Active recombinant rat dipeptidyl aminopeptidase (cathepsin C) produced using the baculovirus expression system

Protein Expression and Purification

Volumn 14, Issue 3, 1998, Pages 434-442

  Lauritzen, Conni ^a   Pedersen, John ^a   Madsen, Mads T ^a,c   Justesen, Just ^b   Martensen, Pia M ^b   Dahl, Søren W ^a  

^a Unizyme Laboratories A/S   (Denmark)

^b AARHUS UNIVERSITY   (Denmark)

^c DANISCO A S   (Denmark)

Author keywords

Activation; Baculovirus; Cathepsin C; Dipeptidyl aminopeptidase I; Expression; Histidine tag; Insect cells; Purification

Indexed keywords

AFFINITY CHROMATOGRAPHY; BACULOVIRUS; CHROMATOGRAPHY; DIPEPTIDYL PEPTIDASE; DIPEPTIDYL PEPTIDASE I; FRACTIONATION; ION EXCHANGE CHROMATOGRAPHY; METAL AFFINITY CHROMATOGRAPHY; PROTEIN EXPRESSION; RECOMBINANT PROTEIN;

EID: 0032420423     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1998.0976     Document Type: Article

References (31)

1. Metrione R. M., Neves A. G., Fruton J. S. Purification and properties of dipeptidyl transferase. Biochemistry. 5:1966;1597-1604.
2. McDonald J. K., Zeitman B. B., Reilly T. J., Ellis S. New observations on substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). J. Biol. Chem. 244:1969;2693-2709.
3. McGuire M. J., Lipsky P. E., Thiele D.L. Purification and characterization of dipeptidyl peptidase I from human spleen. Arch. Biochem. Biophys. 295:1992;280-288.
4. Ishidoh K., Muno D., Sato N., Kominami E. Molecular cloning of cDNA for rat cathepsin C: Cathepsin C, a cysteine proteinase with an extremely long propeptide. Biol. Chem. 266:1991;16312-16317.
5. Paris A., Strukelj B., Pungercar J., Renko M., Dolenc I., Turk V. Molecular cloning and sequence analysis of human preprocathepsin C. FEBS Lett. 369:1995;326-330.
6. McGuire M. J., Lipsky P. E., Thiele D. L. Cloning and characterization of the cDNA encoding mouse dipeptidyl peptidase I (cathepsin C). Biochim. Biophys. Acta. 1351:1997;267-273.
7. Cigic B., Krizaj I., Kralj B., Turk V., Pain R. H. Stoichiometry and heterogeneity of the pro-region chain in tetrameric human cathepsin C. Biochim. Biophys. Acta. 1382:1998;143-150.
8. Dolenc I., Turk B., Pungercic G., Ritonja A., Turk V. Oligomeric structure and substrate induced inhibition of human cathepsin C. J. Biol. Chem. 270:1995;21626-21631.
9. Nikawa T., Towatari T., Katunuma N. Purification and characterization of cathepsin J from rat liver. Eur. J. Biochem. 204:1992;381-393.
10. Lindley H. The specificity of dipeptidyl aminopeptidase I (cathepsin C) and its use in peptide sequence studies. Biochem. J. 126:1972;683-685.
11. McGuire M. J., Lipsky P. E., Thiele D. L. Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I. J. Biol. Chem. 268:1993;2458-2467.
12. Kummer J. A., Kamp A. M., Citarella F., Horrevoets A. J., Hack C. E. Expression of human recombinant granzyme A zymogen and its activation by the cysteine proteinase cathepsin C. J. Biol.Chem. 271:1996;9281-9286.
13. Pham C. T., Thomas D. A., Mercer J. D., Ley T. J. Production of fully active recombinant murine granzyme B in yeast. J. Biol. Chem. 273:1998;1629-1633.
14. Dalbøge H., Dahl H-H., Pedersen J., Hansen J. W., Christensen T. A novel enzymatic method for production of authentic hGH from anEscherichia coli. Bio/Technology. 5:1987;161-164.
15. Hsiung M. H., Mackellar W.C. Expression of bovine growth hormone derivatives inEscherichia coli. Methods Enzymol. 153:1987;390-401.
16. Dalbøge H., Bayne S., Christensen T., Hejnæs K.R. Cloning and expression of an interleukin-1 beta precursor and its conversion to interleukin-1 beta. FEBS Lett. 246:1989;89-93.
17. Lauritzen C., Tuchsen E., Hansen P. E., Skovgaard O. BPTI and N-terminal extended analogues generated by factor Xa cleavage and cathepsin C trimming of a fusion protein expressed inEscherichia coli. Protein Express. Purif. 2:1991;372-378.
18. Hejnaes K. R., Bayne S., Norskov L., Sorensen H. H., Thomsen J., Schaffer L., Wollmer A., Skriver L. Development of an optimized refolding process for recombinant Ala-Glu-IGF-1. Protein Eng. 5:1992;797-806.
19. Belagaje R. M., Reams S. G., Ly S. C., Prouty W. F. Increased production of low molecular weight recombinant proteins inEscherichia coli. Protein Sci. 6:1997;1953-1962.
20. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
21. King L. A., Possee R. D. The Baculovirus Expression System - A Laboratory Guide. 1992;Chapman and Hall, London.
22. Planta R. J., Gruber M. A simple estimation of cathepsin C using a new chromogenic substrate. Anal. Biochem. 5:1963;360-362.
23. Ploug M., Jensen A. L., Barkholt V. Determination of amino acid compositions and NH2-terminal sequences of peptides electroblotted onto PVDF membranes from tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis: Application to peptide mapping of human complement component C3. Anal. Biochem. 181:1989;33-39.
24. Vernet T., Tessier D. C., Richardson C., Laliberte F., Khouri H. E., Bell A. W., Storer A. C., Thomas D. Y. Secretion of functional papain precursor from insect cells: Requirement for N-glycosylation of the pro-region. J. Biol. Chem. 265:1990;16661-16666.
25. Brömme D., McGrath M. E. High level expression and crystallization of recombinant human cathepsin S. Protein Sci. 5:1996;789-791.
26. Brömme D., Okamoto K., Wang B. B., Biroc S. Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 inSpodoptera frugiperda. J. Biol. Chem. 271:1996;2126-2132.
27. Ménard R., Carmona E., Takebe S., Dufour E., Plouffe C., Mason P., Mort J. S. Autocatalytic processing of recombinant human procathepsin L: Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro. J. Biol. Chem. 273:1998;4478-4484.
28. Mach L., Mort J. S., Glossl J. Maturation of human procathepsin B. Proenzyme activation and proteolytic processing of the precursor to the mature proteinase,in vitro, J. Biol. Chem. 269:1994;13030-13035.
29. McQueney M. S., Amegadzie B. Y., D'Alessio K., Hanning C. R., McLaughlin M. M., McNulty D., Carr S. A., Ijames C., Kurdyla J., Jones C. S. Autocatalytic activation of human cathepsin K. J. Biol. Chem. 272:1997;13955-13960.
30. Nomura T., Fujisawa Y. Processing properties of recombinant human procathepsin L. Biochem. Biophys. Res. Commun. 230:1997;143-146.
31. Maley F., Trimble R. B., Tarentino A. L., Plummer T. H. Jr. Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal. Biochem. 180:1989;195-204.