Login Register Cart 0
Generic placeholder image

Current Enzyme Inhibition

Editor-in-Chief

ISSN (Print): 1573-4080
ISSN (Online): 1875-6662

Back
Journal Home About Journal Editorial Board Journal Insight Current Issue Volumes/Issues
Subscribe
Editorial

Inhibition of Perforin: A Potential Therapeutic Approach against Human Ailments

In Press, (this is not the final "Version of Record"). Available online 14 May, 2024
Author(s): Aman Rai and Rohit Bhatia*
Published on: 14 May, 2024

DOI: 10.2174/0115734080298673240424052128

Price: $95

Abstract

Not applicable

[1]
Lopez, J.A.; Susanto, O.; Jenkins, M.R. Perforin forms transient pores on the target cell plasma membrane to facilitate rapid access of granzymes during killer cell attack. Blood, 2013, 121(14), 2659-2668.
[http://dx.doi.org/10.1182/blood-2012-07-446146] [PMID: 23377437]
[2]
Seko, Y.; Shinkai, Y.; Kawasaki, A.; Yagita, H.; Okumura, K.; Yazaki, Y. Evidence of perforin‐mediated cardiac myocyte injury in acute murine myocarditis caused by coxsackie virus B3. J. Pathol., 1993, 170(1), 53-58.
[http://dx.doi.org/10.1002/path.1711700109] [PMID: 8392106]
[3]
Novais, F.O.; Carvalho, L.P.; Graff, J.W. Cytotoxic T cells mediate pathology and metastasis in cutaneous leishmaniasis. PLoS Pathog., 2013, 9(7), e1003504.
[http://dx.doi.org/10.1371/journal.ppat.1003504] [PMID: 23874205]
[4]
Spicer, J.A.; Huttunen, K.M.; Jose, J. Small molecule inhibitors of lymphocyte perforin as focused immunosuppressants for infection and autoimmunity. J. Med. Chem., 2022, 65(21), 14305-14325.
[http://dx.doi.org/10.1021/acs.jmedchem.2c01338] [PMID: 36263926]
[5]
Welz, M.; Eickhoff, S.; Abdullah, Z. Perforin inhibition protects from lethal endothelial damage during fulminant viral hepatitis. Nat. Commun., 2018, 9(1), 4805.
[http://dx.doi.org/10.1038/s41467-018-07213-x] [PMID: 30442932]
[6]
Gonzalez-Fierro, C.; Fonte, C.; Dufourd, E. Effects of a small-molecule perforin inhibitor in a mouse model of CD8 T cell–mediated neuroinflammation. Neurol. Neuroimmunol. Neuroinflamm., 2023, 10(4), e200117.
[http://dx.doi.org/10.1212/NXI.0000000000200117] [PMID: 37080596]
[7]
Gartlan, K.H.; Jaiswal, J.K.; Bull, M.R. Preclinical activity and pharmacokinetic/pharmacodynamic relationship for a series of novel benzenesulfonamide perforin inhibitors. ACS Pharmacol. Transl. Sci., 2022, 5(6), 429-439.
[http://dx.doi.org/10.1021/acsptsci.2c00009] [PMID: 35711815]
[8]
Gynther, M.; Pickering, D.S.; Spicer, J.A.; Denny, W.A.; Huttunen, K.M. Systemic and brain pharmacokinetics of perforin inhibitor prodrugs. Mol. Pharm., 2016, 13(7), 2484-2491.
[http://dx.doi.org/10.1021/acs.molpharmaceut.6b00217] [PMID: 27266990]
[9]
Jose, J.; Law, R.H.P.; Leung, E.W.W. Fragment-based and structure-guided discovery of perforin inhibitors. Eur. J. Med. Chem., 2023, 261, 115786.
[http://dx.doi.org/10.1016/j.ejmech.2023.115786] [PMID: 37716187]
[10]
Yagita, M.; Huang, C.L.; Umehara, H. A novel natural killer cell line (KHYG-1) from a patient with aggressive natural killer cell leukemia carrying a p53 point mutation. Leukemia, 2000, 14(5), 922-930.
[http://dx.doi.org/10.1038/sj.leu.2401769] [PMID: 10803526]
[11]
Klein, E.; Vánky, F.; Ben-Bassat, H. Properties of the K562 cell line, derived from a patient with chronic myeloid leukemia. Int. J. Cancer, 1976, 18(4), 421-431.
[http://dx.doi.org/10.1002/ijc.2910180405] [PMID: 789258]
[12]
Tampio, J.; Huttunen, J.; Montaser, A.; Huttunen, K.M. Targeting of perforin inhibitor into the brain parenchyma via a prodrug approach can decrease oxidative stress and neuroinflammation and improve cell survival. Mol. Neurobiol., 2020, 57(11), 4563-4577.
[http://dx.doi.org/10.1007/s12035-020-02045-7] [PMID: 32754897]
[13]
Spicer, J.A.; Lena, G.; Lyons, D.M. Exploration of a series of 5-arylidene-2-thioxoimidazolidin-4-ones as inhibitors of the cytolytic protein perforin. J. Med. Chem., 2013, 56(23), 9542-9555.
[http://dx.doi.org/10.1021/jm401604x] [PMID: 24195776]
[14]
Spicer, J.A.; Miller, C.K.; O’Connor, P.D. Inhibition of the cytolytic protein perforin prevents rejection of transplanted bone marrow stem cells in vivo. J. Med. Chem., 2020, 63(5), 2229-2239.
[http://dx.doi.org/10.1021/acs.jmedchem.9b00881] [PMID: 31525966]
[15]
Lyons, D.M.; Huttunen, K.M.; Browne, K.A. Inhibition of the cellular function of perforin by 1-amino-2,4-dicyanopyrido[1,2-a]benzimidazoles. Bioorg. Med. Chem., 2011, 19(13), 4091-4100.
[http://dx.doi.org/10.1016/j.bmc.2011.05.013] [PMID: 21664824]
[16]
Miller, C.K.; Huttunen, K.M.; Denny, W.A. Diarylthiophenes as inhibitors of the pore-forming protein perforin. Bioorg. Med. Chem. Lett., 2016, 26(2), 355-360.
[http://dx.doi.org/10.1016/j.bmcl.2015.12.003] [PMID: 26711151]
[17]
Li, W.; Si, H.; Li, Y. 3D-QSAR and molecular docking studies on designing inhibitors of the hepatitis C virus NS5B polymerase. J. Mol. Struct., 2016, 1117, 227-239.
[http://dx.doi.org/10.1016/j.molstruc.2016.03.073]
[18]
Tampio, J.; Markowicz-Piasecka, M.; Huttunen, K.M. Hemocompatible L-Type amino acid transporter 1 (LAT1)-Utilizing prodrugs of perforin inhibitors can accumulate into the pancreas and alleviate inflammation-induced apoptosis. Chem. Biol. Interact., 2021, 345, 109560.
[http://dx.doi.org/10.1016/j.cbi.2021.109560] [PMID: 34153225]

Rights & Permissions Print Cite
© 2025 Bentham Science Publishers | Privacy Policy