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Human Cathepsin V Functional Expression, Tissue Distribution, Electrostatic Surface Potential, Enzymatic Characterization, and Chromosomal Localization‡

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Departments of Human Genetics and of Physiology and Biophysics, Mount Sinai School of Medicine, CUNY, New York, NY 10029, and Axys Pharmaceutical, Inc., South San Francisco, CA 94080
Cite this: Biochemistry 1999, 38, 8, 2377–2385
Publication Date (Web):February 4, 1999
https://doi.org/10.1021/bi982175f
Copyright © 1999 American Chemical Society
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    Abstract

    Cathepsin V, a thymus and testis-specific human cysteine protease, was expressed in Pichia pastoris, and its physicokinetic properties were determined. Recombinant procathepsin V is autocatalytically activated at acidic pH and is effectively inhibited by various cysteine protease class-specific inhibitors. The S2P2 subsite specificity of cathepsin V was found to be intermediate between those of cathepsins S and L. The substrate binding pocket, S2, accepted both aromatic and nonaromatic hydrophobic residues, whereas cathepsins L and S preferred either an aromatic or nonaromatic hydrophobic residue, respectively. In contrast to cathepsin L, but similar to cathepsin S, cathepsin V exhibited only a very weak collagenolytic activity. Furthermore, cathepsin V was determined to be significantly more stable at mildly acidic and neutral pH than cathepsin L, but distinctly less stable than cathepsin S. A homology structure model of cathepsin V revealed completely different electrostatic potentials on the molecular surface when compared with human cathepsin L. The model-based electrostatic potential of human cathepsin V was neutral to weakly positive at and in the vicinity of the active site cleft, whereas that of cathepsin L was negative over extended regions of the surface. Surprisingly, the electrostatic potential of the human cathepsin V model structure resembled that of the model structure of mouse cathepsin L. These differences in the electrostatic potential at the molecular surfaces provide a reactivity determinant that may be the source of differences in substrate selectivity and pH stability. Cathepsin V was mapped to the chromosomal region 9q22.2, a site adjacent to the cathepsin L locus. The high sequence identity and the overlapping chromosomal gene loci suggest that both proteases evolved from an ancestral cathepsin L-like precursor by gene duplication.

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    ‡

     In part presented at the AACR Special Conference:  Proteases and Protease Inhibitors, Panama City, FL, March 1−5, 1996 and the International Conference on Proteolysis and Protein Turnover, Turku, Finland, September 8−11, 1996.

    *

     To whom correspondence should be addressed:  Mount Sinai School of Medicine, Department of Human Genetics, Box 1498, Fifth Avenue at 100th Street, New York, NY 10029. Tel:  212-824-7540. Fax:  212-849-2508. E-mail:  [email protected].

    §

     Department of Human Genetics, Mount Sinai School of Medicine.

    ⊥

     Axys Pharmaceutical, Inc.

    ‖

     Department of Physiology and Biophysics, Mount Sinai School of Medicine.

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    70. Marko Fonović, Boris Turk. Cysteine cathepsins and extracellular matrix degradation. Biochimica et Biophysica Acta (BBA) - General Subjects 2014, 1840 (8) , 2560-2570. https://doi.org/10.1016/j.bbagen.2014.03.017
    71. Ivana Kennedy Parker, Ladeidra Monet Roberts, Laura Hansen, Rudolph L. Gleason, Roy L. Sutliff, Manu O. Platt. Pro-Atherogenic Shear Stress and HIV Proteins Synergistically Upregulate Cathepsin K in Endothelial Cells. Annals of Biomedical Engineering 2014, 42 (6) , 1185-1194. https://doi.org/10.1007/s10439-014-1005-9
    72. Neha Aggarwal, Bonnie F. Sloane. Cathepsin B: Multiple roles in cancer. PROTEOMICS – Clinical Applications 2014, 8 (5-6) , 427-437. https://doi.org/10.1002/prca.201300105
    73. Marko Novinec, Brigita Lenarčič, Boris Turk. Cysteine Cathepsin Activity Regulation by Glycosaminoglycans. BioMed Research International 2014, 2014 , 1-9. https://doi.org/10.1155/2014/309718
    74. Stephen W. Scally, Jan Petersen, Soi Cheng Law, Nadine L. Dudek, Hendrik J. Nel, Khai Lee Loh, Lakshmi C. Wijeyewickrema, Sidonia B.G. Eckle, Jurgen van Heemst, Robert N. Pike, James McCluskey, Rene E. Toes, Nicole L. La Gruta, Anthony W. Purcell, Hugh H. Reid, Ranjeny Thomas, Jamie Rossjohn. A molecular basis for the association of the HLA-DRB1 locus, citrullination, and rheumatoid arthritis. Journal of Experimental Medicine 2013, 210 (12) , 2569-2582. https://doi.org/10.1084/jem.20131241
    75. Xin Du, Nelson L.H. Chen, Andre Wong, Charles S. Craik, Dieter Brömme. Elastin Degradation by Cathepsin V Requires Two Exosites. Journal of Biological Chemistry 2013, 288 (48) , 34871-34881. https://doi.org/10.1074/jbc.M113.510008
    76. Marko Novinec, Brigita Lenarčič. Papain-like peptidases: structure, function, and evolution. BioMolecular Concepts 2013, 4 (3) , 287-308. https://doi.org/10.1515/bmc-2012-0054
    77. Preety Panwar, Xin Du, Vidhu Sharma, Guillaume Lamour, Mickael Castro, Hongbin Li, Dieter Brömme. Effects of Cysteine Proteases on the Structural and Mechanical Properties of Collagen Fibers. Journal of Biological Chemistry 2013, 288 (8) , 5940-5950. https://doi.org/10.1074/jbc.M112.419689
    78. Dieter Brömme. Cathepsin V. 2013, 1831-1834. https://doi.org/10.1016/B978-0-12-382219-2.00413-0
    79. Xiao-Yu Yuan, Ding-Yi Fu, Xing-Feng Ren, Xuexun Fang, Lincong Wang, Shuxue Zou, Yuqing Wu. Highly selective aza-nitrile inhibitors for cathepsin K, structural optimization and molecular modeling. Organic & Biomolecular Chemistry 2013, 11 (35) , 5847. https://doi.org/10.1039/c3ob41165f
    80. Nataša Kopitar-Jerala. Cysteine Proteinase Inhibitors in the Nucleus and Nucleolus in Activated Macrophages. 2013, 305-321. https://doi.org/10.1007/978-94-007-5818-6_13
    81. Jennifer M. Cox, Jason S. Troutt, Michael D. Knierman, Robert W. Siegel, Yue-Wei Qian, Bradley L. Ackermann, Robert J. Konrad. Determination of cathepsin S abundance and activity in human plasma and implications for clinical investigation. Analytical Biochemistry 2012, 430 (2) , 130-137. https://doi.org/10.1016/j.ab.2012.08.011
    82. Yuki Niwa, Takehiro Suzuki, Naoshi Dohmae, Kazuo Umezawa, Siro Simizu. Determination of cathepsin V activity and intracellular trafficking by N‐glycosylation. FEBS Letters 2012, 586 (20) , 3601-3607. https://doi.org/10.1016/j.febslet.2012.08.001
    83. Philip M. Keegan, Catera L. Wilder, Manu O. Platt. Tumor necrosis factor alpha stimulates cathepsin K and V activity via juxtacrine monocyte–endothelial cell signaling and JNK activation. Molecular and Cellular Biochemistry 2012, 367 (1-2) , 65-72. https://doi.org/10.1007/s11010-012-1320-0
    84. Emerson F. Marques, Mauro A. Bueno, Patrícia D. Duarte, Larissa R.S.P. Silva, Ariani M. Martinelli, Caio Y. dos Santos, Richele P. Severino, Dieter Brömme, Paulo C. Vieira, Arlene G. Corrêa. Evaluation of synthetic acridones and 4-quinolinones as potent inhibitors of cathepsins L and V. European Journal of Medicinal Chemistry 2012, 54 , 10-21. https://doi.org/10.1016/j.ejmech.2012.04.002
    85. Lydiane Funkelstein, W. Douglas Lu, Britta Koch, Charles Mosier, Thomas Toneff, Laurent Taupenot, Daniel T. O'Connor, Thomas Reinheckel, Christoph Peters, Vivian Hook. Human Cathepsin V Protease Participates in Production of Enkephalin and NPY Neuropeptide Neurotransmitters. Journal of Biological Chemistry 2012, 287 (19) , 15232-15241. https://doi.org/10.1074/jbc.M111.310607
    86. Marko Novinec, Miha Pavšič, Brigita Lenarčič. A simple and efficient protocol for the production of recombinant cathepsin V and other cysteine cathepsins in soluble form in Escherichia coli. Protein Expression and Purification 2012, 82 (1) , 1-5. https://doi.org/10.1016/j.pep.2011.11.002
    87. Vito Turk, Veronika Stoka, Olga Vasiljeva, Miha Renko, Tao Sun, Boris Turk, Dušan Turk. Cysteine cathepsins: From structure, function and regulation to new frontiers. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2012, 1824 (1) , 68-88. https://doi.org/10.1016/j.bbapap.2011.10.002
    88. Philip M. Keegan, Sindhuja Surapaneni, Manu O. Platt. Sickle Cell Disease Activates Peripheral Blood Mononuclear Cells to Induce Cathepsins K and V Activity in Endothelial Cells. Anemia 2012, 2012 , 1-7. https://doi.org/10.1155/2012/201781
    89. Catera L. Wilder, Keon-Young Park, Philip M. Keegan, Manu O. Platt. Manipulating substrate and pH in zymography protocols selectively distinguishes cathepsins K, L, S, and V activity in cells and tissues. Archives of Biochemistry and Biophysics 2011, 516 (1) , 52-57. https://doi.org/10.1016/j.abb.2011.09.009
    90. Ryan Kirschner, Dirk Hubmacher, Garud Iyengar, Jasvir Kaur, Christine Fagotto-Kaufmann, Dieter Brömme, Rainer Bartels, Dieter P. Reinhardt. Classical and Neonatal Marfan Syndrome Mutations in Fibrillin-1 Cause Differential Protease Susceptibilities and Protein Function. Journal of Biological Chemistry 2011, 286 (37) , 32810-32823. https://doi.org/10.1074/jbc.M111.221804
    91. Melanie A. Adams-Cioaba, Joanne C. Krupa, Chao Xu, John S. Mort, Jinrong Min. Structural basis for the recognition and cleavage of histone H3 by cathepsin L. Nature Communications 2011, 2 (1) https://doi.org/10.1038/ncomms1204
    92. G. Leto, M. Crescimanno, C. Flandina, M. V. Sepporta, F. M. Tumminello. Cathepsin L in Normal and Pathological Bone Remodeling. Clinical Reviews in Bone and Mineral Metabolism 2011, 9 (2) , 107-121. https://doi.org/10.1007/s12018-011-9100-z
    93. Leandro Piovan, Márcio F.M. Alves, Luiz Juliano, Dieter Brömme, Rodrigo L.O.R. Cunha, Leandro H. Andrade. Structure–activity relationships of hypervalent organochalcogenanes as inhibitors of cysteine cathepsins V and S. Bioorganic & Medicinal Chemistry 2011, 19 (6) , 2009-2014. https://doi.org/10.1016/j.bmc.2011.01.054
    94. Richele P. Severino, Rafael V.C. Guido, Emerson F. Marques, Dieter Brömme, M. Fátima das G.F. da Silva, João B. Fernandes, Adriano D. Andricopulo, Paulo C. Vieira. Acridone alkaloids as potent inhibitors of cathepsin V. Bioorganic & Medicinal Chemistry 2011, 19 (4) , 1477-1481. https://doi.org/10.1016/j.bmc.2010.12.056
    95. Dieter Brömme, Susan Wilson. Role of Cysteine Cathepsins in Extracellular Proteolysis. 2011, 23-51. https://doi.org/10.1007/978-3-642-16861-1_2
    96. Sofia Tedelind, Kseniia Poliakova, Amanda Valeta, Ruth Hunegnaw, Eyoel Lemma Yemanaberhan, Nils-Erik Heldin, Junichi Kurebayashi, Ekkehard Weber, Nataša Kopitar-Jerala, Boris Turk, Matthew Bogyo, Klaudia Brix. Nuclear cysteine cathepsin variants in thyroid carcinoma cells. Biological Chemistry 2010, 391 (8) https://doi.org/10.1515/bc.2010.109
    97. Gaetano Leto, Maria Vittoria Sepporta, Marilena Crescimanno, Carla Flandina, Francesca Maria Tumminello. Cathepsin L in metastatic bone disease: therapeutic implications. Biological Chemistry 2010, 391 (6) https://doi.org/10.1515/bc.2010.069
    98. Larissa P. Coppini, Nilana M.T. Barros, Marcela Oliveira, Izaura Y. Hirata, Marcio F.M. Alves, Thaysa Paschoalin, Diego M. Assis, Maria A. Juliano, Luciano Puzer, Dieter Brömme, Adriana K. Carmona. Plasminogen hydrolysis by cathepsin S and identification of derived peptides as selective substrate for cathepsin V and cathepsin L inhibitor. Biological Chemistry 2010, 391 (5) , 561-570. https://doi.org/10.1515/bc.2010.049
    99. Slavko Čeru, Špela Konjar, Katarina Maher, Urška Repnik, Igor Križaj, Mojca Benčina, Miha Renko, Alain Nepveu, Eva Žerovnik, Boris Turk, Nataša Kopitar-Jerala. Stefin B Interacts with Histones and Cathepsin L in the Nucleus. Journal of Biological Chemistry 2010, 285 (13) , 10078-10086. https://doi.org/10.1074/jbc.M109.034793
    100. Timo Burster, Henriette Macmillan, Tieying Hou, Bernhard O. Boehm, Elizabeth D. Mellins. Cathepsin G: Roles in antigen presentation and beyond. Molecular Immunology 2010, 47 (4) , 658-665. https://doi.org/10.1016/j.molimm.2009.10.003
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