메뉴 건너뛰기




Volumn 267, Issue 11, 2000, Pages 3330-3336

Arginine-based structures are specific inhibitors of cathepsin C. Application of peptide combinatorial libraries

Author keywords

Cathepsin C; Combinatorial libraries; Dipeptidyl peptidase I; Lysosomal cysteine proteinase; Peptide inhibitor

Indexed keywords

ARGININE; CYSTEINE PROTEINASE; DIPEPTIDYL PEPTIDASE; GUANIDINE DERIVATIVE; PEPTIDE LIBRARY; PROTEIN INHIBITOR; SYNTHETIC PEPTIDE;

EID: 0034129207     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01364.x     Document Type: Article
Times cited : (26)

References (26)
  • 1
    • 0027518670 scopus 로고
    • Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I
    • 1. McGuire, M.J., Lipsky, P.E. & Thiele, D.L. (1993) Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I. J. Biol. Chem. 268, 2458-2467.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2458-2467
    • McGuire, M.J.1    Lipsky, P.E.2    Thiele, D.L.3
  • 2
    • 0028945071 scopus 로고
    • Human prochymase activation. A novel role for heparin in zymogen processing
    • 2. Murakami, M., Karnik, S.S. & Husain, A. (1995) Human prochymase activation. A novel role for heparin in zymogen processing. J. Biol. Chem. 270, 2218-2223.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2218-2223
    • Murakami, M.1    Karnik, S.S.2    Husain, A.3
  • 3
    • 0028016436 scopus 로고
    • Activation of thrombin-inactivated single-chain urokinase-type plasminogen activator by dipeptidyl peptidase I (cathepsin C)
    • 3. Nauland, U. & Rijken, D.C. (1994) Activation of thrombin-inactivated single-chain urokinase-type plasminogen activator by dipeptidyl peptidase I (cathepsin C). Eur. J. Biochem. 223, 497-501.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 497-501
    • Nauland, U.1    Rijken, D.C.2
  • 4
    • 0027520217 scopus 로고
    • Processing and transport of the precursor of cathepsin C during its transfer into lysosomes
    • 4. Muno, D., Ishidoh, K., Ueno, T. & Kominami, E. (1993) Processing and transport of the precursor of cathepsin C during its transfer into lysosomes. Arch. Biochem. Biophys. 306, 103-110.
    • (1993) Arch. Biochem. Biophys. , vol.306 , pp. 103-110
    • Muno, D.1    Ishidoh, K.2    Ueno, T.3    Kominami, E.4
  • 5
    • 0029163155 scopus 로고
    • Oligomeric structure and substrate induced inhibition of human cathepsin C
    • 5. Dolenc, I., Turk, B., Pungercic, G., Ritonja, A. & Turk, V. (1995) Oligomeric structure and substrate induced inhibition of human cathepsin C. J. Biol. Chem. 270, 21626-21631.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21626-21631
    • Dolenc, I.1    Turk, B.2    Pungercic, G.3    Ritonja, A.4    Turk, V.5
  • 6
    • 0027205170 scopus 로고
    • Endopeptidase activity of cathepsin C, dipeptidyl aminopeptidase I, from bovine spleen
    • 6. Kuribayashi, M., Yamada, H., Ohmori, T., Yanai, M. & Imoto, T. (1993) Endopeptidase activity of cathepsin C, dipeptidyl aminopeptidase I, from bovine spleen. J. Biochem. (Tokyo) 113, 441-449.
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 441-449
    • Kuribayashi, M.1    Yamada, H.2    Ohmori, T.3    Yanai, M.4    Imoto, T.5
  • 7
    • 0019887728 scopus 로고
    • Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases
    • 7. Green, G.D.J. & Shaw, E. (1981) Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases. J. Biol. Chem. 256, 1923-1928.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1923-1928
    • Green, G.D.J.1    Shaw, E.2
  • 8
    • 0001427425 scopus 로고
    • Inhibitors of cysteine proteinases
    • (Barrett, A.J. & Salvesen, G., eds) Elsevier. Amsterdam, New York
    • 8. Rich, D.H. (1986) Inhibitors of cysteine proteinases. In Proteinase Inhibitors (Barrett, A.J. & Salvesen, G., eds), pp. 153-178. Elsevier. Amsterdam, New York.
    • (1986) Proteinase Inhibitors , pp. 153-178
    • Rich, D.H.1
  • 9
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • 9. Palmer, J.T., Rasnick, D., Klaus, J.L. & Bromme, D. (1995) Vinyl sulfones as mechanism-based cysteine protease inhibitors. J. Med. Chemistry. 38, 3193-3196.
    • (1995) J. Med. Chemistry. , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.L.3    Bromme, D.4
  • 10
    • 0019948262 scopus 로고
    • L-trans-Epoxysuccinylleucylamido (4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • 10. Barrett, A.J., Kembhavi, A.A., Brown. M.A., Kirschke, H., Knight, C.G., Tamai, M. & Hanada, K. (1982) L-trans-Epoxysuccinylleucylamido (4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 201, 189-198.
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 11
    • 0027454521 scopus 로고
    • Identification of substrate-analog trypsin inhibitors through the screening of synthetic peptide combinatorial libraries
    • 11. Eichler, J. & Houghten, R.A. (1993) Identification of substrate-analog trypsin inhibitors through the screening of synthetic peptide combinatorial libraries. Biochemistry 32, 11035-11041.
    • (1993) Biochemistry , vol.32 , pp. 11035-11041
    • Eichler, J.1    Houghten, R.A.2
  • 12
    • 0032037456 scopus 로고    scopus 로고
    • Inhibition of cruzipain visualized in a fluorescence quenched solid-phase inhibitor library assay. D-Amino acid inhibitors for cruzipain, cathepsin B and cathepsin L
    • 12. Meldal, M., Svedsen, I.B., Juliano, L., Juliano, M.A., Nery, E.D. & Scharfstein, J. (1998) Inhibition of cruzipain visualized in a fluorescence quenched solid-phase inhibitor library assay. D-Amino acid inhibitors for cruzipain, cathepsin B and cathepsin L. J. Pept. Sci. 4, 83-91.
    • (1998) J. Pept. Sci. , vol.4 , pp. 83-91
    • Meldal, M.1    Svedsen, I.B.2    Juliano, L.3    Juliano, M.A.4    Nery, E.D.5    Scharfstein, J.6
  • 13
    • 0029741201 scopus 로고    scopus 로고
    • Development of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24-15 using combinatorial chemistry
    • 13. Jiráček, J., Yiotakis, A., Vincent, B., Checler, F. & Dive, V. (1996) Development of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24-15 using combinatorial chemistry. J. Biol. Chem. 271, 19606-19611.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19606-19611
    • Jiráček, J.1    Yiotakis, A.2    Vincent, B.3    Checler, F.4    Dive, V.5
  • 14
    • 77956987303 scopus 로고
    • Cathepsin C (dipeptidyl transferase)
    • 14. Mycek, M.J. (1970) Cathepsin C (dipeptidyl transferase). Methods Enzymol. 19, 285-315.
    • (1970) Methods Enzymol. , vol.19 , pp. 285-315
    • Mycek, M.J.1
  • 15
    • 0025944975 scopus 로고
    • S-S bridges of cathepsin B and H from bovine spleen: A basis for cathepsin B model building and possible functional implications for discrimination between exo-and endopeptidase activities among cathepsins B, H and L
    • 15. Baudyš, M., Meloun, B., Gan-Erdene, T., Fusek, M., Mareš, M., Kostka, V., Pohl, J. & Blake, C.C.F. ( 1991) S-S bridges of cathepsin B and H from bovine spleen: a basis for cathepsin B model building and possible functional implications for discrimination between exo-and endopeptidase activities among cathepsins B, H and L. Biomed. Biochim. Acta 50, 569-577.
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 569-577
    • Baudyš, M.1    Meloun, B.2    Gan-Erdene, T.3    Fusek, M.4    Mareš, M.5    Kostka, V.6    Pohl, J.7    Blake, C.C.F.8
  • 18
    • 0014690532 scopus 로고
    • New observations on the substrate specificity of cathepsin C (dipeptidyl-aminopeptidase I). Including the degradation of beta-corticotropin and other peptide hormones
    • 18. McDonald, J.K., Zeitman, B.B., Reilly, T.J. & Ellis, S. (1969) New observations on the substrate specificity of cathepsin C (dipeptidyl-aminopeptidase I). Including the degradation of beta-corticotropin and other peptide hormones. J. Biol. Chem. 244, 2693-2709.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2693-2709
    • McDonald, J.K.1    Zeitman, B.B.2    Reilly, T.J.3    Ellis, S.4
  • 19
    • 0026752536 scopus 로고
    • Purification and characterization of dipeptidyl peptidase I from human spleen
    • 19. McGuire, M.J., Lipsky, P.E. & Thiele, D.L. (1992) Purification and characterization of dipeptidyl peptidase I from human spleen. Arch. Biochem. Biophys. 295, 280-288.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 280-288
    • McGuire, M.J.1    Lipsky, P.E.2    Thiele, D.L.3
  • 20
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin's structure
    • 20. Stubbs, M.T. & Bode, W. (1993) A player of many parts: the spotlight falls on thrombin's structure. Thromb. Res. 69, 1-58.
    • (1993) Thromb. Res. , vol.69 , pp. 1-58
    • Stubbs, M.T.1    Bode, W.2
  • 21
    • 0030565414 scopus 로고    scopus 로고
    • Interaction of human cathepsin C with chicken cystatin
    • 21. Dolenc, I., Turk, B., Kos, J. & Turk, V. (1996) Interaction of human cathepsin C with chicken cystatin. FEBS Lett. 392, 277-280.
    • (1996) FEBS Lett. , vol.392 , pp. 277-280
    • Dolenc, I.1    Turk, B.2    Kos, J.3    Turk, V.4
  • 22
    • 0023801371 scopus 로고
    • Interaction of the cysteine proteinase inhibitor chicken cystatin with papain
    • 22. Lindahl, P., Alriksson, E., Jörnvall, H. & Björk, I. (1988) Interaction of the cysteine proteinase inhibitor chicken cystatin with papain. Biochemistry 27, 5074-5082.
    • (1988) Biochemistry , vol.27 , pp. 5074-5082
    • Lindahl, P.1    Alriksson, E.2    Jörnvall, H.3    Björk, I.4
  • 24
    • 0033614434 scopus 로고    scopus 로고
    • Competitive inhibition of cathepsin C by guanidinium ions and reexamination of substrate inhibition
    • 24. Cigiæ, B. & Pain, R.H. (1999) Competitive inhibition of cathepsin C by guanidinium ions and reexamination of substrate inhibition. Biochem. Biophys. Res. Commun. 258, 6-10.
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 6-10
    • Cigiæ, B.1    Pain, R.H.2
  • 25
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction wilh proteinases
    • 25. Bode, W. & Huber, R. (1992) Natural protein proteinase inhibitors and their interaction wilh proteinases. Eur. J. Biochem. 204, 433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 26
    • 0029911570 scopus 로고    scopus 로고
    • Peptidyl vinyl sulphones: A new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L
    • 26. Bromme, D., Klaus, J.L., Okamoto, K., Rasnick, D. & Palmer, J.T. (1996) Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L. Biochem. J. 315, 85-8927.
    • (1996) Biochem. J. , vol.315 , pp. 85-8927
    • Bromme, D.1    Klaus, J.L.2    Okamoto, K.3    Rasnick, D.4    Palmer, J.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.