Liquefaction and cavity formation in pulmonary TB: A simple method in rabbit skin to test inhibitors

Tuberculosis

Volumn 89, Issue 4, 2009, Pages 243-247

  Dannenberg Jr , Arthur M ^a,b  

^a JOHNS HOPKINS UNIVERSITY   (United States)

^b Center for Tuberculosis Research   (United States)

Author keywords

Pulmonary tuberculosis; Tuberculosis cavity formation; Tuberculosis in rabbits; Tuberculosis liquefaction; Tuberculosis ulceration in skin

Indexed keywords

ACID PHOSPHATASE; ALICAFORSEN; AMPRENAVIR PHOSPHATE; ASPARTIC PROTEINASE INHIBITOR; ATAZANAVIR; AZATHIOPRINE; BETA GALACTOSIDASE; BETA GLUCURONIDASE; CATHEPSIN D; CYTOCHROME C OXIDASE; DEOXYRIBONUCLEASE; ENZYME INHIBITOR; ESTERASE; HYALURONIDASE; HYDROLASE; LOPINAVIR; MATRIX METALLOPROTEINASE; PROTEINASE; PROTEINASE INHIBITOR; RIBONUCLEASE; RITONAVIR; SUCCINATE DEHYDROGENASE; TRIACYLGLYCEROL LIPASE;

ANIMAL EXPERIMENT; ANIMAL MODEL; BACTERIAL GROWTH; DELAYED HYPERSENSITIVITY; DESENSITIZATION; LIQUEFACTION; LUNG CAVITATION; LUNG TUBERCULOSIS; MACROPHAGE; MULTIDRUG RESISTANT TUBERCULOSIS; MYCOBACTERIUM BOVIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; RABBIT; REVIEW; SKIN TEST; SKIN ULCER; TUBERCULOSIS CONTROL;

ANIMALS; ANTITUBERCULAR AGENTS; DISEASE MODELS, ANIMAL; GUINEA PIGS; HUMANS; HYPERSENSITIVITY, DELAYED; MYCOBACTERIUM TUBERCULOSIS; PEPTIDE HYDROLASES; RABBITS; TUBERCULOSIS, CUTANEOUS; TUBERCULOSIS, PULMONARY;

EID: 67650725427     PISSN: 14729792     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tube.2009.05.006     Document Type: Review

References (62)

1. Dannenberg Jr. A.M. Pathogenesis of human tuberculosis: insights from the rabbit model (1966), American Society for Microbiology, Washington, DC
2. Converse P.J., Dannenberg Jr. A.M., Estep J.E., Sugisaki K., Abe Y., Schofield B.H., et al. Cavitary tuberculosis produced in rabbits by aerosolized virulent tubercle bacilli. Infect Immun 64 (1996) 4776-4787
3. Converse P.J., Dannenberg Jr. A.M., Shigenaga T., McMurray D.N., Phalen S.W., Stanford J.L., et al. Pulmonary bovine-type tuberculosis in rabbits: bacillary virulence, inhaled dose effects, tuberculin sensitivity, and Mycobacterium vaccae immunotherapy. Clin Diagn Lab Immunol 5 (1998) 871-888
4. Helke K., Mankowski J.L., and Manabe Y.C. Animal models of cavitation in pulmonary tuberculosis. Tuberculosis 86 (2006) 337-348
5. Heppleston A.G. Quantitative airborne tuberculosis in the rabbit. The course of human-type infection. J Exp Med 89 (1949) 597-610
6. Lurie M.B. Resistance to tuberculosis: experimental studies in native and acquired defensive mechanisms (1964), Harvard University Press, Cambridge, MA
7. Lurie M.B., Abramson S., and Heppleston A.G. On the response of genetically resistant and susceptible rabbits to the quantitative inhalation of human-type tubercle bacilli and the nature of resistance to tuberculosis. J Exp Med 95 (1952) 119-134
8. Manabe Y.C., Dannenberg Jr. A.M., Tyagi S.K., Hatem C.L., Yoder M., Woolwine S.C., et al. Different strains of Mycobacterium tuberculosis cause various spectrums of disease in the rabbit model of tuberculosis. Infect Immun 71 (2003) 6004-6011
9. Yamamura Y. The pathogenesis of tuberculous cavities. Adv Tuberc Res 9 (1958) 13-37
10. Yamamura Y., Ogawa Y., Yamagata H., and Yamamura Y. Prevention of tuberculous cavity formation by desensitization with tuberculin-active peptide. Am Rev Respir Dis 109 (1974) 594-601
11. Yamamura Y., Yasaka S., Yamaguchi M., Endo K., Iwakura H., Nakamura S., et al. Studies on the experimental tuberculous cavity. Med J Osaka Univ 5 (1954) 187-197
12. Kruml J., Trnka L., Urbancík R., and Kuska J. Histologic differences between experimental cavernous tuberculosis in rabbits and human cavitary disease. Am Rev Respir Dis 92 (1965) 299-302
13. Yamamura Y., Ogawa Y., Yamagata H., and Yamamura Y. Prevention of tuberculous cavity formation by immunosuppressive drugs. Am Rev Respir Dis 98 (1968) 720-723
14. Canetti G. The tubercle bacillus in the pulmonary lesion of man: histobacteriology and its bearing on the therapy of pulmonary tuberculosis (1955), Springer Publishing Co., New York, NY
15. Long E.R. The Chemistry and chemotherapy of tuberculosis: a compilation and critical review of existing knowledge on the chemistry of tubercle bacilli and their products, chemical changes and processes in the host, and chemical aspects of the treatment of tuberculosis. 3rd ed. (1958), Williams & Wilkins Co, Baltimore, MD [Bacillary factors: p. 52-61; host factors: p. 163-182]
16. Nedeltchev G., Raghunand T.R., Jassal M.S., Lun S., Cheng Q.J., and Bishai W.R. Extrapulmonary dissemination of Mycobacterium bovis but not Mycobacterium tuberculosis in a bronchoscopic rabbit model of cavitary tuberculosis. Infect Immun 77 (2009) 598-603
17. Pagel W. The role of the bacillus and of "heteroallergy" in tuberculous liquefaction. J Pathol Bacteriol 42 (1936) 417-424
18. Yoder M.A., Lamichhane G., and Bishai W.R. Cavitary tuberculosis: The "Holey Grail" of disease transmission. Curr Sci 86 (2004) 74-81
19. Grosset J. Mycobacterium tuberculosis in the extracellular compartment: an underestimated adversary. Antimicrob Agents Chemother 47 (2003) 833-836
20. Shigenaga T., Dannenberg Jr. A.M., Lowrie D.B., Said W., Urist M.J., Abbey H., et al. Immune responses in tuberculosis: antibodies and CD4/CD8 lymphocytes with vascular adhesion molecules and cytokines (chemokines) cause a rapid antigen-specific cell infiltration at sites of bacillus Calmette-Guérin reinfection. Immunology 102 (2001) 466-479
21. Sugisaki K., Dannenberg Jr. A.M., Abe Y., Tsuruta J., Su W.-J., Said W., et al. Non-specific and immune-specific up-regulation of cytokines in rabbit dermal tuberculous (BCG) lesions. J Leukoc Biol 63 (1998) 440-450
22. Dannenberg Jr. A.M. Cellular hypersensitivity and cellular immunity in the pathogenesis of tuberculosis: specificity, systemic and local nature, and associated macrophage enzymes. Bacteriol Rev 32 (1968) 85-102
23. Dannenberg Jr. A.M., and Sugimoto M. Liquefaction of caseous foci in tuberculosis. Editorial. Am Rev Respir Dis 113 (1976) 257-259
24. Weiss C., and Boyar-Manstein M.L. On the mechanism of liquefaction of tubercles. 1. The behavior of endocellular proteinases in tubercles developing in the lungs of rabbits. Am Rev Respir Dis 63 (1951) 694-705
25. Weiss C., and Singer F.M. Mechanism of softening of tubercles. II. Behavior of desoxyribonuclease in tubercles developing in the lungs of rabbits. Arch Pathol 55 (1953) 516-530
26. Weiss C., Tabachnick J., and Cohen H.P. Mechanism of softening of tubercles. III. Hydrolysis of protein and nucleic acid during anaerobic autolysis of normal and tuberculous lung tissue in vitro. Arch Pathol 57 (1954) 179-193
27. Rojas-Espinosa O., Dannenberg Jr. A.M., Sternberger L.A., and Tsuda T. Role of cathepsin D in the pathogenesis of tuberculosis. A histochemical study employing unlabeled antibodies and the peroxidase-antiperoxidase complex. Am J Pathol 74 (1974) 1-17
28. Tsuda T., Dannenberg Jr. A.M., Ando M., Rojas-Espinosa O., and Shima K. Enzymes in tuberculous lesions hydrolyzing protein, hyaluronic acid and chondroitin sulfate: a study of isolated macrophages and developing and healing rabbit BCG lesions with substrate film techniques; the shift of enzyme pH optima towards neutrality in "intact" cells and tissues. J Reticuloendothel Soc 16 (1974) 220-231
29. Cunningham L. Histochemical observations of the enzymatic hydrolysis of gelatin films. J Histochem Cytochem 15 (1967) 292-298
30. Daoust R., and Amano H. Improved DNA film method for localizing DNAase activity in tissue sections. Exp Cell Res 24 (1961) 559-564
31. Daoust R. Histochemical localization of enzyme activities by substrate film methods: ribonucleases, deoxyribonucleases, proteases, amylase, and hyaluronidase. Int Rev Cytol 18 (1965) 191-221
32. Daoust R. Modified procedure for the histochemical localization of ribonuclease activity by the substrate film method. J Histochem Cytochem 14 (1966) 254-259
33. Elkington P.T.G., Nuttall R.K., Boyle J.J., O'Kane C.M., Horncastle D.E., Edwards D.R., et al. Mycobacterium tuberculosis, not vaccine BCG, specifically up-regulates matrix metalloproteinase-1. Am J Resp Crit Care Med 172 (2005) 1596-1604
34. Elkington P.T.G., Emerson J.E., Lopez-Pascua L.D.C., O'Kane C.M., Horncastle D.E., Boyle J.J., et al. Mycobacterium tuberculosis up-regulates matrix metalloproteinase-1 secretion from human airway epithelial cells via a p38 MAPK switch. J Immunol 175 (2005) 5333-5340
35. Oshima Y., Hagihara T., Mizuta Y., Hattori S., and Mishima J. Histochemical study on the relationship between tuberculosis and lipase activity. I. Lipase and lipids of tuberculous lesions. Kekkaku 30 (1955) 716-720
36. Umezawa H., Aoyagi T., Morishima H., Matsuzaki M., Hamada M., and Takeuchi T. Pepstatin, a new pepsin inhibitor produced by actinomycetes. J Antibiot 23 (1970) 259-262
37. Aoyagi T., Kunimoto S., Morishima H., Takeuchi T., and Umezawa H. Effect of Pepstatin on acid proteases. J Antibiot (Japan) 24 (1971) 687-694
38. McAdoo M.H., Dannenberg Jr. A.M., Hayes C.J., James S.P., and Sanner J.H. Inhibition of the cathepsin D-type proteinase of macrophages by Pepstatin, a specific pepsin inhibitor, and other substances. Infect Immun 7 (1973) 655-665
39. Dannenberg Jr. A.M., Walter P.C., and Kapral F.A. A histochemical study of phagocytic and enzymatic functions of rabbit mononuclear and polymorphonuclear exudate cells and alveolar macrophages. II. The effect of particle ingestion on enzyme activity; two phases of in vitro activation. J Immunol 90 (1963) 448-465
40. Higuchi S., Suga M., Dannenberg Jr. A.M., Affronti L.F., Azuma I., Daniel T.M., et al. Persistence of protein, carbohydrate and wax components of tubercle bacilli in dermal BCG lesions. Am Rev Respir Dis 123 (1981) 397-401
41. Schwarz W.H., and Zverlov V.V. Protease inhibitors in bacteria: an emerging concept for the regulation of bacterial protein complexes?. Mol Microbiol 60 (2006) 1323-1326
42. Bishai W.R. Library of M. tuberculosis mutants. Available from: (2006). www.webhosts.nts/jhu.edu/target/
43. Umezawa H. Enzyme inhibitors of microbial origin (1972), University Park Press, Baltimore
44. Abbenante G., and Fairlie D.P. Protease inhibitors in the clinic. Med Chem 1 (2005) 71-104
45. Gewirtz A.T., and Sitaraman S.C. Technology evaluation: Alicaforsen, Isis. Curr Opin Mol Ther 7 (2005) 273-281
46. Dannenberg Jr. A.M., and Smith E.L. Proteolytic enzymes of lung. J Biol Chem 215 (1955) 45-54
47. Dannenberg Jr. A.M., and Smith E.L. Action of proteinase I of bovine lung. Hydrolysis of the oxidized B chain of insulin; polymer formation from amino acid esters. J Biol Chem 215 (1955) 55-66
48. Rojas-Espinosa O., Dannenberg Jr. A.M., Murphy P.A., Straat P.A., Huang P.C., and James S.P. Purification and properties of the cathepsin D-type proteinase from beef and rabbit lung and its identification in macrophages. Infect Immun 8 (1973) 1000-1008
49. Bernardi G. Mechanism of action and structure of acid deoxyribonuclease. Adv Enzymol Relat Areas Mol Biol 31 (1968) 1-49
50. Dickson K.A., Haigis M.C., and Raines R.T. Ribonuclease inhibitor: structure and function. Prog Nucleic Acid Res Mol Biol 80 (2005) 349-374
51. Olivecrona T., and Bengtsson-Olivecrona G. Lipoprotein lipase-the molecule and its interactions. Agents Actions 16 Suppl. (1984) 55-67
52. Quistad G.B., Liang S.N., Fisher K.J., Nomura D.K., and Casida J.E. Each lipase has a unique sensitivity profile for organophosphorus inhibitors. Toxicol Sci 91 (2006) 166-172
53. Shepherd R.E., and Fain J.N. Inhibition of rat fat cell triglyceride lipase by sulfonylureas. Fed Proc 36 (1977) 2732-2734
54. Uusitupa M. New aspects in the management of obesity: operation and the impact of lipase inhibitors. Curr Opin Lipidol 10 (1999) 3-7
55. Dannenberg Jr. A.M., and Bennett W.E. Hydrolases of mononuclear exudate cells and tuberculosis. I. Exudate characteristics, esterases, proteinases and lipase. Arch Pathol 76 (1963) 581-591
56. Dannenberg Jr. A.M., and Bennett W.E. Hydrolytic enzymes of rabbit mononuclear exudate cells. I. Quantitative assay and properties of certain proteases, nonspecific esterases and lipases of mononuclear and polymorphonuclear cells and erythrocytes. J Cell Biol 21 (1964) 1-13
57. Rojas-Espinosa O., Arce-Paredez P., Dannenberg Jr. A.M., and Kamenetz R.L. Macrophage esterase: identification, purification and properties of a chymotrypsin-like esterase from lung that hydrolyzes and transfers nonpolar amino acid esters. Biochim Biophys Acta 403 (1975) 161-179
58. 2 by the peroxidase-antiperoxidase technique in professional phagocytes (pulmonary alveolar macrophages and granulocytic and mononuclear peritoneal exudate cells) and in glycol methacrylate sections of dermal tuberculous (BCG) lesions. J Reticuloendothel Soc 34 (1983) 425-435
59. Sugimoto M., Dannenberg Jr. A.M., Wahl L.M., Ettinger Jr. W.H., Hastie A.T., Daniels D.C., et al. Extracellular hydrolytic enzymes of rabbit dermal tuberculous lesions and tuberculin reactions collected in skin chambers. Am J Pathol 90 (1978) 583-608
60. Hastie A.T. Monospecific antibodies to rabbit lung ribonucleases. J Biol Chem 256 (1970) 12553-12560
61. Meyer O.T., Dannenberg Jr. A.M., and Mizunoe K. Hydrolytic enzymes of rabbit mononuclear and polymorphonuclear exudate cells and pulmonary alveolar macrophages. III. Deoxyribonuclease and ribonuclease: properties and quantitative assay in macrophages from tuberculous and control inbred rabbits. J Reticuloendothel Soc 7 (1970) 15-31
62. Lurie M.B., Heppleston A.G., Abramson S., and Swartz I.B. An evaluation of the method of quantitative airborne infection and its use in the study of the pathogenesis of tuberculosis. Am Rev Tuberc 61 (1950) 765-797