Endotoxin Induces Increased Intracellular Cathepsin B Activity in THP-1 Cells

References

• Page R C, Schroeder H E. Periodontitis in Man and Other Animals. A Comparative Review. Karger, Basel 1982; 17–57; 222–263
   Google Scholar
• Slots J. Subgingival microflora and periodontal disease. J. Clin. Periodontal. 1979; 6: 351–382
   PubMed Web of Science ®Google Scholar
• Williams R. Medical progress: periodontal disease. N. Engl. J. Med. 1990; 322: 373–382
   PubMed Web of Science ®Google Scholar
• Cimasoni G. Crevicular fluid updated. monographs in oral sciences, H M Myers. Karger, Basel 1983; 1–152
   Google Scholar
• Kunimatsu K, Yamamoto K, Ichimaru E, Kato Y, Kato I. Cathepsin B, H and L activities in gingival crevicular fluid from chronic adult periodontitis patients and experimental gingivitis subjects. J. Periodont. Res. 1990; 25: 69–73
   PubMedGoogle Scholar
• Trabandt A, Muller-Ladner U, Kriegsmann J, Gay R E, Gay S. Expression of proteolytic cathepsin B, D and L in periodontal gingival fibroblasts and tissues. Lab. Invest. 1995; 73: 205–212
   PubMed Web of Science ®Google Scholar
• Lah T, Skaleric U, Babnik J, Turk V. Cathepsin B, D and L in inflamed human gingiva. J. Periodont. Res. 1985; 20: 458–466
   PubMedGoogle Scholar
• Etherington D J, Evans P J. The action of cathepsin B and collagenoiytic cathepsin in the degradation of collagen. Acta Biol. Med. Ger. 1977; 36: 1555–1563
   PubMedGoogle Scholar
• Cardozo C., Kurtz C, Lesser M. Degradation of rat lung collagens by cathepsin B. J. Lab. Clin. Med. 1992; 119: 169–175
   PubMedGoogle Scholar
• Barrett A J, Kirschke H., Cathepsin B, Cathepsin H, Cathepsin L. Methods of Enzymol. 1981; 80: 535–561
   PubMed Web of Science ®Google Scholar
• Etherington D J. Proteinases in connective tissue breakdown. Excerpta Medica 1980; 75: 87–103
   Google Scholar
• Lah T T, Buck M R, Honn K V, et al. Degradation of laminin by human tomor cathepsin B. Clin. Exp. Metastasis 1989; 7: 461–468
   PubMedGoogle Scholar
• Adams D O, Hamilton T A. The cell biology of macrophage activation. Ann. Rev. Immunol. 1984; 2: 283–318
   PubMed Web of Science ®Google Scholar
• Adams D O, Hamilton T A. Molecular transductional mechanisms by which IFN-γ and other signals regulate macrophage development. Immunol. Rev. 1987; 97: 5
   PubMed Web of Science ®Google Scholar
• Hamilton T A. Molecular mechanisms in the activation of mononuclear phagocytes. Immunopharmacology, T J Rogers, S C Gilman. Telford Press, New Jersey 1988; 213
   Google Scholar
• Rietschel E T, Brade H. Bacterial endotoxins. Sci. Amer. 1992; 267: 54
   PubMed Web of Science ®Google Scholar
• Tsuchiya S, Yamabe M, Yamaguchi Y, Kobayashi Y, Konno T, Tada K. Establishment and characterization of a human acute monocytic leukemia cell line (THP-1). Int. J. Cancer 1980; 26: 171–176
   PubMed Web of Science ®Google Scholar
• Bever C T, Snyder D S, Endres R O, Morgan K D, Postlethwaite A, Whitaker J N. Activation of astrocytic lysosomal proteinases by factors released by mononuclear leukocytes. Neurochem. Res. 1989; 14: 37–41
   PubMedGoogle Scholar
• Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 1987; 162: 156–159
   PubMed Web of Science ®Google Scholar
• Sambrook J, Fritsch E F, Maniatis T. Molecular Cloning: A laboratory Manual. Cold Spring Harbor, Cold Spring Harbor, NY 1989
   Google Scholar
• Cieri M, Bever C T. Gamma interferon induced increases in cathepsin B activity are blocked by alpha and beta interferons (Type I interferon). FASEB J. 1990; 4: A339
   Google Scholar
• Page R. The role of inflammatory mediators in the pathogenesis of periodontal disease. J. Periodont. Dis. 1991; 26: 230–242
   PubMed Web of Science ®Google Scholar
• Klausen B, Evans R, Nangavaram S, Ramamurthy N, Golub L, Sfintescu C. Periodontal bone loss and gingival proteinase activity in gnotobiotic rats immunized with Bacteroides gingivalis. Oral Microbiol. Immunol. 1991; 6: 193–201
   PubMedGoogle Scholar
• Sodek J, Overall C. Matrix metalloproteinases in periodontal tissue remodeling. Matrix 1992; 1(Suppl)352–362
   PubMedGoogle Scholar
• Birkedal-Hansen H, Moore G, Bodden M, Windsor L, Birkedal-Hansen B, DeCarlo A. Matrix metalloproteinases. Crit. Rev. Oral Biol. Med. 1993; 4: 197–250
   PubMedGoogle Scholar
• Eeckhout Y, Vaes G. Further studies on the activation of procollagenase, the latent precursor of bone collagenase: effects of lysosomal cathepsin B, plasmin and kallikrein, and spontaneous activation. Biochem. J. 1977; 166: 21–31
   PubMed Web of Science ®Google Scholar
• Dalet-Fumeron V, Guinec N, Pagano M. In vitro activation of pro-cathepsin B by three serine proteases: leucocyte elastase, cathepsin G, and the urokinase-type plasminogen activator. FEBS Lett. 1993; 332: 251–254
   PubMed Web of Science ®Google Scholar
• Unemori E, Werb Z. Collagenase expression and endogenous activation in rabbit synovial fibroblasts stimulated by the calcium ionophore A23187. J. Biol. Chem. 1988; 31: 16252–16259
   Google Scholar
• Tanaka K, Ikegaki N, Ichihara A. Effects of leupeptin and pepstatin on protein turnover in adult rat hepatocytes in primary culture. Arch. Biochem. Biophys 1981; 208: 296–304
   PubMedGoogle Scholar
• Maciewicz R, Wotton S. Degradation of cartilage matrix components by the cysteine proteinases, Cathepsin B and L. Biomed. Biochim. Acta 1991; 50: 561–564
   PubMedGoogle Scholar
• Nguyen Q, Mort J, Roughley P. Cartilage proteoglycan is degradated more extensively by cathepsin L than cathepsin B. Biochem. J. 1992; 66: 569–573
   Google Scholar
• Mizuochi T, Yee S T, Kasai M, Kakiuchi T, Muno D, Kominami E. Both cathepsin B and cathepsin D are necessary for processing of ovalbumin as well as for degradation of class II MHC invariant Chain. Immunol. Lett. 1994; 43: 189–193
   PubMed Web of Science ®Google Scholar
• Reyes V E, Lu S, Humphreys R E. Cathepsin B cleavage of Ii from class II MHC alpha-and beta-chains. J. Immunol. 1991; 146: 3877–3880
   PubMedGoogle Scholar
• Roche P A, Cresswell P. Proteolysis of the class II associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules. Proc. Natl. Acad. Sci. U. S. A. 1991; 88: 3150–3154
   PubMed Web of Science ®Google Scholar
• Daibata M, Xu M, Humphreys R E, Reyes V E. More efficient peptide binding to MHC class II molecules during cathepsin B digestion of Ii than after Ii release. Mol. Immunol. 1994; 31: 255–260
   PubMed Web of Science ®Google Scholar
• Matsunaga Y, Saibara T, Kido H, Katunuma N. Participation of cathepsin B in processing of antigen presentation to MHC class II. FEBS Lett. 1993; 324: 325–330
   PubMedGoogle Scholar
• Jonsson R, Pitts A, Lue C, Gay S, Mestecky J. Immunoglobulin isotype distribution of locally produced autoantibodies to collagen type I in adult periodontitis: relationship to periodontal treatment. J. Clin. Periodont. 1991; 18: 703–707
   PubMed Web of Science ®Google Scholar
• Cox S, Eley B. Detection of cathepsin B-and L-, elastase-, tryptase-, trypsin-, and dipeptidyl peptidase IV-like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin. J. Periodont. Res. 1989; 24: 353–361
   PubMed Web of Science ®Google Scholar
• Eley B, Cox S. Correlation of gingival crevicular fluid proteases with clinical and radiological measurements of periodontal attachment loss. J. Dent. 1992; 20: 90–99
   PubMed Web of Science ®Google Scholar
• Vaes G. Cellular biology and biochemical mechanism of bone resorption. A review of recent developments on the formation, activation and mode of action of osteoclasts. Clin. Ortho. Rel. Res. 1988; 231: 239–271
   PubMed Web of Science ®Google Scholar
• Eley B, Cox S. Cathepsin B and L-like activities at local gingival tissue sites of chronic periodontitis patients. I. Clin. Periodontol. 1991; 18: 499–504
   PubMedGoogle Scholar
• Morrison D C, Ryan J L. Bacterial endotoxins and host immune responses. Adv. Immunol. 1979; 28: 293–450
   PubMedGoogle Scholar
• Pabst M J, Johnston R B. Bacterial lipopolysaccharide: a mediator of inflammation. Handbook of Inflammation, P M Henson, R C. Murphy. Elsevier, New York 1989; 361–393
   Google Scholar
• Morrison D C, Ryan J L. Endotoxins and disease mechanisms. Annu. Rev. Med. 1987; 38: 417–432
   PubMed Web of Science ®Google Scholar
• Lesser M, Chang J C, Orlowski M. Cathepsin B and D activity in stimulated peritoneal macrophages. Mol. Cell. Biochem. 1985; 69: 67–73
   PubMedGoogle Scholar
• Morland B. Cathepsin B activity in human blood monocytes during differentiation in vitro. Scand. J. Immunol. 1985; 22: 9–16
   PubMed Web of Science ®Google Scholar
• Ward C J, Crocker J, Chan S J, Stockley R A, Burnett D. Changes in the expression of elastase and cathepsin B with differentiation of U937 promonocytes by GMCSF. Biochem. Biophys. Res. Commun. 1990; 167: 659–664
   PubMedGoogle Scholar
• Taylor J L, Grossberg S E. Recent progress in interferon research: molecular mechanism of regulation, action and virus circumvention. Virus Res. 1990; 15: 1–26
   PubMedGoogle Scholar
• Baron S, Dianzani F, Stanton G J, Fleischmann W R. The interferon system: a current review to 1987. University of Texas, Austin, TX 1987
   Google Scholar
• Dianzani F, Antonelli G. Physiological mechanism of production and action of interferons in response to viral infections. Adv. Exp. Med. Biol. 1989; 257: 47–60
   PubMedGoogle Scholar
• Nelson B E, Borden E C. Interferons: biological and clinical effects. Semin. Surg. Oncol. 1989; 5: 391–401
   PubMedGoogle Scholar
• Baron S, Coppenhaver D H, Dianzani F, et al. Introduction to the interferon system; interferon-principles and medical applications. University of Texas, Galveston, TX 1992
   Google Scholar
• Cooper S M, Sriram S, Ranges G E. Suppression of murine collagen-induced arthritis with monoclonal anti-Ia antibodies and augmentation with IFN-γ. J. Immunol. 1988; 141: 1958
   PubMedGoogle Scholar
• Jacob C O, Holoshitz J, van der Meide P, Strober S, McDevitt H O. Heterogenous effects of interferon-γ in adjuvant arthritis. J. Immunol. 1989; 142: 1500
   PubMedGoogle Scholar
• Gaffney E V, Lingenfelter S E, Koch G A, Lisi P J, Chu C W, Tsai S C. Regulation by interferon-γ of function in the acute monocytic leukemia cell line, THP-1. J. Leukocyte Biol. 1988; 43: 248–255
   PubMedGoogle Scholar
• Harris P E, Ralph P, Litcofsky P, Moore M A. Distinct activities of interferon-γ, lymphokine, and cytokine differentiation-inducing factors acting on the human monoblastic leukemia cell line U937. Cancer Res. 1985; 45: 9
   PubMed Web of Science ®Google Scholar
• Qian F, Chan S J, Achkar C., Steiner D F, Frankfater A. Transcriptional regulation of cathepsin B expression in B16 melanomas of varying metastatic potential. Biochem. Biophys. Res. Commun. 1994; 202: 429–436
   PubMedGoogle Scholar
• Sloane B F, Moin K, Krepela E, Rozhin J. Cathepsin B and its endogenous inhibitors: the role in tumor malignancy. Cancer and Metastasis Reviews 1990; 9: 333–352
   PubMed Web of Science ®Google Scholar
• Rao N K, Shi G P, Chapman H A. Urokinase receptor is a multifunctional protein: influence of receptor occupancy on macrophage gene expression. J. Clin. Invest. 1995; 96: 465–474
   PubMedGoogle Scholar
• Keppler D, Waridel P, Abrahamson M, Bachmann D, Berdoz J, Sordat B. Latency of cathepsin B secreted by human colon carcinoma cells is not linked to secretion of cystatin C and is relieved by neutrophil elastase. Biochim. Biophys. Acta 1994; 1226: 117–125
   PubMedGoogle Scholar
• Burnett D, Abrahamson M, Devalia J L, Sapsford R J, Davies R J, Buttle D J. Synthesis and secretion of procathepsin B and cystatin C by human bronchial epithelial cells in vitro: modulation of cathepsin B activity by nertrophil elastase. Arch. Biochem. Biophys 1995; 317: 305–310
   PubMed Web of Science ®Google Scholar