Gene targeting of the cysteine peptidase cathepsin H impairs lung surfactant in mice

PLoS ONE

Volumn 6, Issue 10, 2011, Pages

  Bühling, Frank ^a   Kouadio, Martin ^b   Chwieralski, Caroline E ^c   Kern, Ursula ^b   Hohlfeld, Jens M ^d   Klemm, Nicole ^b   Friedrichs, Nicole ^b   Roth, Wera ^b   Deussing, Jan M ^b,e   Peters, Christoph ^b   Reinheckel, Thomas ^b  

^a CARL THIEM KLINIKUM   (Germany)

^b UNIVERSITY OF FREIBURG   (Germany)

^c OTTO VON GUERICKE UNIVERSITY   (Germany)

^d FRAUNHOFER INSTITUTE FOR TOXICOLOGY AND EXPERIMENTAL MEDICINE   (Germany)

^e MAX PLANCK INSTITUTE OF PSYCHIATRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; CATHEPSIN H; LUNG SURFACTANT; PHOSPHOLIPID; SURFACTANT PROTEIN B; SURFACTANT ASSOCIATED PROTEIN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; EMBRYO; EMBRYONIC STEM CELL; ENZYME ACTIVITY; GENE CONSTRUCT; GENE EXPRESSION; GENE TARGETING; GROWTH RETARDATION; IN VIVO STUDY; LIPID COMPOSITION; LUNG ALVEOLUS SURFACE TENSION; LUNG FUNCTION; LUNG LAVAGE; MALE; MOUSE; NONHUMAN; PROTEIN SECRETION; REPORTER GENE; ANIMAL; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; HUMAN; LUNG; METABOLISM; PATHOLOGY; PHENOTYPE;

MUS;

ANIMALS; CATHEPSIN H; GENE EXPRESSION REGULATION; GENE TARGETING; HUMANS; LUNG; MICE; PHENOTYPE; PULMONARY SURFACTANT-ASSOCIATED PROTEINS; PULMONARY SURFACTANTS;

EID: 84857134891     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026247     Document Type: Article

References (28)

1. Rawlings ND, Barrett AJ, Bateman A, (2010) MEROPS: the peptidase database. Nucleic Acids Res 38: D227-233.
2. Puzer L, Cotrin SS, Alves MF, Egborge T, Araujo MS, et al. (2004) Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L. Arch Biochem Biophys 430: 274-283.
3. Hagemann S, Gunther T, Dennemarker J, Lohmuller T, Bromme D, et al. (2004) The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles. Eur J Cell Biol 83: 775-780.
4. Tedelind S, Poliakova K, Valeta A, Hunegnaw R, Yemanaberhan EL, et al. (2010) Nuclear cysteine cathepsin variants in thyroid carcinoma cells. Biol Chem 391: 923-935.
5. Reiser J, Adair B, Reinheckel T, (2010) Specialized roles for cysteine cathepsins in health and disease. J Clin Invest 120: 3421-3431.
6. Brix K, Dunkhorst A, Mayer K, Jordans S, (2008) Cysteine cathepsins: cellular roadmap to different functions. Biochimie 90: 194-207.
7. Vasiljeva O, Reinheckel T, Peters C, Turk D, Turk V, et al. (2007) Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr Pharm Des 13: 387-403.
8. Baudys M, Meloun B, Gan-Erdene T, Fusek M, Mares M, et al. (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.
9. Kirschke H, Langner J, Wiederanders B, Ansorge S, Bohley P, et al. (1977) Cathepsin H: an endoaminopeptidase from rat liver lysosomes. Acta Biol Med Ger 36: 185-199.
10. Koga H, Mori N, Yamada H, Nishimura Y, Tokuda K, et al. (1992) Endo- and aminopeptidase activities of rat cathepsin H. Chem Pharm Bull (Tokyo) 40: 965-970.
11. Guncar G, Podobnik M, Pungercar J, Strukelj B, Turk V, et al. (1998) Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Structure 6: 51-61.
12. Vasiljeva O, Dolinar M, Turk V, Turk B, (2003) Recombinant human cathepsin H lacking the mini chain is an endopeptidase. Biochemistry 42: 13522-13528.
13. Dodt J, Reichwein J, (2003) Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase. Biol Chem 384: 1327-1332.
14. Ueno T, Linder S, Na CL, Rice WR, Johansson J, et al. (2004) Processing of pulmonary surfactant protein B by napsin and cathepsin H. J Biol Chem 279: 16178-16184.
15. Brasch F, Ten Brinke A, Johnen G, Ochs M, Kapp N, et al. (2002) Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes. Am J Respir Cell Mol Biol 26: 659-670.
16. D'Angelo ME, Bird PI, Peters C, Reinheckel T, Trapani JA, et al. (2010) Cathepsin H Is an Additional Convertase of Pro-granzyme B. J Biol Chem 285: 20514-20519.
17. Nogee LM, (2004) Alterations in SP-B and SP-C expression in neonatal lung disease. Annu Rev Physiol 66: 601-623.
18. Tokieda K, Whitsett JA, Clark JC, Weaver TE, Ikeda K, et al. (1997) Pulmonary dysfunction in neonatal SP-B-deficient mice. Am J Physiol 273: L875-882.
19. Guttentag S, Robinson L, Zhang P, Brasch F, Buhling F, et al. (2003) Cysteine protease activity is required for surfactant protein B processing and lamellar body genesis. Am J Respir Cell Mol Biol 28: 69-79.
20. Weaver TE, Lin S, Bogucki B, Dey C, (1992) Processing of surfactant protein B proprotein by a cathepsin D-like protease. Am J Physiol 263: L95-103.
21. Lu J, Qian J, Keppler D, Cardoso WV, (2007) Cathespin H is an Fgf10 target involved in Bmp4 degradation during lung branching morphogenesis. J Biol Chem 282: 22176-22184.
22. Gocheva V, Chen X, Peters C, Reinheckel T, Joyce JA, (2010) Deletion of cathepsin H perturbs angiogenic switching, vascularization and growth of tumors in a mouse model of pancreatic islet cell cancer. Biol Chem 391: 937-945.
23. Chirgwin JM, Przybyla AE, MacDonald RJ, Rutter WJ, (1979) Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18: 5294-5299.
24. Saftig P, Hetman M, Schmahl W, Weber K, Heine L, et al. (1995) Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. Embo J 14: 3599-3608.
25. Hohlfeld JM, Ahlf K, Enhorning G, Balke K, Erpenbeck VJ, et al. (1999) Dysfunction of pulmonary surfactant in asthmatics after segmental allergen challenge. Am J Respir Crit Care Med 159: 1803-1809.
26. Enhorning G, (1977) Pulsating bubble technique for evaluating pulmonary surfactant. J Appl Physiol 43: 198-203.
27. Wasano K, Hirakawa Y, (1994) Lamellar bodies of rat alveolar type 2 cells have late endosomal marker proteins on their limiting membranes. Histochemistry 102: 329-335.
28. Albrecht S, Usmani SM, Dietl P, Wittekindt OH, (2010) Plasma membrane trafficking in alveolar type II cells. Cell Physiol Biochem 25: 81-90.