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Home / Equine Research Bank / Animals (Basel) / Myeloperoxidase Inhibition Decreases the Expression of Colla...
Animals : an open access journal from MDPI2021; 11(1); 208; doi: 10.3390/ani11010208

Myeloperoxidase Inhibition Decreases the Expression of Collagen and Metallopeptidase in Mare Endometria under In Vitro Conditions.

Abstract: Neutrophils can originate neutrophil extracellular traps (NETs). Myeloperoxidase (MPO) is a peroxidase found in NETs associated to equine endometrosis and can be inhibited by 4-aminobenzoic acid hydrazide (ABAH). Metallopeptidases (MMPs) participate in extracellular matrix stability and fibrosis development. The objectives of this in vitro work were to investigate, in explants of mare's endometrium, (i) the ABAH capacity to inhibit MPO-induced collagen type I (COL1) expression; and (ii) the action of MPO and ABAH on the expression and gelatinolytic activity of MMP-2/-9. Explants retrieved from the endometrium of mares in follicular or mid-luteal phases were treated with MPO, ABAH, or their combination, for 24 or 48 h. The qPCR analysis measured the transcription of , , and . Western blot and zymography were performed to evaluate COL1 protein relative abundance and gelatinolytic activity of MMP-2/-9, respectively. Myeloperoxidase elevated COL1 relative protein abundance at both treatment times in follicular phase ( < 0.05). The capacity of ABAH to inhibit MPO-induced COL1 was detected in follicular phase at 48 h ( < 0.05). The gelatinolytic activity of activated MMP-2 augmented in mid-luteal phase at 24 h after MPO treatment, but it was reduced with MPO+ABAH treatment. The activity of MMP-9 active form augmented in MPO-treated explants. However, this effect was inhibited by ABAH in the follicular phase at 48 h ( < 0.05). By inhibiting the pro-fibrotic effects of MPO, it might be possible to reduce the development of endometrosis. Metallopeptidase-2 might be involved in an acute response to MPO in the mid-luteal phase, while MMP-9 might be implicated in a prolonged exposition to MPO in the follicular phase.
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Publication Date: 2021-01-16 PubMed ID: 33467081PubMed Central: PMC7830995DOI: 10.3390/ani11010208Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research investigates how inhibiting a certain enzyme found in horse endometrium cells affects collagen production and the activity of proteins involved in maintaining the structure of tissues. The results suggest that this enzyme might play a role in the development of a common equine uterine disease, and that inhibiting it could potentially help reduce the risk of this disease.

Objective of the Research

  • The research aimed to understand how the inhibition of Myeloperoxidase (MPO), an enzyme found in the endometrium of mares associated with the disease endometrosis, affects the production of collagen and the activity of proteins known as metallopeptidases (MMPs). MPO can be inhibited by a substance known as 4-aminobenzoic acid hydrazide (ABAH), and the researchers were interested in how this might affect the behavior of cells in the endometrium.

Methodology of the Research

  • The researchers collected samples from the endometrium of mares and treated them with MPO, ABAH, or a combination of both. They carried out this process over 24 or 48 hours and then analyzed the samples using quantitative PCR (a method to measure gene expression), Western blot (a technique to identify specific proteins in a sample), and zymography (a technique to detect enzymatic activity).

Findings of the Research

  • The researchers found that MPO increased the relative abundance of collagen protein (COL1) in the samples, particularly at both treatment times in the follicular phase, a certain stage of the mares’ reproductive cycle.
  • They also found that ABAH was able to inhibit this increase in collagen production caused by MPO after 48 hours in the follicular phase.
  • Moreover, the study revealed that the activity of MMPs was increased after treating the samples with MPO. Specifically, they recorded an increase in the gelatinolytic activity (ability to break down gelatin) of MMP-2 and MMP-9, two specific types of metallopeptidases. However, the combination of MPO and ABAH reduced this effect.
  • Finally, they found that the activity of the active form of MMP-9 increased when the explants were treated with MPO. This effect was also inhibited by ABAH at 48 hours in the follicular phase.

Implications of the Research

  • The findings suggest that MPO contributes to the progression of endometriosis, a common equine uterine disease, by stimulating collagen production and increasing the activity of MMPs. Inhibiting MPO using ABAH could potentially help reduce the risk of this disease.
  • The results also indicate that different MMPs may play a role in the body’s response to the presence of MPO at different stages of the mares’ reproductive cycle. This suggests that the MPO-MMP interaction could be a useful area for future research into the prevention and treatment of equine endometriosis.

Cite This Article

APA
Amaral A, Fernandes C, Rebordão MR, Szóstek-Mioduchowska A, Lukasik K, Pinto-Bravo P, Telo da Gama L, Jan Skarzynski D, Ferreira-Dias G. (2021). Myeloperoxidase Inhibition Decreases the Expression of Collagen and Metallopeptidase in Mare Endometria under In Vitro Conditions. Animals (Basel), 11(1), 208. https://doi.org/10.3390/ani11010208

Publication

Animals : an open access journal from MDPI
ISSN: 2076-2615
NlmUniqueID: 101635614
Country: Switzerland
Language: English
Volume: 11
Issue: 1
PII: 208

Researcher Affiliations

Amaral, Ana
  • CIISA-Centro de Investigação Interdisciplinar em Sanidade Animal, Departamento de Morfologia e Função, Faculdade de Medicina Veterinária, Universidade de Lisboa, 1300-477 Lisboa, Portugal.
Fernandes, Carina
  • CIISA-Centro de Investigação Interdisciplinar em Sanidade Animal, Departamento de Morfologia e Função, Faculdade de Medicina Veterinária, Universidade de Lisboa, 1300-477 Lisboa, Portugal.
Rebordão, Maria Rosa
  • CIISA-Centro de Investigação Interdisciplinar em Sanidade Animal, Departamento de Morfologia e Função, Faculdade de Medicina Veterinária, Universidade de Lisboa, 1300-477 Lisboa, Portugal.
  • Polytechnic of Coimbra, Coimbra Agriculture School, Bencanta, 3045-601 Coimbra, Portugal.
Szóstek-Mioduchowska, Anna
  • Institute of Animal Reproduction and Food Research, Polish Academy of Science, 10-748 Olsztyn, Poland.
Lukasik, Karolina
  • Institute of Animal Reproduction and Food Research, Polish Academy of Science, 10-748 Olsztyn, Poland.
Pinto-Bravo, Pedro
  • Polytechnic of Coimbra, Coimbra Agriculture School, Bencanta, 3045-601 Coimbra, Portugal.
Telo da Gama, Luís
  • CIISA-Centro de Investigação Interdisciplinar em Sanidade Animal, Departamento de Morfologia e Função, Faculdade de Medicina Veterinária, Universidade de Lisboa, 1300-477 Lisboa, Portugal.
Jan Skarzynski, Dariusz
  • Institute of Animal Reproduction and Food Research, Polish Academy of Science, 10-748 Olsztyn, Poland.
Ferreira-Dias, Graça
  • CIISA-Centro de Investigação Interdisciplinar em Sanidade Animal, Departamento de Morfologia e Função, Faculdade de Medicina Veterinária, Universidade de Lisboa, 1300-477 Lisboa, Portugal.

Conflict of Interest Statement

The authors declare no conflict of interest.

References

This article includes 65 references
  1. Nicholls SJ, Hazen SL. Myeloperoxidase and cardiovascular disease.. Arterioscler Thromb Vasc Biol 2005 Jun;25(6):1102-11.
    doi: 10.1161/01.ATV.0000163262.83456.6dpubmed: 15790935google scholar: lookup
  2. Liu WQ, Zhang YZ, Wu Y, Zhang JJ, Li TB, Jiang T, Xiong XM, Luo XJ, Ma QL, Peng J. Myeloperoxidase-derived hypochlorous acid promotes ox-LDL-induced senescence of endothelial cells through a mechanism involving β-catenin signaling in hyperlipidemia.. Biochem Biophys Res Commun 2015 Nov 27;467(4):859-65.
    doi: 10.1016/j.bbrc.2015.10.053pubmed: 26474698google scholar: lookup
  3. Klebanoff SJ. Myeloperoxidase: friend and foe.. J Leukoc Biol 2005 May;77(5):598-625.
    doi: 10.1189/jlb.1204697pubmed: 15689384google scholar: lookup
  4. Teng TS, Ji AL, Ji XY, Li YZ. Neutrophils and Immunity: From Bactericidal Action to Being Conquered.. J Immunol Res 2017;2017:9671604.
    doi: 10.1155/2017/9671604pmc: PMC5337389pubmed: 28299345google scholar: lookup
  5. Brinkmann V, Reichard U, Goosmann C, Fauler B, Uhlemann Y, Weiss DS, Weinrauch Y, Zychlinsky A. Neutrophil extracellular traps kill bacteria.. Science 2004 Mar 5;303(5663):1532-5.
    doi: 10.1126/science.1092385pubmed: 15001782google scholar: lookup
  6. Segal AW. How neutrophils kill microbes.. Annu Rev Immunol 2005;23:197-223.
    doi: 10.1146/annurev.immunol.23.021704.115653pmc: PMC2092448pubmed: 15771570google scholar: lookup
  7. Nauseef WM. Myeloperoxidase in human neutrophil host defence.. Cell Microbiol 2014 Aug;16(8):1146-55.
    doi: 10.1111/cmi.12312pmc: PMC4301731pubmed: 24844117google scholar: lookup
  8. Kotilainen T, Huhtinen M, Katila T. Sperm-induced leukocytosis in the equine uterus.. Theriogenology 1994 Feb 2;41(3):629-36.
    doi: 10.1016/0093-691X(94)90173-Gpubmed: 16727418google scholar: lookup
  9. Katila T. Onset and Duration of Uterine Inflammatory Response of Mares after Insemination with Fresh Semen. Biol. Reprod. 1995;52:515–517.
    doi: 10.1093/biolreprod/52.monograph_series1.515google scholar: lookup
  10. Troedsson MH, Liu IK, Thurmond M. Function of uterine and blood-derived polymorphonuclear neutrophils in mares susceptible and resistant to chronic uterine infection: phagocytosis and chemotaxis.. Biol Reprod 1993 Sep;49(3):507-14.
    doi: 10.1095/biolreprod49.3.507pubmed: 8399843google scholar: lookup
  11. Troedsson MH. Breeding-induced endometritis in mares.. Vet Clin North Am Equine Pract 2006 Dec;22(3):705-12.
    doi: 10.1016/j.cveq.2006.07.003pubmed: 17129798google scholar: lookup
  12. Alghamdi AS, Foster DN. Seminal DNase frees spermatozoa entangled in neutrophil extracellular traps.. Biol Reprod 2005 Dec;73(6):1174-81.
    doi: 10.1095/biolreprod.105.045666pubmed: 16107606google scholar: lookup
  13. Alghamdi AS, Lovaas BJ, Bird SL, Lamb GC, Rendahl AK, Taube PC, Foster DN. Species-specific interaction of seminal plasma on sperm-neutrophil binding.. Anim Reprod Sci 2009 Sep;114(4):331-44.
    doi: 10.1016/j.anireprosci.2008.10.015pubmed: 19081210google scholar: lookup
  14. Rebordão MR, Carneiro C, Alexandre-Pires G, Brito P, Pereira C, Nunes T, Galvão A, Leitão A, Vilela C, Ferreira-Dias G. Neutrophil extracellular traps formation by bacteria causing endometritis in the mare.. J Reprod Immunol 2014 Dec;106:41-9.
    doi: 10.1016/j.jri.2014.08.003pubmed: 25218891google scholar: lookup
  15. Manda A, Pruchniak MP, Araźna M, Demkow UA. Neutrophil extracellular traps in physiology and pathology.. Cent Eur J Immunol 2014;39(1):116-21.
    doi: 10.5114/ceji.2014.42136pmc: PMC4439979pubmed: 26155111google scholar: lookup
  16. Parrilla-Hernandez S, Ponthier J, Franck TY, Serteyn DD, Deleuze SC. High concentrations of myeloperoxidase in the equine uterus as an indicator of endometritis.. Theriogenology 2014 Apr 15;81(7):936-40.
    doi: 10.1016/j.theriogenology.2014.01.011pubmed: 24565475google scholar: lookup
  17. Nazhat SA, Kitahara G, Kozuka N, Mido S, Sadawy M, Ali HE, Osawa T. Associations of periparturient plasma biochemical parameters, endometrial leukocyte esterase and myeloperoxidase, and bacterial detection with clinical and subclinical endometritis in postpartum dairy cows.. J Vet Med Sci 2018 Feb 20;80(2):302-310.
    doi: 10.1292/jvms.17-0478pmc: PMC5836768pubmed: 29332864google scholar: lookup
  18. Rebordão MR, Amaral A, Lukasik K, Szóstek-Mioduchowska A, Pinto-Bravo P, Galvão A, Skarzynski DJ, Ferreira-Dias G. Constituents of neutrophil extracellular traps induce in vitro collagen formation in mare endometrium.. Theriogenology 2018 Jun;113:8-18.
    doi: 10.1016/j.theriogenology.2018.02.001pubmed: 29452855google scholar: lookup
  19. Amaral A, Fernandes C, Lukasik K, Szóstek-Mioduchowska A, Baclawska A, Rebordão MR, Aguiar-Silva J, Pinto-Bravo P, Skarzynski DJ, Ferreira-Dias G. Elastase inhibition affects collagen transcription and prostaglandin secretion in mare endometrium during the estrous cycle.. Reprod Domest Anim 2018 Sep;53 Suppl 2:66-69.
    doi: 10.1111/rda.13258pubmed: 30238664google scholar: lookup
  20. Amaral A, Fernandes C, Rebordão MR, Szóstek-Mioduchowska A, Lukasik K, Gawronska-Kozak B, Telo da Gama L, Skarzynski DJ, Ferreira-Dias G. The In Vitro Inhibitory Effect of Sivelestat on Elastase Induced Collagen and Metallopeptidase Expression in Equine Endometrium.. Animals (Basel) 2020 May 16;10(5).
    doi: 10.3390/ani10050863pmc: PMC7278485pubmed: 32429399google scholar: lookup
  21. Amaral A, Fernandes C, Morazzo S, Rebordão MR, Szóstek-Mioduchowska A, Lukasik K, Gawronska-Kozak B, Telo da Gama L, Skarzynski DJ, Ferreira-Dias G. The Inhibition of Cathepsin G on Endometrial Explants With Endometrosis in the Mare.. Front Vet Sci 2020;7:582211.
    doi: 10.3389/fvets.2020.582211pmc: PMC7661753pubmed: 33195599google scholar: lookup
  22. Kenney R.M. The aetiology, diagnosis, and classification of chronic degenerative endometritis. In: Hughes J.P., editor. Workshop on Equine Endometritis. Volume 125. Newmarket Press; New York, NY, USA: 1992. p. 186.
  23. Hoffmann C, Ellenberger C, Mattos RC, Aupperle H, Dhein S, Stief B, Schoon HA. The equine endometrosis: new insights into the pathogenesis.. Anim Reprod Sci 2009 Apr;111(2-4):261-78.
    doi: 10.1016/j.anireprosci.2008.03.019pubmed: 18468817google scholar: lookup
  24. Sagel SD, Wagner BD, Anthony MM, Emmett P, Zemanick ET. Sputum biomarkers of inflammation and lung function decline in children with cystic fibrosis.. Am J Respir Crit Care Med 2012 Nov 1;186(9):857-65.
    doi: 10.1164/rccm.201203-0507OCpmc: PMC3530222pubmed: 22904182google scholar: lookup
  25. Sly PD, Gangell CL, Chen L, Ware RS, Ranganathan S, Mott LS, Murray CP, Stick SM. Risk factors for bronchiectasis in children with cystic fibrosis.. N Engl J Med 2013 May 23;368(21):1963-70.
    doi: 10.1056/NEJMoa1301725pubmed: 23692169google scholar: lookup
  26. Beard M.R, Jones B.E. Hepatitis C Virus and Oxidative Stress: A Dangerous Liaison. Future Virol. 2006;1:223–232.
    doi: 10.2217/17460794.1.2.223google scholar: lookup
  27. Pulli B, Ali M, Iwamoto Y, Zeller MW, Schob S, Linnoila JJ, Chen JW. Myeloperoxidase-Hepatocyte-Stellate Cell Cross Talk Promotes Hepatocyte Injury and Fibrosis in Experimental Nonalcoholic Steatohepatitis.. Antioxid Redox Signal 2015 Dec 1;23(16):1255-69.
    doi: 10.1089/ars.2014.6108pmc: PMC4677570pubmed: 26058518google scholar: lookup
  28. Kettle AJ, Gedye CA, Winterbourn CC. Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide.. Biochem J 1997 Jan 15;321 ( Pt 2)(Pt 2):503-8.
    doi: 10.1042/bj3210503pmc: PMC1218097pubmed: 9020887google scholar: lookup
  29. Lazarević-Pasti T, Leskovac A, Vasić V. Myeloperoxidase Inhibitors as Potential Drugs.. Curr Drug Metab 2015;16(3):168-90.
    doi: 10.2174/138920021603150812120640pubmed: 26279325google scholar: lookup
  30. Kim H, Wei Y, Lee JY, Wu Y, Zheng Y, Moskowitz MA, Chen JW. Myeloperoxidase Inhibition Increases Neurogenesis after Ischemic Stroke.. J Pharmacol Exp Ther 2016 Nov;359(2):262-272.
    doi: 10.1124/jpet.116.235127pmc: PMC5074486pubmed: 27550713google scholar: lookup
  31. Hair PS, Sass LA, Krishna NK, Cunnion KM. Inhibition of Myeloperoxidase Activity in Cystic Fibrosis Sputum by Peptide Inhibitor of Complement C1 (PIC1).. PLoS One 2017;12(1):e0170203.
    doi: 10.1371/journal.pone.0170203pmc: PMC5279725pubmed: 28135312google scholar: lookup
  32. Vandooren J, Van den Steen PE, Opdenakker G. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decade.. Crit Rev Biochem Mol Biol 2013 May-Jun;48(3):222-72.
    doi: 10.3109/10409238.2013.770819pubmed: 23547785google scholar: lookup
  33. Wang X, Khalil RA. Matrix Metalloproteinases, Vascular Remodeling, and Vascular Disease.. Adv Pharmacol 2018;81:241-330.
    doi: 10.1016/bs.apha.2017.08.002pmc: PMC5765875pubmed: 29310800google scholar: lookup
  34. Aresu L, Benali S, Giannuzzi D, Mantovani R, Castagnaro M, Falomo ME. The role of inflammation and matrix metalloproteinases in equine endometriosis.. J Vet Sci 2012 Jun;13(2):171-7.
    doi: 10.4142/jvs.2012.13.2.171pmc: PMC3386342pubmed: 22705739google scholar: lookup
  35. Centeno L.A.M., Bastos H.B.A., Bueno V.L.C., Trentin J.M., Fiorenza M.F., Fiala-Rechsteiner S., Kretzmann N.A., Mattos R.C., Rubin M.I.B. Gene Expression of MMP-1, MMP-2 and TNF-α in the Endometrium of Mares With Different Degrees of Fibrosis. J. Equine Vet. Sci. 2018;66:143–144.
    doi: 10.1016/j.jevs.2018.05.182google scholar: lookup
  36. Walter I, Handler J, Miller I, Aurich C. Matrix metalloproteinase 2 (MMP-2) and tissue transglutaminase (TG 2) are expressed in periglandular fibrosis in horse mares with endometrosis.. Histol Histopathol 2005 Oct;20(4):1105-13.
    doi: 10.14670/HH-20.1105pubmed: 16136493google scholar: lookup
  37. Szóstek-Mioduchowska AZ, Baclawska A, Okuda K, Skarzynski DJ. Effect of proinflammatory cytokines on endometrial collagen and metallopeptidase expression during the course of equine endometrosis.. Cytokine 2019 Nov;123:154767.
    doi: 10.1016/j.cyto.2019.154767pubmed: 31265984google scholar: lookup
  38. Szóstek-Mioduchowska A, Słowińska M, Pacewicz J, Skarzynski DJ, Okuda K. Matrix metallopeptidase expression and modulation by transforming growth factor-β1 in equine endometrosis.. Sci Rep 2020 Jan 24;10(1):1119.
    doi: 10.1038/s41598-020-58109-0pmc: PMC6981191pubmed: 31980722google scholar: lookup
  39. Szóstek-Mioduchowska AZ, Baclawska A, Rebordão MR, Ferreira-Dias G, Skarzynski DJ. Prostaglandins effect on matrix metallopeptidases and collagen in mare endometrial fibroblasts.. Theriogenology 2020 Sep 1;153:74-84.
    doi: 10.1016/j.theriogenology.2020.04.040pubmed: 32442743google scholar: lookup
  40. Roberto da Costa RP, Ferreira-Dias G, Mateus L, Korzekwa A, Andronowska A, Platek R, Skarzynski DJ. Endometrial nitric oxide production and nitric oxide synthases in the equine endometrium: Relationship with microvascular density during the estrous cycle.. Domest Anim Endocrinol 2007 May;32(4):287-302.
    doi: 10.1016/j.domaniend.2006.03.007pubmed: 16647832google scholar: lookup
  41. Rebordão MR, Amaral A, Lukasik K, Szóstek-Mioduchowska A, Pinto-Bravo P, Galvão A, Skarzynski DJ, Ferreira-Dias G. Impairment of the antifibrotic prostaglandin E(2) pathway may influence neutrophil extracellular traps-induced fibrosis in the mare endometrium.. Domest Anim Endocrinol 2019 Apr;67:1-10.
    doi: 10.1016/j.domaniend.2018.10.004pubmed: 30522057google scholar: lookup
  42. Kenney R.M, Doig P.A. Equine endometrial biopsy. In: Current Therapy in Theriogenology 2: Diagnosis, Treatment, and Prevention of Reproductive Diseases in Small and Large Animals. 2nd ed. David A.M., editor. W.B. Saunders; Philadelphia, PA, USA: 1986. pp. 723–729.
  43. Nash D, Lane E, Herath S, Sheldon IM. Endometrial explant culture for characterizing equine endometritis.. Am J Reprod Immunol 2008 Feb;59(2):105-17.
    doi: 10.1111/j.1600-0897.2007.00548.xpubmed: 18211536google scholar: lookup
  44. Szóstek AZ, Lukasik K, Galvão AM, Ferreira-Dias GM, Skarzynski DJ. Impairment of the interleukin system in equine endometrium during the course of endometrosis.. Biol Reprod 2013 Oct;89(4):79.
    doi: 10.1095/biolreprod.113.109447pubmed: 23946535google scholar: lookup
  45. Forbes LV, Sjögren T, Auchère F, Jenkins DW, Thong B, Laughton D, Hemsley P, Pairaudeau G, Turner R, Eriksson H, Unitt JF, Kettle AJ. Potent reversible inhibition of myeloperoxidase by aromatic hydroxamates.. J Biol Chem 2013 Dec 20;288(51):36636-47.
    doi: 10.1074/jbc.M113.507756pmc: PMC3868775pubmed: 24194519google scholar: lookup
  46. Dheda K, Huggett JF, Bustin SA, Johnson MA, Rook G, Zumla A. Validation of housekeeping genes for normalizing RNA expression in real-time PCR.. Biotechniques 2004 Jul;37(1):112-4, 116, 118-9.
    doi: 10.2144/04371RR03pubmed: 15283208google scholar: lookup
  47. Zhao S, Fernald RD. Comprehensive algorithm for quantitative real-time polymerase chain reaction.. J Comput Biol 2005 Oct;12(8):1047-64.
    doi: 10.1089/cmb.2005.12.1047pmc: PMC2716216pubmed: 16241897google scholar: lookup
  48. Posch A, Kohn J, Oh K, Hammond M, Liu N. V3 stain-free workflow for a practical, convenient, and reliable total protein loading control in western blotting.. J Vis Exp 2013 Dec 30;(82):50948.
    doi: 10.3791/50948pmc: PMC4094170pubmed: 24429481google scholar: lookup
  49. Manuel JA, Gawronska-Kozak B. Matrix metalloproteinase 9 (MMP-9) is upregulated during scarless wound healing in athymic nude mice.. Matrix Biol 2006 Oct;25(8):505-14.
    doi: 10.1016/j.matbio.2006.07.008pubmed: 17010584google scholar: lookup
  50. Raykin J, Snider E, Bheri S, Mulvihill J, Ethier CR. A modified gelatin zymography technique incorporating total protein normalization.. Anal Biochem 2017 Mar 15;521:8-10.
    doi: 10.1016/j.ab.2017.01.003pubmed: 28069453google scholar: lookup
  51. Aurich C. Reproductive cycles of horses.. Anim Reprod Sci 2011 Apr;124(3-4):220-8.
    doi: 10.1016/j.anireprosci.2011.02.005pubmed: 21377299google scholar: lookup
  52. Marth CD, Firestone SM, Glenton LY, Browning GF, Young ND, Krekeler N. Oestrous cycle-dependent equine uterine immune response to induced infectious endometritis.. Vet Res 2016 Nov 8;47(1):110.
    doi: 10.1186/s13567-016-0398-xpmc: PMC5101692pubmed: 27825391google scholar: lookup
  53. Ferreira-Dias G, Nequin LG, King SS. Influence of estrous cycle stage on adhesion of Streptococcus zooepidemicus to equine endometrium.. Am J Vet Res 1994 Jul;55(7):1028-31.
    pubmed: 7978620
  54. Gebhardt S, Merkl M, Herbach N, Wanke R, Handler J, Bauersachs S. Exploration of global gene expression changes during the estrous cycle in equine endometrium.. Biol Reprod 2012 Jun;87(6):136.
    doi: 10.1095/biolreprod.112.103226pubmed: 23077167google scholar: lookup
  55. Stenbäck F. Collagen type III formation and distribution in the uterus: effects of hormones and neoplasm development.. Oncology 1989;46(5):326-34.
    doi: 10.1159/000226742pubmed: 2674809google scholar: lookup
  56. Chandler JD, Margaroli C, Horati H, Kilgore MB, Veltman M, Liu HK, Taurone AJ, Peng L, Guglani L, Uppal K, Go YM, Tiddens HAWM, Scholte BJ, Tirouvanziam R, Jones DP, Janssens HM. Myeloperoxidase oxidation of methionine associates with early cystic fibrosis lung disease.. Eur Respir J 2018 Oct;52(4).
    doi: 10.1183/13993003.01118-2018pmc: PMC7034951pubmed: 30190273google scholar: lookup
  57. Friedrichs K, Baldus S, Klinke A. Fibrosis in Atrial Fibrillation - Role of Reactive Species and MPO.. Front Physiol 2012;3:214.
    doi: 10.3389/fphys.2012.00214pmc: PMC3379725pubmed: 22723783google scholar: lookup
  58. Szóstek-Mioduchowska AZ, Lukasik K, Skarzynski DJ, Okuda K. Effect of transforming growth factor -β1 on α-smooth muscle actin and collagen expression in equine endometrial fibroblasts.. Theriogenology 2019 Jan 15;124:9-17.
    doi: 10.1016/j.theriogenology.2018.10.005pubmed: 30321755google scholar: lookup
  59. Burner U, Obinger C, Paumann M, Furtmüller PG, Kettle AJ. Transient and steady-state kinetics of the oxidation of substituted benzoic acid hydrazides by myeloperoxidase.. J Biol Chem 1999 Apr 2;274(14):9494-502.
    doi: 10.1074/jbc.274.14.9494pubmed: 10092633google scholar: lookup
  60. Fabian E, Gomes C, Birk B, Williford T, Hernandez TR, Haase C, Zbranek R, van Ravenzwaay B, Landsiedel R. In vitro-to-in vivo extrapolation (IVIVE) by PBTK modeling for animal-free risk assessment approaches of potential endocrine-disrupting compounds.. Arch Toxicol 2019 Feb;93(2):401-416.
    doi: 10.1007/s00204-018-2372-zpubmed: 30552464google scholar: lookup
  61. Clippinger AJ, Ahluwalia A, Allen D, Bonner JC, Casey W, Castranova V, David RM, Halappanavar S, Hotchkiss JA, Jarabek AM, Maier M, Polk W, Rothen-Rutishauser B, Sayes CM, Sayre P, Sharma M, Stone V. Expert consensus on an in vitro approach to assess pulmonary fibrogenic potential of aerosolized nanomaterials.. Arch Toxicol 2016 Jul;90(7):1769-83.
    doi: 10.1007/s00204-016-1717-8pmc: PMC4894935pubmed: 27121469google scholar: lookup
  62. Harvey A, Montezano AC, Lopes RA, Rios F, Touyz RM. Vascular Fibrosis in Aging and Hypertension: Molecular Mechanisms and Clinical Implications.. Can J Cardiol 2016 May;32(5):659-68.
    doi: 10.1016/j.cjca.2016.02.070pmc: PMC4906153pubmed: 27118293google scholar: lookup
  63. Nascimento GC, Rizzi E, Gerlach RF, Leite-Panissi CR. Expression of MMP-2 and MMP-9 in the rat trigeminal ganglion during the development of temporomandibular joint inflammation.. Braz J Med Biol Res 2013 Nov;46(11):956-967.
    doi: 10.1590/1414-431X20133138pmc: PMC3854335pubmed: 24270905google scholar: lookup
  64. Accorsi-Mendonça T, Silva EJ, Marcaccini AM, Gerlach RF, Duarte KM, Pardo AP, Line SR, Zaia AA. Evaluation of gelatinases, tissue inhibitor of matrix metalloproteinase-2, and myeloperoxidase protein in healthy and inflamed human dental pulp tissue.. J Endod 2013 Jul;39(7):879-82.
    doi: 10.1016/j.joen.2012.11.011pubmed: 23791255google scholar: lookup
  65. Spallarossa P, Garibaldi S, Barisione C, Ghigliotti G, Altieri P, Tracchi I, Fabbi P, Barsotti A, Brunelli C. Postprandial serum induces apoptosis in endothelial cells: Role of polymorphonuclear-derived myeloperoxidase and metalloproteinase-9 activity.. Atherosclerosis 2008 Jun;198(2):458-67.
    doi: 10.1016/j.atherosclerosis.2007.11.030pubmed: 18177875google scholar: lookup

Citations

This article has been cited 5 times.
  1. Amaral A, Cebola N, Szóstek-Mioduchowska A, Rebordão MR, Kordowitzki P, Skarzynski D, Ferreira-Dias G. Inhibition of Myeloperoxidase Pro-Fibrotic Effect by Noscapine in Equine Endometrium.. Int J Mol Sci 2023 Feb 10;24(4).
    doi: 10.3390/ijms24043593pubmed: 36835008google scholar: lookup
  2. Parrilla Hernández S, Franck T, Munaut C, Feyereisen É, Piret J, Farnir F, Reigner F, Barrière P, Deleuze S. Characterization of Myeloperoxidase in the Healthy Equine Endometrium.. Animals (Basel) 2023 Jan 21;13(3).
    doi: 10.3390/ani13030375pubmed: 36766264google scholar: lookup
  3. Amaral A, Fernandes C, Szóstek-Mioduchowska A, Lukasik K, Rebordão MR, Pinto-Bravo P, Skarzynski DJ, Ferreira-Dias G. The Inhibitory Effect of Noscapine on the In Vitro Cathepsin G-Induced Collagen Expression in Equine Endometrium.. Life (Basel) 2021 Oct 19;11(10).
    doi: 10.3390/life11101107pubmed: 34685478google scholar: lookup
  4. Fantini P, Jiménez R, Vilés K, Iborra A, Palhares MS, Catalán J, Prades M, Miró J. Simple Tube Centrifugation Method for Platelet-Rich Plasma (PRP) Preparation in Catalonian Donkeys as a Treatment of Endometritis-Endometrosis.. Animals (Basel) 2021 Oct 9;11(10).
    doi: 10.3390/ani11102918pubmed: 34679937google scholar: lookup
  5. Amaral A, Fernandes C, Szóstek-Mioduchowska A, Rebordão MR, Skarzynski DJ, Ferreira-Dias G. Noscapine Acts as a Protease Inhibitor of In Vitro Elastase-Induced Collagen Deposition in Equine Endometrium.. Int J Mol Sci 2021 May 19;22(10).
    doi: 10.3390/ijms22105333pubmed: 34069423google scholar: lookup
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