Renaturation of SPARC expressed in Escherichia coli requires isomerization of disulfide bonds for recovery of biological activity

International Journal of Biochemistry and Cell Biology

Volumn 28, Issue 9, 1996, Pages 1031-1043

  Bassuk, James A ^a,c   Braun, Laura P ^a   Motamed, Kouros ^a   Baneyx, François ^b   Sage, E Helene ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b University of Washington   (United States)

^c UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

BM 40; Extracellular matrix; Osteonectin; Recombinant protein expression; SPARC

Indexed keywords

OSTEONECTIN; RECOMBINANT PROTEIN;

ARTICLE; CELL INCLUSION; CELL INTERACTION; DNA LIBRARY; ENDOTHELIUM CELL; ESCHERICHIA COLI; EXTRACELLULAR MATRIX; GENE EXPRESSION; GENETIC TRANSFORMATION; HUMAN; ISOMERISM; MOLECULAR CLONING; PLASMID; POLYMERASE CHAIN REACTION; PROTEIN PROCESSING; PROTEIN PURIFICATION; PROTEIN STRUCTURE;

ESCHERICHIA COLI; VERTEBRATA;

EID: 0030250219     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/1357-2725(96)00036-2     Document Type: Article

References (32)

1. Alliel P. M., Perin J. P., Jolles P. and Bonnet F. J. (1993) Testican, a multidomain testicular proteoglycan resembling modulators of cell social behaviour. Eur. J. Biochem. 21, 347-350.
2. Anfinsen C. B. (1973) Principles that govern the folding of protein chains. Science 181, 223-230.
3. Bassuk J. A., Iruela-Arispe M. L., Lane T. F., Benson J. M., Berg R. A. and Sage E. H. (1993) Molecular analysis of chicken embryo SPARC (osteonectin). Eur. J. Biochem. 218, 117-127.
4. Bassuk J. A., Baneyx F., Vernon R. B., Funk S. E. and Sage E. H. (1996) Expression of biologically active human SPARC from Escherichia coli. Arch. Biochem. Biophys. 325, 8-19.
5. Bassuk J. A. and Berg R. A. (1989) Protein disulphide isomerase: a multifunctional endoplasmic reticulum protein. Matrix 9, 244-258.
6. Engel J., Taylor W., Paulsson M., Sage H. and Hogan B. (1987) Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues. Biochemistry 26, 6958-6965.
7. 2+-binding glycoprotein SPARC modulates cell cycle progression in bovine aortic endothelial cells. Proc. Natl Acad. Sci. U.S.A. 88, 2648-2652.
8. Girard J.-P. and Springer T. A. (1995) Cloning from purified high endothelial venule cells of hevin, a close relative of the antiadhesive extracellular matrix protein SPARC. Immunity 2, 113-123.
9. Guermah M., Crisanti P., Laugier D., Dezelee P., Bidou L., Pessac B. and Calothy G. (1991) Transcription of a quail gene expressed in embryonic retinal cells is shut off sharply at hatching. Proc. Natl Acad. Sci. U.S.A. 88, 4503-4507.
10. Helenius A. (1994) How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Cell Biol. 5, 253-265.
11. Hochuli E., Dobeli H. and Schacher A. (1987) New metal chelate adsorbent is selective for proteins and peptides containing neighbouring histidine residues. J. Chromatogr. 411, 177-184.
12. 2+-binding module in BM-40/SPARC/ osteonectin. Nature: Struct. Biol. 3, 67-73.
13. Johnston I. G., Paladino T., Gurd J. W. and Brown I. R. (1990) Molecular cloning of SC1: a putative brain extracellular matrix glycoprotein showing partial similarity to osteonectin/BM40/SPARC. Neuron 2, 165-176.
14. Kim P. S. and Arvan P. (1995) Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J. Cell Biol. 128, 29-38.
15. 2+-binding sites modulate cell shape. J. Cell. Biol. 111, 3065-3076.
16. Lane T. F., Iruela-Arispe M. L., Johnson R. and Sage E. H. (1994) SPARC is a source of copper-binding peptides that stimulate angiogenesis. J. Cell. Biol. 125, 929-943.
17. Lane T. F. and Sage E. H. (1994) The biology of SPARC, a protein that modulates cell-matrix interactions. FASEB J. 8, 163-173.
18. Maurer P., Hohenadl C., Hohenester E., Gohring W., Timpl R. and Engel J. (1995) The C-terminal portion of BM-40 (SPARC/osteonectin) is an autonomously folding and crystallisable domain that binds calcium and collagen IV. J. Mol. Biol. 253, 347-357.
19. Motamed K., Bassuk J. A. and Sage E. H. (1995) SPARC as a counter adhesive protein: structural and functional correlates. In Tenascin and Counteradhesive Molecules of the Extracellular Matrix (Edited by K. Crossin). Harwood Academic Press, Amsterdam, pp. 127-144.
20. 2+-binding EF-hand. J. Cell. Biochem. 57, 341-350.
21. Patthy L. (1991) Modular exchange principles in proteins. Curr. Opin. Struct. Biol. 1, 351-361.
22. Pichler R. H., Bassuk J. A., Hugo C., Reed M. J., Eng E., Gordon K. L., Pippin J., Alpers C. A., Couser W. G., Sage E. H. and Johnson R. J. (1996) SPARC is expressed by mesangial cells in experimental mesangial proliferative nephritis and inhibits PDGF-mediated mesangial cell proliferation in vitro. Am. J. Pathol., 148, 1153-1167.
23. Pottgiesser J., Maurer P., Mayer U., Nischt R., Mann K., Timpl R., Krieg T. and Engel J. (1994) Changes in calcium and collagen IV binding caused by mutations in the EF hand and other domains of extracellular matrix protein BM-40 (SPARC, osteonectm). J. Mol. Biol. 238, 563-574.
24. 2+. Biochem. Cell Biol. 70, 56-62.
25. 2+-binding EF-hand sequence. J. Cell. Biochem. 57, 127-140.
26. Sage E. H. and Bornstein P. (1991) Extracellular proteins that modulate cell-matrix interactions: SPARC, tenascin, and thrombospondin. J. biol. Chem. 266, 14831-14834.
27. Sage E. H. and Vernon R. B. (1994) Regulation of angiogenesis by extracellular matrix: the growth and the glue. J. Hypertens. Suppl. 12, S145-152.
28. 2+-dependent binding to the extracellular matrix. J. Cell Biol. 109, 341-356.
29. Schneider E. L., Bassuk J. A., Sage E. H. and Baneyx F. (1996) Factors affecting the aggregation of recombinant human SPARC (osteonectin, BM-40) in the cytoplasm of Escherichia coli. Biotech. Progr., submitted.
30. Shibanuma M., Mashimo J., Mita A., Kuroki T. and Nose K. (1993) Cloning from a mouse osteoblastic cell line of a set of transforming-growth-factor β1-regulated genes, one of which seems to encode a follistatin-related polypeptide. Eur. J. Biochem. 217, 15-19.
31. Xie R.-L. and Long G. L. (1995) Role of N-linked glycosylation in human osteonectin. J. biol. Chem. 270, 23212-23217.
32. Yost J. C., Bell A., Scale R. and Sage E. H. (1994) Purification of biologically active SPARC expressed in Saccharomyces cerevisiae. Arch. Biochem. Biophys. 314, 50-63.