.3390/antiox9090899.

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Paraoxonase 1 (PON1) is the high density lipoprotein-associated esterase which inhibits the development of atherosclerosis by metabolizing lipid peroxidation products as well as hydrolyzing proatherogenic metabolite of homocysteine (Hcy), Hcy thiolactone, which otherwise reacts with lysine groups of proteins, thus forming N-Hcy-protein in a process referred to as protein N-homocysteinylation. Rheumatoid arthritis (RA) is the chronic inflammatory autoimmune disease associated with increased risk of cardiovascular complications, but the underlying mechanisms are incompletely understood. We examined PON1 status and N-homocysteinylation of serum proteins in patients with RA. Blood was collected from 74 RA patients and 70 control subjects. PON1 activity was measured toward synthetic (paraoxon, phenyl acetate) and natural (Hcy thiolactone) substrates. PON1 protein concentration was measured by ELISA. Total Hcy as well as N-Hcy-protein were measured in serum as well. PON1 activity toward Hcy thiolactone was lower in RA patients than in control subjects which was accompanied by increased concentration of N-Hcy-protein despite normal total Hcy concentration. PON1 protein concentration was unchanged in the RA group, but the specific enzyme activity was reduced. When RA patients were categorized according to the DAS28-ESR score, PON1 concentration and enzymatic activity were lower whereas N-Hcy-protein was higher in those with high disease activity. PON1 activity and Hcy thiolactone were correlated with DAS28-ESR score and myeloperoxidase concentration. In conclusion, RA is associated with deficiency of PON1 activity and increased protein N-homocyseinylation which may contribute to accelerated development of cardiovascular diseases.

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31

Khodadadi, Sirus, Gholam Hossein Riazi, Shahin Ahmadian, Elham Hoveizi, Oveis Karima, and Hassan Aryapour. "Effect ofN-homocysteinylation on physicochemical and cytotoxic properties of amyloid β-peptide." FEBS Letters 586, no. 2 (December 23, 2011): 127–31. http://dx.doi.org/10.1016/j.febslet.2011.12.018.

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32

Wang, Dan, Rui Zhao, Yuan-Yuan Qu, Xin-Yu Mei, Xuan Zhang, Qian Zhou, Yang Li, et al. "Colonic Lysine Homocysteinylation Induced by High-Fat Diet Suppresses DNA Damage Repair." Cell Reports 25, no. 2 (October 2018): 398–412. http://dx.doi.org/10.1016/j.celrep.2018.09.022.

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33

Zinellu, Angelo, Salvatore Sotgia, Bastianina Scanu, Luca Deiana, Giuseppe Talanas, PierFranco Terrosu, and Ciriaco Carru. "Low density lipoprotein S-homocysteinylation is increased in acute myocardial infarction patients." Clinical Biochemistry 45, no. 4-5 (March 2012): 359–62. http://dx.doi.org/10.1016/j.clinbiochem.2011.12.017.

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34

Hop, Cornelis E. C. A., and Ray Bakhtiar. "Homocysteine thiolactone and protein homocysteinylation: mechanistic studies with model peptides and proteins." Rapid Communications in Mass Spectrometry 16, no. 11 (2002): 1049–53. http://dx.doi.org/10.1002/rcm.681.

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35

Jamroz-Wiśniewska, Anna, Jerzy Bełtowski, Grażyna Wójcicka, Halina Bartosik-Psujek, and Konrad Rejdak. "Cladribine Treatment Improved Homocysteine Metabolism and Increased Total Serum Antioxidant Activity in Secondary Progressive Multiple Sclerosis Patients." Oxidative Medicine and Cellular Longevity 2020 (March 17, 2020): 1–7. http://dx.doi.org/10.1155/2020/1654754.

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Hyperhomocysteinemia plays a crucial role in the pathogenesis of many diseases of the central nervous system (CNS). The nervous system is particularly sensitive to high homocysteine (Hcy) level mainly due to its prooxidative and cytotoxic effects. Cladribine, a drug recently registered for the treatment of multiple sclerosis (MS), possesses additionally neuroprotective effects which are independent of its peripheral immunosuppressant action. Accumulating evidence suggests that oxidative stress and homocysteine thiolactone-mediated protein homocysteinylation play a causal role in MS. Both of these processes may be attenuated by paraoxonase 1 (PON1). Therefore, in the present study, we aimed to examine whether the beneficial effects of the drug in MS patients with a secondary progressive (SP) clinical course, treated with cladribine subcutaneously (s.c.), may be related to its ability to modify serum PON1 activity, Hcy concentration, and protein homocysteinylation, as well as to correct total antioxidant status. A total of 118 subjects were enrolled into the study: (1) patients with a SP type of MS, SP-MS (n=40); (2) patients with a relapsing-remitting (RR) type of MS, RR-MS (n=30); and (3) healthy people (n=48). Patients with SP-MS were treated with cladribine. The drug was given in SP-SM patients s.c. six times every 6 weeks up to a total mean cumulative dose of 1.8 mg/kg. PON1 activity was assessed spectrophotometrically. The level of Hcy, homocysteine thiolactone (HTL) attached to plasma proteins (N-Hcy-protein), and antibodies against homocysteinylated proteins was assessed with an enzyme immunoassay. The total antioxidant activity of the serum was assessed with the ferric-reducing activity of plasma (FRAP) method. Basically, there was no difference in PON1 activity between untreated SP-MS, RR-MS, and control subjects. Serum Hcy was significantly higher in RR-MS patients (p<0.001) and in SP-MS patients (p<0.01) compared to the control group. The N-Hcy protein level was higher in RR-MS patients (p<0.05) in comparison to the control group. Moreover, the elevated level of antibodies against homocysteinylated proteins was observed in the serum of patients with SP-MS. The total antioxidant capacity of serum was lower in MS patients vs. the control group (p<0.001). After cladribine treatment, the activity of PON1 did not change in SP-MS patients, whereas cladribine treatment decreased the level of total Hcy (p<0.05). Treatment with cladribine increased the total serum antioxidant activity in SP-MS patients (p<0.01). The Expanded Disability Status Scale (EDSS) score did not change in SP-MS patients. Cladribine treatment in the SP-MS group attenuates hyperhomocysteinemia-induced protein homocysteinylation (n.s.). It also stabilises the neurological condition of SP-MS patients. The stabilisation of a neurological condition observed in SP-MS patients after cladribine treatment may be partially related to its ability to reduce elevated Hcy level and to improve serum antioxidant potential.

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36

Borowczyk, Kamila, Jacek Wróblewski, Joanna Suliburska, Noriyuki Akahoshi, Isao Ishii, and Hieronim Jakubowski. "Mutations in Homocysteine Metabolism Genes Increase Keratin N-Homocysteinylation and Damage in Mice." International Journal of Genomics 2018 (September 23, 2018): 1–7. http://dx.doi.org/10.1155/2018/7570850.

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Genetic or nutritional deficiencies in homocysteine (Hcy) metabolism increase Hcy-thiolactone, which causes protein damage by forming isopetide bonds with lysine residues, generating N-Hcy-protein. In the present work, we studied the prevalence and genetic determinants of keratin damage caused by homocysteinylation. We found that in mammals and birds, 35 to 98% of Hcy was bound to hair keratin via amide or isopeptide bond (Hcy-keratin), while 2 to 65% was S-Hcy-keratin. A major fraction of hair Hcy-keratin (56% to 93%), significantly higher in birds than in mammals, was sodium dodecyl sulfate-insoluble. Genetic hyperhomocysteinemia significantly increased N-Hcy-keratin levels in the mouse pelage. N-Hcy-keratin was elevated 3.5-, 6.3-, and 11.7-fold in hair from Mthfr−/−, Cse−/−, or Cbs−/− mice, respectively. The accumulation of N-Hcy in hair keratin led to a progressive reduction of N-Hcy-keratin solubility in sodium dodecyl sulfate, from 0.39 ± 0.04 in wild-type mice to 0.19 ± 0.03, 0.14 ± 0.01, and 0.07 ± 0.03 in Mthfr−/−, Cse−/−, or Cbs−/−animals, respectively. N-Hcy-keratin accelerated aggregation of unmodified keratin in Cbs−/− mouse hair. Keratin methionine, copper, and iron levels in mouse hair were not affected by hyperhomocysteinemia. These findings provide evidence that pelage keratin is N-homocysteinylated in vivo in mammals and birds, and that this process causes keratin damage, manifested by a reduced solubility.

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37

Hubmacher, Dirk, Judith T. Cirulis, Ming Miao, Fred W. Keeley, and Dieter P. Reinhardt. "Functional Consequences of Homocysteinylation of the Elastic Fiber Proteins Fibrillin-1 and Tropoelastin." Journal of Biological Chemistry 285, no. 2 (November 4, 2009): 1188–98. http://dx.doi.org/10.1074/jbc.m109.021246.

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Rossi, R., D. Giustarini, A. Milzani, and I. Dalle-Donne. "Cysteinylation and homocysteinylation of plasma protein thiols during ageing of healthy human beings." Journal of Cellular and Molecular Medicine 13, no. 9b (July 10, 2008): 3131–40. http://dx.doi.org/10.1111/j.1582-4934.2008.00417.x.

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Ferretti, G., T. Bacchetti, E. Marotti, and G. Curatola. "Effect of homocysteinylation on human high-density lipoproteins: A correlation with paraoxonase activity." Metabolism 52, no. 2 (February 2003): 146–51. http://dx.doi.org/10.1053/meta.2003.50033.

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Głowacki, Rafał, and Hieronim Jakubowski. "Cross-talk between Cys34and Lysine Residues in Human Serum Albumin Revealed byN-Homocysteinylation." Journal of Biological Chemistry 279, no. 12 (December 29, 2003): 10864–71. http://dx.doi.org/10.1074/jbc.m313268200.

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Sharma, Gurumayum Suraj, Tarun Kumar, and Laishram Rajendrakumar Singh. "N-Homocysteinylation Induces Different Structural and Functional Consequences on Acidic and Basic Proteins." PLoS ONE 9, no. 12 (December 31, 2014): e116386. http://dx.doi.org/10.1371/journal.pone.0116386.

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Schiappacasse, Agustina, Romina Eugenia Maltaneri, María Eugenia Chamorro, Alcira Beatriz Nesse, Diana Elena Wetzler, and Daniela Cecilia Vittori. "Modification of erythropoietin structure by N ‐homocysteinylation affects its antiapoptotic and proliferative functions." FEBS Journal 285, no. 20 (August 29, 2018): 3801–14. http://dx.doi.org/10.1111/febs.14632.

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Sotgia, Salvatore, Ciriaco Carru, Gerard Aime Pinna, Luca Deiana, and Angelo Zinellu. "D-Penicillamine Interferes With S-Homocysteinylation and S-Cysteinylation of LDL Apolipoprotein B." Journal of Clinical Pharmacology 51, no. 12 (December 2011): 1728–32. http://dx.doi.org/10.1177/0091270010385933.

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Gałczyński, Krzysztof, Jerzy Bełtowski, Łukasz Nowakowski, Danuta Vasilevska, Tomasz Rechberger, and Andrzej Semczuk. "Serum paraoxonase 1 activity and protein N-homocysteinylation in primary human endometrial cancer." Tumor Biology 40, no. 9 (August 2018): 101042831879786. http://dx.doi.org/10.1177/1010428318797869.

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Zinellu, Angelo, Salvatore Sotgia, Elisabetta Pisanu, Giacomina Loriga, Luca Deiana, Andrea Ercole Satta, and Ciriaco Carru. "LDL S-homocysteinylation decrease in chronic kidney disease patients undergone lipid lowering therapy." European Journal of Pharmaceutical Sciences 47, no. 1 (August 2012): 117–23. http://dx.doi.org/10.1016/j.ejps.2012.05.006.

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Stroylova, Yulia Y., Jaroslaw Zimny, Reza Yousefi, Jean-Marc Chobert, Hieronim Jakubowski, Vladimir I. Muronetz, and Thomas Haertlé. "Aggregation and structural changes of αS1-, β- and κ-caseins induced by homocysteinylation." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1814, no. 10 (October 2011): 1234–45. http://dx.doi.org/10.1016/j.bbapap.2011.05.017.

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Sharma, Gurumayum Suraj, and Laishram Rajendrakumar Singh. "Conformational status of cytochrome c upon N-homocysteinylation: Implications to cytochrome c release." Archives of Biochemistry and Biophysics 614 (January 2017): 23–27. http://dx.doi.org/10.1016/j.abb.2016.12.006.

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Zinellu, Angelo, Salvatore Sotgia, Bastianina Scanu, Dionigia Arru, Annalisa Cossu, Anna Maria Posadino, Roberta Giordo, Arduino A. Mangoni, Gianfranco Pintus, and Ciriaco Carru. "N- and S-homocysteinylation reduce the binding of human serum albumin to catechins." European Journal of Nutrition 56, no. 2 (December 10, 2015): 785–91. http://dx.doi.org/10.1007/s00394-015-1125-5.

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Sundaramoorthy, Elayanambi, Souvik Maiti, Samir K. Brahmachari, and Shantanu Sengupta. "Predicting protein homocysteinylation targets based on dihedral strain energy and pKa of cysteines." Proteins: Structure, Function, and Bioinformatics 71, no. 3 (December 12, 2007): 1475–83. http://dx.doi.org/10.1002/prot.21846.

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Zhang, Xuan, Yuan-Yuan Qu, Lian Liu, Ya-Nan Qiao, Hao-Ran Geng, Yan Lin, Wei Xu, Jing Cao, and Jian-Yuan Zhao. "Homocysteine inhibits pro-insulin receptor cleavage and causes insulin resistance via protein cysteine-homocysteinylation." Cell Reports 37, no. 2 (October 2021): 109821. http://dx.doi.org/10.1016/j.celrep.2021.109821.

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