Inhibition of human kallikreins 5 and 7 by the serine protease inhibitor lympho-epithelial Kazal-type inhibitor (LEKTI)

Biological Chemistry

Volumn 386, Issue 11, 2005, Pages 1173-1184

  Schechter, Norman M ^a   Choi, Eun Jung ^a   Wang, Zhe Mei ^a   Hanakawa, Yasushi ^a   Stanley, John R ^a   Kang, Ya'an ^b   Clayman, Gary L ^b   Jayakumar, Arumugam ^b  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF TEXAS   (United States)

Author keywords

Desquamation; Netherton syndrome; SPINK5; Standard mechanism inhibitor

Indexed keywords

CHYMOTRYPSIN; KALLIKREIN INHIBITOR; SERINE PROTEINASE INHIBITOR;

ACIDITY; ALKALINITY; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CALCULATION; DESQUAMATION; ENZYME MECHANISM; HUMAN; NETHERTON DISEASE; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN TARGETING; SKIN; STRATUM CORNEUM;

CARRIER PROTEINS; DNA, COMPLEMENTARY; ENZYME INHIBITORS; HUMANS; HYDROGEN-ION CONCENTRATION; KALLIKREINS; KINETICS; PEPTIDE FRAGMENTS; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES;

EQUUS ASINUS;

EID: 28244435723     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2005.134     Document Type: Article

References (47)

1. Beatty, K., Bieth, J., and Travis, J. (1980). Kinetics of association of serine proteinases with native and oxidized a1-proteinase inhibitor and a1-antichymotrypsin. J. Biol. Chem. 255, 3931-3934.
2. Berg, O.G. and von Hippel, P.H. (1985). Diffusion-controlled macromolecular interactions. Annu. Rev. Biophys. Bioeng. 14, 131-160.
3. Bieth, J. (1974). Some kinetic consequences of the tight binding of protein-proteinase-inhibitors to proteolytic enzymes and their application to the determination of dissociation constants. In: Bayer Symposium V on Proteinase Inhibitors (Berlin, Germany: Springer-Verlag), pp. 463-469.
4. Bitoun, E., Chavanas, S., Irvine, A.D., Lonie, L., Bodemer, C., Paradisi, M., Hamel-Teillac, D., Ansai, S.-I., Mitsuhashi, Y., et al. (2002). Netherton syndrome: disease expression and spectrum of SPINK5 mutations in 21 families. J. Invest. Dermatol. 118, 352-361.
5. Bitoun, E., Micheloni, A., Lamant, L., Bonnart, C., Tartaglia-Polcini, A., Cobbold, C., Al Saati, T., Mariotti, F., Mazereeuw-Hautier, J., et al. (2003). LEKTI proteolyic processing in human primary keratinocytes, tissue distribution and defective expression on Netherton syndrome. Hum. Mol. Genet. 12, 2417-2430.
6. Boudier, C. and Bieth, J. (1989). Mucus proteinase inhibitor: a fast-acting inhibitor of leukocyte elastase. Biochem. Biophys. Acta 995, 36-41.
7. Brattsand, M. and Egelrud, T. (1999). Purification, molecular cloning, and expression of a human stratum corneum trypsin-like serine protease with possible function in desquamation. J. Biol. Chem. 274, 30033-30040.
8. Caubet, C., Jonca, N., Brattsand, M., Guerrin, M., Bernard, D., Schmidt, R., Egelrud, T., Simon, M., and Serre, G. (2004). Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7. J. Invest. Dermatol. 122, 1235-1244.
9. Chavanas, S., Bodemer, C., Rochat, A., Hamel-Teillac, D., Ali, M., Irvine, A.D., Bonafé, J.L., Wilkinson, J., Taieb, A., et al. (2000). Mutations in SPINK5, encoding a serine protease inhibitor, cause of Netherton syndrome. Nat. Genet. 25, 141-142.
10. Descargues, P., Deraison, C., Bonnart, C., Kreft, M., Kishibe, M., Ishida-Yamamoto, A., Elias, P.M., Barrandon, Y., Zambruno, G., Sonnenberg, A., and Hovnanian, A. (2005). Spink5-deficient mice mimic Netherton syndrome through degradation of desmoglein 1 by epidermal protease hyperactivity. Nat. Genet. 1, 56-65.
11. Egelrud, T. (1993). Purification and preliminary characterization of stratum corneum chymotryptic enzyme: a proteinase that may be involved in desquamation. J. Invest. Dermatol. 101, 200-204.
12. Egelrud, T. (2000). Desquamation in the stratum corneum. Acta Dermatol. Venereol. 208 (Suppl.), 44-45.
13. Ekholm, E., Brattsand, M., and Egelrud, T. (2000). Stratum corneum tryptic enzyme in normal epidermis: a missing link in the desquamation process. J. Invest. Dermatol. 114, 56-62.
14. Fluhr, J.W., Mao-Qiang, M., Brown, B.E., Hachem, J.-P., Moskowitz, D.G., Haftek, M., Serre, G., Crumrine, D., Mauro, T.M., Elias, P.M., and Feingold, K.R. (2004). Functional consequences of a neutral pH in neonatal rat stratum corneum. J. Invest. Dermatol. 123, 140-151.
15. Gettins, G.W. (2002). Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4803.
16. Gettins, P.G.W., Patston, P.A., and Olson, S.T. (1996). Serpins: Structure, Function and Biology (New York, USA: Chapman and Hall).
17. Hachem, J.-P., Crumrine, D., Fluhr, J.W., Brown, B.E., Feingold, K.R., and Elias, P.M. (2003). pH directly regulates epidermal permeability barrier homeostasis and stratum corneum integrity/cohesion. J. Invest. Dermatol. 121, 345-353.
18. Hansson, L., Strömqvist, M., Bäckman, A., Wallbrandt, P., Carlstein, A., and Egelrud, T. (1994). Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. J. Biol. Chem. 269, 19420-19426.
19. Ishida-Yamamoto, A., Deraison, C., Bonnart, C., Bitoun, E., Robinson, R., O'Brien, T.J., Wakamatsu, K., Ohtsubo, S., Takahashi, H., et al. (2005). LEKTI is localized in lamellar granules, separated from KLK5 and KLK7, and is secreted in the extracellular spaces of the superficial stratum corneum. J. Invest. Dermatol. 124, 360-366.
20. Jayakumar, A., Kang, Y., Mitsudo, K., Henderson, Y., Frederick, M.J., Wang, M., El-Naggaar, A.K., Marx, U.C., Briggs, K., and Clayman, G.L. (2004). Expression of LEKTI domains 6-9′ in the baculovirus expression system: recombinant LEKTI domains 6-9′ inhibit trypsin and subtilisin A. Protein Expr. Purif. 35, 93-101.
21. Jayakumar, A., Kang, Y., Henderson, Y., Mitsudo, K., Liu, X., Briggs, K., Wang, M., Frederick, M.J., El-Naggaar, A.K., Bebök, Z., and Clayman, G.L. (2005). Consequences of C-terminal domains and N-terminal signal peptide deletions in LEKTI secretion, stability, and subcellular distribution. Arch. Biochem. Biophys. 435, 89-102.
22. Knight, C.G. (1986). The characterization of enzyme inhibition. In: Proteinase Inhibitors, Vol. 12, A.J. Barrett and G.S. Salvesen, eds. (New York, USA: Elsevier), pp. 23-51.
23. Komatsu, N., Takata, M., Otsuki, N., Ohka, R., Amano, O., Takehara, K., and Saijoh, K. (2002). Elevated stratum corneum hydrolytic activity in Netherton syndrome suggests an inhibitory regulation of desquamation by SPINK5-derived peptides. J. Invest. Dermatol. 118, 436-443.
24. Komatsu, N., Takata, M., Otsuki, N., Toyama, T., Ohka, R., Takehara, K., and Saijoh, K. (2003). Expression and localization of tissue kallikrein mRNAs in human epidermis and appendages. J. Invest. Dermatol. 121, 542-549.
25. Kreutzmann, P., Schutz, A., Ständker, L., Forssmann, W.-G., and Mägert, H.-J. (2004). Recombinant production, purification and biochemical characterization of domain 6 of LEKTI: a temporary Kazal-type-related serine proteinase inhibitor. J. Chromatogr. B 803, 75-81.
26. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
27. Laskowski, M.J. and Kato, I. (1980). Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626.
28. Lauber, T., Schutz, A., Schweimer, K., Adermann, K., and Marx, U.C. (2003). Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI. J. Mol. Biol. 328, 205-219.
29. Longstaff, C. and Gaffney, P.J. (1991). Serpin-serpin protease binding kinetics: a-antiplasmin as a model inhibitor. Biochemistry 30, 979-996.
30. Longstaff, C., Campbell, A.F., and Fersht, A.R. (1990). Recombinant chymotrypsin inhibitor 2: expression, kinetic analysis of inhibition of a-chymotrypsin and wild-type and mutant subtilisin BPN′, and protein engineering to investigate inhibitory specificity and mechanism. Biochemistry 29, 7339-7347.
31. Magert, H.-J., Ständker, L., Kreutzmann, P., Zucht, H.-D., Reinecke, M., Sommerhoff, C.P., Fritz, H., and Forssmann, W.-G. (1999). LEKTI, a novel 15-domain type of human serine proteinase inhibitor. J. Biol. Chem. 274, 21499-21502.
32. Mitsudo, K., Jayakumar, A., Henderson, Y., Frederick, M.J., Kang, Y., Wang, M., El-Naggaar, A.K., and Clayman, G.L. (2003). Inhibition of serine proteinases plasmin, trypsin, cathepsin G, and elastase by LEKTI: a kinetic analysis. Biochemistry 42, 3874-3881.
33. Morrison, J.F. and Walsh, C.T. (1987). The significance of slow-binding enzyme inhibitors. Adv. Enzymol. 61, 210-301.
34. Pace, C.N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995). How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
35. Plotnick, M.I., Rubin, H., and Schechter, N.M. (2002). The effects of reactive site location on the inhibitory properties of the serpin a1-antichymotrypsin. J. Biol. Chem. 277, 29927-29935.
36. Raghunath, M., Tontsidou, L., Oji, V., Aufenvenne, K., Schürmeyer-Horst, F., Jayakumar, A., Stander, H., Smolle, J., Clayman, G.L., and Traupe, H. (2004). SPINK5 and Netherton syndrome: novel mutations, demonstration of missing LEKTI, and differential expression of transglutaminases. J. Invest. Dermatol. 123, 474-483.
37. Read, R.J. and James, M.N.G. (1986). Introduction to the protein inhibitors: X-ray crystallography. In: Proteinase Inhibitors, Vol. 12, A.J. Barrett and G.S. Salvesen, eds. (New York, USA: Elsevier), pp. 301-336.
38. Schechter, N.M., Jordan, L.M., James, A.M., Cooperman, B.S., Wang, Z.-M., and Rubin, H. (1993). Reaction of human chymase with reactive site variants of α1-antichymotrypsin: modulation of inhibitor vs. substrate properties. J. Biol. Chem. 268, 23626-23633.
39. Schreiber, G. and Fersht, A. (1996). Rapid, electrostatically assisted association of proteins. Nat. Struct. Biol. 3, 427-431.
40. Tanimoto, H., Underwood, L.J., Shigemasa, K., Yan, Y., Clarke, J., Parmley, T.H., and O'Brien, T.J. (1999). The stratum corneum chymotryptic enzyme that mediates shedding and desquamation of skin cells is highly overexpressed in ovarian tumor cells. Cancer 86, 2074-2082.
41. Tidow, H., Lauber, T., Vitzithum, K., Sommerhoff, C.P., Rösch, P., and Marx, U.C. (2004). The solution structure of a chimeric LEKTI domain reveals a chameleon sequence. Biochemistry 43, 11238-11247.
42. Walley, A.J., Chavanas, S., Moffatt, M.F., Esnouf, R.M., Ubhi, B., Lawrence, R., Wong, K., Abecsis, G.R., Jones, E.Y., Harper, J.I., Hovnanian, A., and Cookson, W.O. (2001). Gene polymorphism in Netherton and common atopic disease. Nat. Genet. 29, 175-178.
43. Wang, Z.-M., Rubin, H., and Schechter, N.M. (1995). Production of active recombinant human chymase from a construct containing the enterokinase cleavage site of trypsinogen in place of the native propeptide sequence. Biol. Chem. Hoppe-Seyler 376, 681-684.
44. Wang, Z.M., Walter, M., Selwood, T., Rubin, H., and Schechter, N.M. (1998). Recombinant expression of human mast cell proteases chymase and tryptase. Biol. Chem. 379, 167-174.
45. -/- mice. Genes Dev. 18, 2354-2358.
46. Ying, Q.-L. and Simon, M. (1993). Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor of human skin. J. Biol. Chem. 32, 1866-1874.
47. Yousef, G.M. and Diamandis, E.P. (2001). The new human tissue kallikrein gene family: structure, function and association with disease. Endocrinol. Rev. 22, 184-204.