Cathepsin S from Bovine Spleen. Purification, Distribution, Intracellular Localization and Action on Proteins

Overview

Journal Biochem J

Specialty Biochemistry

Date 1989 Dec 1

PMID 2690828

Citations 55

Authors

H KIRSCHKE

B Wiederanders

D Bromme

A Rinne

Affiliations

Soon will be listed here.

Abstract

Cathepsin S was detected in bovine kidney, spleen, lymph nodes and lung by immunochemical methods. The immunostaining of cathepsin S in kidney was concentrated to the cells of the proximal tubule, where the enzyme was present in cytoplasmic granules. The purification method for cathepsin S from bovine spleen involved (NH4)2SO4 fractionation, chromatography on CM-Sephadex C-50, gel filtration on Sephacryl S-200 and chromatofocusing (pH 8.0-6.0). The enzyme was partially destroyed by autolysis of the homogenate at pH 4.2. The isoelectric point of cathepsin S was 7.0. Cathepsin S was found to hydrolyse proteins at a similar rate to cathepsin L below pH 7.0. At pH values of 7.0-7.5 cathepsin S retained most of its activity, whereas cathepsin L was completely inactive.

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References

Etherington D . Bovine spleen cathepsin B1 and collagenolytic cathepsin. A comparative study of the properties of the two enzymes in the degradation of native collagen. Biochem J. 1976; 153(2):199-209. PMC: 1172563. DOI: 10.1042/bj1530199. View

KIRSCHKE H, Langner J, Wiederanders B, Ansorge S, Bohley P . Cathepsin L. A new proteinase from rat-liver lysosomes. Eur J Biochem. 1977; 74(2):293-301. DOI: 10.1111/j.1432-1033.1977.tb11393.x. View

Hsu S, RAINE L, FANGER H . Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures. J Histochem Cytochem. 1981; 29(4):577-80. DOI: 10.1177/29.4.6166661. View

Wiederanders B, Schaper S, KIRSCHKE H . Isolation and some properties of a cathepsin E type proteinase from rat spleen. Biomed Biochim Acta. 1989; 48(1):23-32. View

KIRSCHKE H, Locnikar P, Turk V . Species variations amongst lysosomal cysteine proteinases. FEBS Lett. 1984; 174(1):123-7. DOI: 10.1016/0014-5793(84)81089-3. View

Bromme D, Steinert A, Friebe S, FITTKAU S, Wiederanders B, KIRSCHKE H . The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B. Biochem J. 1989; 264(2):475-81. PMC: 1133604. DOI: 10.1042/bj2640475. View

Barrett A, KIRSCHKE H . Cathepsin B, Cathepsin H, and cathepsin L. Methods Enzymol. 1981; 80 Pt C:535-61. DOI: 10.1016/s0076-6879(81)80043-2. View

Wiederanders B, KIRSCHKE H . Antibodies to rat liver cathepsins: characterization and use for the identification of enzyme precursors. Biomed Biochim Acta. 1986; 45(11-12):1421-31. View

Bohley P, KIRSCHKE H, Langner J, Ansorge S . . FEBS Lett. 1969; 5(3):233-236. DOI: 10.1016/0014-5793(69)80341-8. View

10.

Woessner Jr J . The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acid. Arch Biochem Biophys. 1961; 93:440-7. DOI: 10.1016/0003-9861(61)90291-0. View

11.

Mason R, Taylor M, Etherington D . Purification and characterisation of collagenolytic cathepsins from rabbit liver. FEBS Lett. 1982; 146(1):33-6. DOI: 10.1016/0014-5793(82)80699-6. View

12.

Maciewicz R, Etherington D . A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen. Biochem J. 1988; 256(2):433-40. PMC: 1135428. DOI: 10.1042/bj2560433. View

13.

Wiederanders B, KIRSCHKE H, Schaper S . The azocasein-urea-pepstatin assay discriminates between lysosomal proteinases. Biomed Biochim Acta. 1986; 45(11-12):1477-83. View

14.

Rinne A, Jarvinen M, KIRSCHKE H, Wiederanders B, Hopsu-Havu V . Demonstration of cathepsins H and L in rat tissues. Biomed Biochim Acta. 1986; 45(11-12):1465-76. View

15.

KIRSCHKE H, Schmidt I, Wiederanders B . Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC 3.4.22.15). Biochem J. 1986; 240(2):455-9. PMC: 1147438. DOI: 10.1042/bj2400455. View

16.

Etherington D . The purification of bovine cathepsin B1 and its mode of action on bovine collagens. Biochem J. 1974; 137(3):547-57. PMC: 1166156. DOI: 10.1042/bj1370547. View

17.

Langner J, Ansorge S, Bohhley P, KIRSCHKE H, Hanson H . Intracellular protein breakdown. I. Activity determinations of endoipeptidases using protein substrates. Acta Biol Med Ger. 1971; 26(5):935-51. View

18.

Burnette W . "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981; 112(2):195-203. DOI: 10.1016/0003-2697(81)90281-5. View

19.

Kregar I, Locnikar P, Popovic T, Suhar A, Lah T, Ritonja A . Bovine intracellular cysteine proteinases. Acta Biol Med Ger. 1981; 40(10-11):1433-8. View

20.

Turnsek T, Kregar I, LEBEZ D . Acid sulphydryl protease from calf lymph nodes. Biochim Biophys Acta. 1975; 403(2):514-20. DOI: 10.1016/0005-2744(75)90079-0. View