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Current Proteomics

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ISSN (Print): 1570-1646
ISSN (Online): 1875-6247

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Research Article

A Motif in Metallopeptidase Inhibitor Decreases Effectively the Activity of Macrophage Metalloproteinases

Author(s): Golnaz Esfandiari, Ghasem Ghasempour, Naser Kakavandi, Ali Akbar Soleimani, Borhan Rahimi Abkenar, Elham Bahraini, Mohammad Najafi* and Mohsen Khosravi

Volume 19, Issue 3, 2022

Published on: 01 April, 2022

Page: [256 - 261] Pages: 6

DOI: 10.2174/1570164619666220304162545

Price: $65

Abstract

Objective: The tissue remodeling process and cellular migration relate to the activities of Matrix Metalloproteinases (MMPs). The aim of this study was to investigate the effects of a predicted motif from TIMPs on the MMP-2 and MMP-9 activities secreted from the differentiated macrophages.

Materials and Methods: The monocytes were isolated from the healthy individuals by RosetteSep kit and were differentiated into macrophages using M-CSF. A 4-amino acid motif (TCAP) was predicted using bioinformatics tools. Zymography technique was applied for the measurement of MMP activities. The docking studies were also investigated between MMPs, tetrapeptide, and Batimastat.

Results: The TCAP inhibited significantly the differentiated macrophage MMP-2 and MMP-9 activities (p=0.0001and p=0.01, respectively). The docking results suggested that some MMP amino acids are involved with both tetrapeptide (TCAP) and Batimastat,

Conclusion: The data showed that the small motif (TCAP) of TIMPs inhibits effectively the MMP- 2 activity.

Keywords: MMP-2, MMP-9, macrophage, TIMP, prediction, motif.

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[1]
Alaseem, A.; Alhazzani, K.; Dondapati, P.; Alobid, S.; Bishayee, A.; Rathinavelu, A. Matrix metalloproteinases: A challenging paradigm of cancer management. In: Semin Cancer Biol;, 2019, 100-115.
[PMID: 29155240]
[2]
Miguel, A.F.; Mello, F.W.; Melo, G.; Rivero, E.R.J.H. neck, Association between immunohistochemical expression of matrix metallopro-teinases and metastasis in oral squamous cell carcinoma: Systematic review and meta-analysis. Head Neck, 2020, 42(3), 569-584.
[PMID: 31750584]
[3]
Moore, C.S.; Crocker, S.J. An alternate perspective on the roles of TIMPs and MMPs in pathology. Am. J. Pathol., 2012, 180(1), 12-16.
[PMID: 22033229]
[4]
Raffetto, J.D.J.S.C. Pathophysiology of chronic venous disease and venous ulcers. Surg. Clin. North Am., 2018, 98(2), 337-347.
[http://dx.doi.org/10.1016/j.suc.2017.11.002] [PMID: 29502775]
[5]
Chen, Y.; Peng, W.; Raffetto, J.D.; Khalil, R.A. Matrix metalloproteinases in remodeling of lower extremity veins and chronic venous dis-ease. Prog. Mol. Biol. Transl. Sci., 2017, 147, 267-299.
[http://dx.doi.org/10.1016/bs.pmbts.2017.02.003] [PMID: 28413031]
[6]
Chang, J.W.; Maeng, Y-H.; Kim, S.W. Expression of matrix metalloproteinase-2 and -13 and tissue inhibitor of metalloproteinase-4 in varicose veins. Korean J. Thorac. Cardiovasc. Surg., 2011, 44(6), 387-391.
[http://dx.doi.org/10.5090/kjtcs.2011.44.6.387] [PMID: 22324022]
[7]
Chirco, R.; Liu, X-W.; Jung, K-K.; Kim, H-R.C.J.C.; Reviews, M. Novel functions of TIMPs in cell signaling. Cancer Metastasis Rev., 2006, 25(1), 99-113.
[http://dx.doi.org/10.1007/s10555-006-7893-x] [PMID: 16680576]
[8]
Saito, S.; Trovato, M.J.; You, R.; Lal, B.K.; Fasehun, F.; Padberg, F.T., Jr; Hobson, R.W., II; Durán, W.N.; Pappas, P.J. Role of matrix metalloproteinases 1, 2, and 9 and tissue inhibitor of matrix metalloproteinase-1 in chronic venous insufficiency. J. Vasc. Surg., 2001, 34(5), 930-938.
[http://dx.doi.org/10.1067/mva.2001.119503] [PMID: 11700497]
[9]
Chen, C.; Yang, X.; Fang, H.; Hou, X. Design, synthesis and preliminary bioactivity evaluations of 8-hydroxyquinoline derivatives as matrix metalloproteinase (MMP) inhibitors. Eur. J. Med. Chem., 2019, 181, 111563.
[http://dx.doi.org/10.1016/j.ejmech.2019.111563] [PMID: 31415980]
[10]
Hassanpour, P.; Amirfarhangi, A.; Hosseini-Fard, S.R.; Yarnazari, A.; Najafi, M. Interleukin 6 may be related to indoleamine 2,3-dioxygense function in M2 macrophages treated with small dense LDL particles. Gene, 2017, 626, 442-446.
[http://dx.doi.org/10.1016/j.gene.2017.05.063] [PMID: 28596088]
[11]
Yarnazari, A.; Hassanpour, P.; Hosseini-Fard, S.R.; Amirfarhangi, A.; Najafi, M.; Targets, H.D-D. The sdLDL reduces MRC1 expression level and secretion of Histamin e in differentiated M2-macrophages from patients with coronary artery stenosis. Cardiovasc. Hematol. Disord. Drug Targets, 2017, 17(1), 28-32.
[http://dx.doi.org/10.2174/1871529X17666170106095554] [PMID: 28059035]
[12]
Esfandiari, G.; Biranvand, A.S.; Poursaleh, A.; Kakavandi, N.; Fattahi, F.; Ghasempour, G.; Bahraini, E.; Khosravi, M.; Najafi, M. Effect of a peptide construct on differentiated macrophage MMP-2 and MMP-9 levels of varicose patients. Curr. Pharm. Des., 2019, 25(40), 4303-4309.
[http://dx.doi.org/10.2174/1381612825666191029105203] [PMID: 31663473]
[13]
Castro-Ferreira, R.; Cardoso, R.; Leite-Moreira, A.; Mansilha, A. The role of endothelial dysfunction and inflammation in chronic venous disease. Ann. Vasc. Surg., 2018, 46, 380-393.
[http://dx.doi.org/10.1016/j.avsg.2017.06.131] [PMID: 28688874]
[14]
Raffetto, J.D.; Barros, Y.V.; Wells, A.K.; Khalil, R.A.J.J.S.R. MMP-2 induced vein relaxation via inhibition of [Ca2+]e-dependent mecha-nisms of venous smooth muscle contraction. Role of RGD peptides. J. Surg. Res., 2010, 159(2), 755-764.
[http://dx.doi.org/10.1016/j.jss.2008.09.022] [PMID: 19482300]
[15]
Raffetto, J.D.; Ross, R.L.; Khalil, R.A. Matrix metalloproteinase 2-induced venous dilation via hyperpolarization and activation of K+ channels: relevance to varicose vein formation. J. Vasc. Surg., 2007, 45(2), 373-380.
[http://dx.doi.org/10.1016/j.jvs.2006.10.041] [PMID: 17264019]
[16]
Baker, A.H.; Edwards, D.R.; Murphy, G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J. Cell Sci., 2002, 115(Pt 19), 3719-3727.
[http://dx.doi.org/10.1242/jcs.00063] [PMID: 12235282]
[17]
Caimi, G.; Ferrara, F.; Montana, M.; Muratori, I.; Amato, C.; Canino, B.; Lo Presti, R.; Hopps, E. Behaviour of the plasma concentration of gelatinases and their tissue inhibitors in subjects with venous leg ulcers. Clin. Hemorheol. Microcirc., 2015, 60(3), 309-316.
[http://dx.doi.org/10.3233/CH-141863] [PMID: 25159491]
[18]
Sansilvestri-Morel, P.; Fioretti, F.; Rupin, A.; Senni, K.; Fabiani, J.N.; Godeau, G.; Verbeuren, T.J.J.C.S. Comparison of extracellular ma-trix in skin and saphenous veins from patients with varicose veins: does the skin reflect venous matrix changes? Clin. Sci. (Lond.), 2007, 112(4), 229-239.
[http://dx.doi.org/10.1042/CS20060170] [PMID: 17020541]
[19]
Chen, Q.; Jin, M.; Yang, F.; Zhu, J.; Xiao, Q.; Zhang, L. Matrix metalloproteinases: inflammatory regulators of cell behaviors in vascular formation and remodeling. Mediators Inflamm., 2013, 2013, 928315.
[http://dx.doi.org/10.1155/2013/928315]
[20]
Hu, J.; Van den Steen, P.E.; Sang, Q-X.A.; Opdenakker, G. Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nat. Rev. Drug Discov., 2007, 6(6), 480-498.
[http://dx.doi.org/10.1038/nrd2308] [PMID: 17541420]
[21]
Overall, C.M.; López-Otín, C. Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat. Rev. Cancer, 2002, 2(9), 657-672.
[http://dx.doi.org/10.1038/nrc884] [PMID: 12209155]
[22]
Zhong, Y.; Lu, Y-T.; Sun, Y.; Shi, Z-H.; Li, N-G.; Tang, Y-P.; Duan, J.A. Recent opportunities in matrix metalloproteinase inhibitor drug design for cancer. Expert Opin. Drug Discov., 2018, 13(1), 75-87.
[http://dx.doi.org/10.1080/17460441.2018.1398732] [PMID: 29088927]
[23]
Sagi, I.; Gaffney, J. Matrix metalloproteinase biology; Wiley Online Library, 2015.
[http://dx.doi.org/10.1002/9781118772287]
[24]
Koivunen, E.; Arap, W.; Valtanen, H.; Rainisalo, A.; Medina, O.P.; Heikkilä, P.; Kantor, C.; Gahmberg, C.G.; Salo, T.; Konttinen, Y.T.; Sorsa, T.; Ruoslahti, E.; Pasqualini, R. Tumor targeting with a selective gelatinase inhibitor. Nat. Biotechnol., 1999, 17(8), 768-774.
[http://dx.doi.org/10.1038/11703] [PMID: 10429241]
[25]
Ferry, G.; Boutin, J.A.; Atassi, G.; Fauchère, J.L.; Tucker, G.C. Selection of a histidine-containing inhibitor of gelatinases through decon-volution of combinatorial tetrapeptide libraries. Mol. Divers., 1997, 2(3), 135-146.
[http://dx.doi.org/10.1007/BF01682201] [PMID: 9238644]

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