Antiproteases and retinoids for treatment of chronic obstructive pulmonary disease

Bibliography

• TURINO GM: The origins of a concept: the protease-antiprotease imbalance hypothesis. Chest (2002) 122:1058–1060.
   PubMed Web of Science ®Google Scholar
• HOGG JC, SENIOR PM: Chronic obstructive pulmonary disease - part 2: pathology and biochemistry of emphysema. Thorax (2002) 57:830–834.
   PubMed Web of Science ®Google Scholar
• BARNES PJ: New concepts in chronic obstructive pulmonary disease. Ann. Rev Med. (2003) 54:113–129.
   PubMed Web of Science ®Google Scholar
• •Extensive and up-to-date explanation of current ideas on the pathophysiology of COPD and how this differs from asthma.
   Google Scholar
• CULPITT SV, ROGERS DF: Evaluation of current pharmacotherapy of chronic obstructive pulmonary disease. Expert Opin. Pharmacother. (2000) 1:1007–1020.
   PubMedGoogle Scholar
• •Critical discussion of the effectiveness, or otherwise, of current treatment for COPD, with some evaluation of newer treatments available.
   Google Scholar
• BARNES PJ: Therapy of chronic obstructive pulmonary disease. Pharmacol The]: (2003) 97:87–94.
   PubMed Web of Science ®Google Scholar
• DONNELLY LE, ROGERS DF: Therapy for COPD in the 21st Century. Drugs (2003) 63(19).
   PubMed Web of Science ®Google Scholar
• SHAPIRO SD: Proteinases in chronic obstructive pulmonary disease. Biochem. Soc. Trans. (2002) 30:98–102.
   PubMed Web of Science ®Google Scholar
• MASSARO D, DE CARLO MG: Retinoids, alveolus formation, and alveolar deficiency: clinical implications. Am. J. Respic Cell Mol Biol (2003) 28:271–274.
   PubMed Web of Science ®Google Scholar
• •Useful editorial on retinoids as they pertain to the lung by one of the leading researchers in the field.
   Google Scholar
• NORMAN P: Pulmonary Diseases. DiseaseTrend and Market Opportunities Financial Times Business Ltd, London (1999).
   Google Scholar
• NATIONAL HEART, LUNG & BLOOD INST. WORLD HEALTH ORGANIZATION: Global Initiative for Chronic Obstructive Lung Disease. National Institutes of Health (2001) (Publication number 2701) .
   Google Scholar
• •Current best guidelines, and additional information, on clinical management of COPD.
   Google Scholar
• HURD S: The impact of COPD on lung health worldwide: epidemiology and incidence. Chest (2000) 117:1S–4S.
   Google Scholar
• BRITTON M: The burden of COPD in the UK: results from the Confronting COPD survey. Respic Med. (2003) 97(Suppl.C):S71–S79.
   Google Scholar
• MANNINO DM: COPD: epidemiology, prevalence, morbidity and mortality, and disease heterogeneity. Chest (2002) 121:121S–126S.
   Google Scholar
• HALPERN MT, STANFORD RH, BORKER R: The burden of COPD in the USA: results from the confronting COPD survey. Respic Med. (2003) 97(Suppl.C):S81–S89.
   Google Scholar
• SULLIVAN SD, RAMSEY SD, LEE TA: The economic burden of COPD. Chest (2000) 117:5S–9S.
   Google Scholar
• FLETCHER C, PETO R: The natural history of chronic airflow obstruction. Br. Med. J. (1977) 1:1645–1648.
   PubMed Web of Science ®Google Scholar
• ••'Classical' original article on theepidemiology linking cigarette smoking to development of chronic airflow obstruction in susceptible smokers.
   Google Scholar
• ANTHONISEN NR, CONNETT JE, KILEY JP et al: Effects of smoking intervention and the use of an inhaled anticholinergic bronchodilator on the rate of decline of FEV1. The Lung Health Study. JAMA (1994) 272:1497–1505.
   Google Scholar
• ROGERS DF: Mucus pathophysiology in COPD: differences to asthma, and pharmacotherapy. Monaldi Arch. Chest Dis. (2000) 55:324–332.
   PubMedGoogle Scholar
• JEFFERY PK: Remodeling in asthma and chronic obstructive lung disease. km J. Respic Grit. Care Med. (2001) 164:S28–S38.
   PubMed Web of Science ®Google Scholar
• MAESTRELLI P, SAETTA M, MAPP CE, FABBRI LM: Remodeling in response to infection and injury. Airway inflammation and hypersecretion of mucus in smoking subjects with chronic obstructive pulmonary disease. Am. J. Respic Crit. Care Med. (2001) 164:S76–S80.
   Google Scholar
• TETLEY TD: Macrophages and the pathogenesis of COPD. Chest (2002) 121:156S–159S.
   Google Scholar
• STOCKLEY RA: Neutrophils and the pathogenesis of COPD. Chest (2002) 121:151S–155S.
   Google Scholar
• STOCKLEY RA: Proteases and antiproteases. Novartis Found. Symp. (2001) 234:189–199.
   PubMedGoogle Scholar
• JEFFERY PK: Comparison of the structural and inflammatory features of COPD and asthma. Giles F Filley Lecture. Chest (2000) 117(5:Supp1.1):251S–260S.
   Google Scholar
• BARNES PJ: Mechanisms in COPD: differences from asthma. Chest (2000) 117:10S–14S.
   Google Scholar
• BARNES PJ: Inhaled corticosteroids are notbeneficial in chronic obstructive pulmonary disease. Am. J. Respic Grit. Care Med. (2000) 161:342–344.
   PubMed Web of Science ®Google Scholar
• CALVERLEY PM: Inhaled corticosteroids are beneficial in chronic obstructive pulmonary disease. Am. J. Respic Crit. Care Med. (2000) 161:341–342.
   PubMed Web of Science ®Google Scholar
• STARCHER BC: Lung elastin and matrix. Chest (2000) 117:229S–234S.
   Google Scholar
• FORONLY R, D'ARMIENTO J: The role of collagenase in emphysema. Respic Res. (2001) 2:348–352.
   PubMed Web of Science ®Google Scholar
• OHBAYASHI H: Matrix metalloproteinases in lung diseases. Can: Protein Pept. Sci. (2002) 3:409–421.
   PubMed Web of Science ®Google Scholar
• •Extensive and thorough review of IVEVIPs and their role in pathophysiology of lung diseases, including COPD.
   Google Scholar
• SHIOMI T, OKADA Y, FORONJY R et al: Emphysematous changes are caused by degradation of Type III collagen in transgenic mice expressing MMP-1. Exp. Lung Res. (2003) 29:1–15.
   PubMed Web of Science ®Google Scholar
• PARKS WC, SHAPIRO SD: Matrix metalloproteinases in lung biology. Respic Res. (2001) 2:10–19.
   PubMed Web of Science ®Google Scholar
• STERNLICHT MD, WERB Z: How matrix metalloproteinases regulate cell behavior. Ann. Rev Cell Dev. Biol. (2001) 17:463–516.
   PubMed Web of Science ®Google Scholar
• KAJITA M, ITOH Y, CHIBA T et al.: Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J. Cell Biol. (2001) 153:893–904.
   PubMed Web of Science ®Google Scholar
• WALLACE AM, SANDFORD AJ: Genetic polymorphisms of matrix metalloproteinases: functional importance in the development of chronic obstructive pulmonary disease? Am. J. Pharmacogenomics (2002) 2:167–175.
   PubMedGoogle Scholar
• SELMAN M, MONTANO M, RAMOS C et al.: Tobacco smoke-induced lung emphysema in guinea pigs is associated with increased interstitial collagenase. Am. J. Physic] (1996) 271:L734–L743.
   Google Scholar
• FORONJY RE OKADA Y, COLE R, D'ARMIENTO J: Progressive adult-onset emphysema in transgenic mice expressing human MMP-1 in the lung. Am. j Physiol Lung Cell Ma Physiol (2003) 284:L727–L737.
   Google Scholar
• FINLAY GA, O'DRISCOLL LR, RUSSELL KJ et al.: Matrix metalloproteinase expression and production by alveolar macrophages in emphysema. Am. I Respir. Crit. Care Med. (1997) 156:240–247.
   Google Scholar
• SEGURA-VALDEZ L, PARDO A, GAXIOLA M, UHAL BD, BECERRIL C, SELMAN M: Upregulation of gelatinases A and B, collagenases 1 and 2, and increased parenchymal cell death in COPD. Chest (2000) 117:684–694.
   PubMed Web of Science ®Google Scholar
• IMAI K, DALAL SS, CHEN ES et al.: Human collagenase (matrix metalloproteinase-1) expression in the lungs of patients with emphysema. Am. j Respir. Crit. Care Med. (2001) 163:786–791.
   PubMed Web of Science ®Google Scholar
• JOOS L, HE JQ, SHEPHERDSON MB et al.: The role of matrix metalloproteinase polymorphisms in the rate of decline in lung function. Hum. Ma Genet. (2002) 11:569–576.
   PubMed Web of Science ®Google Scholar
• BETSUYAKU T, NISHIMURA M, TAKEYABU K et al.: Neutrophil granule proteins in bronchoalveolar lavage fluid from subjects with subclinical emphysema. Am. J. Respir. Crit. Care Med. (1999) 159:1985–1991.
   PubMed Web of Science ®Google Scholar
• FINLAY GA, RUSSELL KJ, MCMAHON KJ et al.: Elevated levels of matrix metalloproteinases in bronchoalveolar lavage fluid of emphysematous patients. Thorax (1997) 52:502–506.
   PubMed Web of Science ®Google Scholar
• •Original article showing that MMP-2 and, more importantly, MMP-9 are elevated in lungs of patients with emphysema and, thereby, linked to pathophysiology of COPD.
   Google Scholar
• OPDENAKKER G, VAN DEN STEEN PE et al.: Gelatinase B functions as regulator and effector in leukocyte biology. .1. Leukoc. Biol. (2001) 69:851–859.
   Google Scholar
• RUSSELL RE, CULPITT SV, DEMATOS C et al.: Release and activity of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 by alveolar macrophages from patients with chronic obstructive pulmonary disease. Am. J. Respir. Cell Ma Biol. (2002) 26:602–609.
   PubMed Web of Science ®Google Scholar
• MINEMATSU N, NAKAMURA H, TATENO H, NAKAJIMA T, YAMAGUCHI K: Genetic polymorphism in matrix metalloproteinase-9 and pulmonary emphysema. Biochem. Biophys. Res. Commun. (2001) 289:116–119.
   PubMed Web of Science ®Google Scholar
• SHAPIRO SD: Elastolytic metalloproteinases produced by human mononuclear phagocytes. Potential roles in destructive lung disease. Am. Respir Crit. Care Med (1994) 150:S160–S164.
   Web of Science ®Google Scholar
• BUSIEK DF, BARAGI V, NEHRING LC, PARKS WC, WELGUS HG: Matrilysin expression by human mononuclear phagocytes and its regulation by cytokines and hormones. Immunol (1995) 154:6484–6491.
   Web of Science ®Google Scholar
• WILSON CL, MATRISIANLM: Matrilysin: an epithelial matrix metalloproteinase with potentially novel functions. Intl: Biochem. Cell Biol. (1996) 28:123–136.
   PubMed Web of Science ®Google Scholar
• SU WY, JASKOT RH, RICHARDS J et al.: Induction of pulmonary matrilysin expression by combustion and ambient air particles. Am. I Physic] Lung Cell Ma Physic] (2000) 279:L152–L160.
   Web of Science ®Google Scholar
• COSGROVE GP, SCHWARZ MI, GERACI MW, BROWN KK, WORTHEN GS: Overexpression of matrix metalloproteinase-7 in pulmonary fibrosis. Chest (2002) 121:25S–26S.
   Google Scholar
• HAUTAMAKI RD, KOBAYASHI DK, SENIOR RM, SHAPIRO SD: Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice. Science (1997) 277:2002–2004.
   PubMed Web of Science ®Google Scholar
• •Original article demonstrating the importance of MIVIP-12 to development of emphysema in knockout mice.
   Google Scholar
• GRONSKI TJ Jr, MARTIN RL, KOBAYASHI DK et al.: Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase. J. Biol. Chem. (1997) 272:12189–12194.
   PubMed Web of Science ®Google Scholar
• WANG Z, ZHENG T, ZHU Z et a/.: Interferon-y induction of pulmonary emphysema in the adult murine lung. J. Exp. Med. (2000) 192:1587–1600.
   Google Scholar
• CHURG A, WANG RD, TAI H et al.: Macrophage metalloelastase mediates acute cigarette smoke-induced inflammation via tumor necrosis factor-alpha release. Am. J. Re9ch: Crit. Cam Med. (2003) 167:1083–1089.
   Google Scholar
• OHNISHI K, TAKAGI M, KUROKAWAY, SATOMI S, KONTTINEN YT: Matrix metalloproteinase-mediated extracellular matrix protein degradation in human pulmonary emphysema. Lab. Invest. (1998) 78:1077–1087.
   PubMed Web of Science ®Google Scholar
• JOOS L, PARE PD, SANDFORD AJ: Genetic risk factors of chronic obstructive pulmonary disease. Swiss. Med. Wk/y(2002) 132:27–37.
   PubMed Web of Science ®Google Scholar
• CAUGHEY GH: Serine proteinases of mastcell and leukocyte granules. A league of their own. Am. J. Respir Crit. Care Med. (1994) 150:S138–S142.
   Web of Science ®Google Scholar
• HEDSTROM L: Serine protease mechanism and specificity. Chem.Rev. (2002) 102:4501–4524.
   PubMed Web of Science ®Google Scholar
• BODE W, MEYER E Jr, POWERS JC: Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. Biochemistry (1989) 28:1951–1963.
   PubMed Web of Science ®Google Scholar
• LEE WL, DOWNEY GP: Leukocyte elastase: physiological functions and role in acute lung injury. Am. I Respir. Crit. Care Med. (2001) 164:896–904.
   PubMed Web of Science ®Google Scholar
• SHAPIRO SD: Neutrophil elastase: path clearer, pathogen killer, or just pathologic? Am. Respir. Cell Md. Biol. (2002) 26:266–268.
   PubMed Web of Science ®Google Scholar
• BELAAOUAJ A: Neutrophil elastase-mediated killing of bacteria: lessons from targeted mutagenesis. Microbes Infect. (2002) 4:1259–1264.
   PubMed Web of Science ®Google Scholar
• TKALCEVIC J, NOVELLI M, PHYLACTIDES M, IREDALE JP, SEGAL AW, ROES J: Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G. Immunity (2000) 12:201–210.
   PubMed Web of Science ®Google Scholar
• LAURELL C, ERIKSSON S: The electrophoretic a-1 globulin pattern of serum in arantitrypsin deficiency. Scand. Clin. Lab invest. (1963) 15:132–140.
   Web of Science ®Google Scholar
• MAHADEVA R, SHAPIRO SD: Experimental animal models of pulmonary emphysema. Thorax (2002) 57:908–914.
   PubMed Web of Science ®Google Scholar
• •Critical discussion of the relative usefulness of various animal models of COPD (see also [146] and [147]).
   Google Scholar
• LUCEY EC, STONE PJ, BREUER R et al: Effect of combined human neutrophil cathepsin G and elastase on induction of secretory cell metaplasia and emphysema in hamsters, with in vitro observations on elastolysis by these enzymes. Am. Rev Respir. Dis. (1985) 132:362–366.
   PubMed Web of Science ®Google Scholar
• SOMMERHOFF CP, NADEL JA, BASBAUM CB, CAUGHEY GH: Neutrophil elastase and cathepsin G stimulate secretion from cultured bovine airway gland serous cells. J. Clin. Invest. (1990) 85:682–689.
   PubMed Web of Science ®Google Scholar
• FISCHER BM, CUELLAR JG, DIEHL ML et al: Neutrophil elastase increases MUC4 expression in normal human bronchial epithelial cells. Am. j Physiol Lung Cell Mol Physiol (2003) 284:L671–L679.
   Web of Science ®Google Scholar
• FISCHER BM VOYNOW JA: Neutrophil elastase induces MUC5AC gene expression in airway epithelium via a pathway involving reactive oxygen species. Am. J. Respir. Cell Ma Biol. (2002) 26:447–452.
   PubMed Web of Science ®Google Scholar
• ROGERS DF: The airway goblet cell. Int. Biochem. Cell Biol. (2003) 35:1–6.
   PubMed Web of Science ®Google Scholar
• LE BARILLEC K, SI-TAHAR M, BALLOY V, CHIGNARD M: Proteolysis of monocyte CD14 by human leukocyte elastase inhibits lipopolysaccharide-mediated cell activation. I. Clin. Invest. (1999) 103:1039–1046.
   PubMed Web of Science ®Google Scholar
• VANDIVIER RW, FADOK VA, HOFFMANN PR et al: Elastase-mediated phosphatidylserine receptor cleavage impairs apoptotic cell clearance in cystic fibrosis and bronchiectasis. I Clin. Invest. (2002) 109:661–670.
   PubMed Web of Science ®Google Scholar
• GROSSO LE, SCOTT M: Peptide sequences selected by BA4, a tropoelastin-specific monoclonal antibody, are ligands for the 67-kDa bovine elastin receptor. Biochemistry (1993) 32:13369–13374.
   PubMed Web of Science ®Google Scholar
• UEMURA, Y. OKAMOTO K: Elastin-derived peptide induces monocyte chemotaxis by increasing intracellular cyclic GMP level and activating cyclic GMP dependent protein kinase. Biochem. Mol Biol. Int. (1997) 41:1085–1092.
   PubMedGoogle Scholar
• BANGALORE N, TRAVIS J, ONUNKA VC, POHL J, SHAFER WM:Identification of the primary antimicrobialdomains in human neutrophil cathepsin G.Biol Chem. (1990) 265:13584–13588.
   Web of Science ®Google Scholar
• REEVES EP, LU H, JACOBS HL et al: Killing activity of neutrophils is mediated through activation of proteases by K+ flux. Nature (2002) 416:291–297.
   PubMed Web of Science ®Google Scholar
• ROOS D, WINTERBOURN CC: Immunology. Lethal weapons. Science (2002) 296:669–671.
   Google Scholar
• MACIVOR DM, SHAPIRO SD, PHAM CT, BELAAOUAJ A, ABRAHAM SN, LEY TJ: Normal neutrophil function in cathepsin G-deficient mice. Blood (1999) 94:4282–4293.
   PubMed Web of Science ®Google Scholar
• LE BARILLEC K, PIDARD D, BALLO YV, CHIGNARD M: Human neutrophil cathepsin G down-regulates LPS-mediated monocyte activation through CD14 proteolysis. Leukoc. Biol. (2000) 68:209–215.
   PubMed Web of Science ®Google Scholar
• BANK U, KUPPER B, ANSORGE S: Inactivation of interleukin-6 by neutrophil proteases at sites of inflammation. Protective effects of soluble IL-6 receptor chains. Adv. Exp. Med. Biol. (2000) 477:431–437.
   PubMed Web of Science ®Google Scholar
• SHAMAMIAN P, SCHWARTZ JD, POCOCK BJ et al.: Activation of progelatinase A (MMP-2) by neutrophil elastase, cathepsin G, and proteinase-3: a role for inflammatory cells in tumor invasion and angiogenesis. 1 Cell Physiol (2001) 189:197–206.
   Google Scholar
• NUFER O, CORBETT M, WALZ A: Amino-terminal processing of chemokine ENA-78 regulates biological activity. Biochemistry (1999) 38:636–642.
   PubMed Web of Science ®Google Scholar
• SAMBRANO GR, HUANG W, FARUQI T, MAHRUS S, CRAIK C, COUGHLIN SR: Cathepsin G activates protease-activated receptor-4 in human platelets. J. Biol. Chem. (2000) 275:6819–6823.
   PubMed Web of Science ®Google Scholar
• OWEN CA, CAMPBELL EJ: The cell biology of leukocyte-mediated proteolysis. Leukoc. Biol. (1999) 65:137–150.
   PubMed Web of Science ®Google Scholar
• CAMPBELL EJ, CAMPBELL MA, OWEN CA: Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition.' Immunol (2000) 165:3366–3374.
   Web of Science ®Google Scholar
• RAO NV, WEHNER NG, MARSHALL BC, GRAY WR, GRAY BH, HOIDAL JR: Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties. Biol. Chem. (1991) 266:9540–9548.
   Google Scholar
• KAO RC, WEHNER NG, SKUBITZ KM, GRAY BH, HOIDAL JR: Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that produces emphysema in hamsters. J. Clin. Invest (1988) 82:1963–1973.
   Google Scholar
• PEZZATO E, DONA M, SARTOR L et al.: Proteinase-3 directly activates MMP-2 and degrades gelatin Matrigel; differential inhibition by Hepigallocatechin-3-gallate.f Leukoc. Biol. (2003) 74:88–94.
   Google Scholar
• CHAPMAN HA, RIESE RJ, SHI GP: Emerging roles for cysteine proteases in human biology. Ann. Rev Physiol (1997) 59:63–88.
   PubMed Web of Science ®Google Scholar
• WOLTERS PJ, CHAPMAN HA: Importance of lysosomal cysteine proteases in lung disease. Respic Res. (2000) 1:170–177.
   PubMedGoogle Scholar
• BUHLING F, FENGLER A, BRANDT W,WELTE T, ANSORGE S, NAGLER DK: Review: novel cysteine proteases of the papain family. Adv. Exp. Med. Biol. (2000) 477:241–254.
   PubMed Web of Science ®Google Scholar
• TAKAHASHI H, ISHIDOH K, MUNO D et al: Cathepsin L activity is increased in alveolar macrophages and bronchoalveolar lavage fluid of smokers. Am. Rev. Respic Dis. (1993) 147:1562–1568.
   PubMed Web of Science ®Google Scholar
• TAKEYABU K, BETSUYAKU T, NISHIMURA M et al.: Cysteine proteinases and cystatin C in bronchoalveolar lavage fluid from subjects with subclinical emphysema. Eui: Respic (1998) 12:1033–1039.
   PubMed Web of Science ®Google Scholar
• TAGGART CC, LOWE GJ, GREENE CM et al.: Cathepsin B, L, S cleave and inactivate secretory leucoprotease inhibitor. J. Biol. Chem. (2001) 276:33345–33352.
   PubMed Web of Science ®Google Scholar
• PADILLA ML, GALICKI NI, KLEINERMAN J, ORLOWSKI M, LESSER M: High cathepsin B activity in alveolar macrophages occurs with elastase-induced emphysema but not with bleomycin-induced pulmonary fibrosis in hamsters. Am. Pathol (1988) 131:92–101.
   PubMed Web of Science ®Google Scholar
• SCHWAIBLMAIR M, VOGELMEIER C: Alpha 1-antitrypsin. Hope on the horizon for emphysema sufferers? Drugs Aging (1998) 12:429–440.
   PubMed Web of Science ®Google Scholar
• STOCKLEY RA, BAYLEY DL, UNSAL I, DOWSON LJ: The effect of augmentation therapy on bronchial inflammation in alphal-antitrypsin deficiency. Am. I Respic Grit. Care Med. (2002) 165:1494–1498.
   PubMed Web of Science ®Google Scholar
• ••Phase I clinical study on arantitrypsin,Prolastin, augmentation in 12 subjects with arantitrypsin deficiency.
   Google Scholar
• STOLLER JK, ROUHANI F, BRANTLY M et al.: Biochemical efficacy and safety of a new pooled human plasma arantitrypsin, Respitin. Chest (2002) 122:66–74.
   PubMed Web of Science ®Google Scholar
• MITSUHASHI H, ASANO S, NONAKA T, HAMAMURA I, MASUDA K, KIYOKI M: Administration of truncated secretory leukoprotease inhibitor ameliorates bleomycin-induced pulmonary fibrosis in hamsters. Am. Respic Crit. Care Med. (1996) 153:369–374.
   PubMed Web of Science ®Google Scholar
• MITSUHASHI H, ASANO S, NONAKA T, MASUDA K, KIYOKI M: Potency of truncated secretory leukoprotease inhibitor assessed in acute lung injury models in hamsters. I Pharmacol Exp. Thec (1997) 282:1005–1010.
   PubMed Web of Science ®Google Scholar
• TREMBLAY GM, VACHON E, LAROUCHE C, BOURBONNAIS Y: Inhibition of human neutrophil elastase-induced acute lung injury in hamsters by recombinant human pre-elafin (trappin-2). Chest (2002) 121:582–588.
   PubMed Web of Science ®Google Scholar
• OHBAYASHI H: Neutrophil elastase inhibitors as treatment for COPD. Expert Opin. Investig. Drugs (2002) 11:965–980.
   PubMed Web of Science ®Google Scholar
• LUISETTI M, STURANI C, SELLA D et al: MR-889, a neutrophil elastase inhibitor, in patients with chronic obstructive pulmonary disease: a double-blind, randomized, placebo-controlled clinical trial. Eur. Respir J. (1996) 9:1482–1486.
   PubMed Web of Science ®Google Scholar
• KAPUI Z, VARGA M, URBAN-SZABO K et al.: Biochemical and pharmacological characterization of 24942-piperidinoethoxy)-4-0x0-4H-pyrido [1,2-a]pyrimidin-2-yloxymethyl) 4 (1 methylethyl) - 6-methoxy-1,2-benzisothiazol-3 (2H)-one-1,1-dioxide (SSR-69071), a novel, orally active elastase inhibitor. Pharmacol Exp. The]: (2003) 305:451–459.
   Google Scholar
• VARGA M, KAPUI Z, BATORI S et al: A novel orally active inhibitor of HLE. Eur. J. Med. Chem. (2003) 38:421–425.
   PubMed Web of Science ®Google Scholar
• DOVE A: MMP inhibitors: glimmers of hope amidst clinical failures. Nat. Med. (2002) 8:95.
   PubMed Web of Science ®Google Scholar
• SELMAN M, CISNEROS-LIRA J, GAXIOLA M et al.: Matrix metalloproteinases inhibition attenuates tobacco smoke-induced emphysema in guinea-pigs. Chest (2003) 123:1633–1641.
   PubMed Web of Science ®Google Scholar
• CHAMBON P: A decade of molecular biology of retinoic acid receptors. FASEB (1996) 10:940–954.
   PubMed Web of Science ®Google Scholar
• NAGPAL S, ATHANIKARJ, CHANDRARATNA RA: Separation of transactivation AP1 antagonism functions of retinoic acid receptor a. J. Biol. Chem. (1995) 270:923–927.
   PubMed Web of Science ®Google Scholar
• ONG DE, CHYTIL F: Changes in levels of cellular retinol- and retinoic-acid-binding proteins of liver and lung during perinatal development of rat. Proc. Natl. Acad. Sci. USA (1976) 73:3976–3978.
   PubMed Web of Science ®Google Scholar
• MASSARO GD, MASSARO D: Postnatal treatment with retinoic acid increases the number of pulmonary alveoli in rats. Am. J. Physiol (1996) 2701305–L310.
   Google Scholar
• BENOIT G, ALTUCCI L, FLEXOR M et al.: PAR-independent RXR signaling induces t(15;17) leukemia cell maturation. EMBO J. (1999) 18:7011–7018.
   PubMed Web of Science ®Google Scholar
• BERGER J, WAGNER JA: Physiological and therapeutic roles of perwdsome proliferator-activated receptors. Diabetes Technol Ther. (2002) 4:163–174.
   PubMedGoogle Scholar
• ELDER JT, FISHER GJ, ZHANG QY et al: Retinoic acid receptor gene expression in human skin. J. Invest. Dermatol (1991) 96:425–433.
   PubMed Web of Science ®Google Scholar
• REES J: The molecular biology of retinoic acid receptors: orphan from good family seeks home. Br. J. Dermatol (1992) 126:97–104.
   PubMed Web of Science ®Google Scholar
• FISHER GJ, TALWAR HS, XIAO JH et al: Immunological identification and functional quantitation of retinoic acid and retinoid X receptor proteins in human skin. J. Biol. Chem. (1994) 269:20629–20635.
   PubMed Web of Science ®Google Scholar
• MASSARO GC, MASSARO D, CHAMBON P: Retinoic acid receptor-a regulates pulmonary alveolus formation in mice after, but not during, perinatal period. Am. J. Physiol Lung Cell Ma Physiol (2003) 284:L431–L433.
   Web of Science ®Google Scholar
• MASSARO GD, MASSARO D, CHAN WY et al.: Retinoic acid receptor-beta: an endogenous inhibitor of the perinatal formation of pulmonary alveoli. Physiol Cenomics (2000) 4:51–57.
   PubMed Web of Science ®Google Scholar
• MCGOWAN S, JACKSON SK, JENKINS-MOORE M, DAI HH, CHAMBON P, SNYDER JM: Mice bearing deletions of retinoic acid receptors demonstrate reduced lung elastin and alveolar numbers. Am..! Respir Cell Mol Biol. (2000) 23:162–167.
   PubMed Web of Science ®Google Scholar
• NO AUTHORS LISTED: Selective PAR-y agonists for treating emphysema. Expert Opin. Ther. Patents (2002) 12:1107–1110.
   Web of Science ®Google Scholar
• GUZMAN K, GRAY TE, YOON JH, NETTESHEIM P: Quantitation of mucin RNA by PCR reveals induction of both MUC2 MUC5AC mRNA levels by retinoids. Am. J. Physiol (1996) 271:L1023–L1028.
   Google Scholar
• YOON JH, GRAY T, GUZMAN K, KOO JS, NETTESHEIM P: Regulation of the secretory phenotype of human airway epithelium by retinoic acid, triiodothyronine, and extracellular matrix. Am. J. Respir: Cell MM. Biol. (1997) 16:724–731.
   PubMed Web of Science ®Google Scholar
• KOO JS, YOON JH, GRAY T, NORFORD D, JETTEN AM, NETTESHEIM P: Restoration of the mucous phenotype by retinoic acid in retinoid-deficient human bronchial cell cultures: changes in mucin gene expression. Am. J. Respir: Cell MM. Biol. (1999) 20:43–52.
   PubMed Web of Science ®Google Scholar
• KOO JS, JETTEN AM, BELLONI P, YOON JH, KIM YD, NETTESHEIM P: Role of retinoid receptors in the regulation of mucin gene expression by retinoic acid in human tracheobronchial epithelial cells. Biochem. J. (1999) 338:351–357.
   PubMed Web of Science ®Google Scholar
• APFEL C, BAUER F, CRETTAZ M et al: A retinoic acid receptor a antagonist selectively counteracts retinoic acid effects. Proc: Natl. Acad. Sci. USA (1992) 89:7129–7133.
   PubMed Web of Science ®Google Scholar
• KOO JS, MM YD, JETTEN AM, BELLONI p, NETTESHEIM P: Overexpression of mucin genes induced by interleukin-1 13, tumor necrosis factor-a, lipopolysaccharide, and neutrophil elastase is inhibited by a retinoic acid receptor a antagonist. Exp. Lung Res (2002) 28:315–332.
   PubMed Web of Science ®Google Scholar
• MASSARO GD MASSARO D: Retinoic acid treatment abrogates elastase-induced pulmonary emphysema in rats. Nat. Med. (1997) 3:675–677.
   PubMed Web of Science ®Google Scholar
• ••'Classical' original article demonstratingthat retinoic acid suppresses development of experimentally-induced pulmonary emphysema.
   Google Scholar
• BELLONI PN, GARVIN L, MAO CP, BAILEY-HEALY I, LEAFFER D: Effects of all- trans-retinoic acid in promoting alveolar repair. Chest (2000) 117:235S–241S.
   Google Scholar
• AN L, ZHANG H, PANG B et al: [Prophylactic effect of retinoic acid on chronic obstructive pulmonary emphysema in rats]. Zhonghua Be. He. He. Hu Xi. Za Zhi. (2002) 25:356–359.
   PubMedGoogle Scholar
• MESHI B, VITALIS TZ, IONESCU D et al.: Emphysematous lung destruction by cigarette smoke. The effects of latent adenoviral infection on the lung inflammatory response. Am. J. Respir: Cell MM. Biol. (2002) 26:52–57.
   Google Scholar
• MAO JT, GOLDIN JG, DERMAND J et al: A pilot study of all- trans-retinoic acid for the treatment of human emphysema. Am. J. Respir. Crit. Care Med. (2002) 165:718–723.
   PubMed Web of Science ®Google Scholar
• •Phase I clinical study on the effect of ATRA treatment on 20 patients with severe emphysema.
   Google Scholar
• KRUMME D, WENZEL H, TSCHESCHE H: Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases. FEBS Lett. (1998) 436:209–212.
   PubMed Web of Science ®Google Scholar
• KRUMME D, TSCHESCHE H: Oxal hydroxamic acid derivatives with inhibitory activity against matrix metalloproteinases. Bioorg. Med. Chem. Lett. (2002) 12:933–936.
   PubMed Web of Science ®Google Scholar
• COPELAND RA, LOMBARDO D, GIANNARAS J, DECICCO CP: Estimating Ki values for tight binding inhibitors from dose-response plots. Bioorg. Med. Chem. Lett. (1995) 5:1947–1952.
   Web of Science ®Google Scholar
• MOHLER KM, SLEATH PR, FITZNER JN et al.: Protection against a lethal dose of endotwdn by an inhibitor of tumour necrosis factor processing. Nature (1994) 370:218–220.
   PubMed Web of Science ®Google Scholar
• KOIVUNEN E, GAY DA, RUOSLAHTI E: Selection of peptides binding to the a5131 integrin from phage display library. Biol. Chem. (1993) 268:20205–20210.
   Web of Science ®Google Scholar
• MAGERT HJ, STANDKER L, KREUTZMANN P et al.: LEKTI, a novel 15-domain type of human serine proteinase inhibitor. Biol. Chem. (1999) 274:21499–21502.
   Web of Science ®Google Scholar
• MAGERT HJ, KREUTZMANN P, DROGEMULLER K et al: The 15-domain serine proteinase inhibitor LEKTI: biochemical properties, genomic organization, and pathophysiological role. Eur.j Med. Res. (2002) 7:49–56.
   PubMed Web of Science ®Google Scholar
• MAGERT HJ, KREUTZMANN P, STANDKER L, WALDEN M, DROGEMULLER K, FORSSMANN WG: LEKTI: a multidomain serine proteinase inhibitor with pathophysiological relevance. hat. Biochem. Cell Biol. (2002) 34:573–576.
   PubMed Web of Science ®Google Scholar
• DEL MAR EG, LARGMAN C, BRODRICK JW, FASSETT M, GEOKAS MC: Substrate specificity of human pancreatic elastase 2. Biochemistry (1980) 19:468–472.
   PubMed Web of Science ®Google Scholar
• GROUTAS WC, KUANG R, VENKATARAMAN R, EPP JB, RUAN S, PRAKASH O: Structure-based design of a general class of mechanism-based inhibitors of the serine proteinases employing a novel amino acid-derived heterocyclic scaffold. Biochemistry (1997) 36:4739–4750.
   PubMed Web of Science ®Google Scholar
• SCHECHTER NM, JORDAN LM, JAMES AM, COOPERMAN BS, WANG ZM, RUBIN H: Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus substrate properties. J. Biol. Chem. (1993) 268:23626–23633.
   Google Scholar
• MAUBACH G, SCHILLING K, ROMMERSKIRCH W et al: The inhibition of cathepsin S by its propeptide-specificity and mechanism of action. Eur: Biochem. (1997) 250:745–750.
   PubMedGoogle Scholar
• HORVATH ZS, CORTHALS GL, WRIGLEY CW, MARGOLIS J: Multifunctional apparatus for electrokinetic processing of proteins. Electrophoresis (1994) 15:968–971.
   PubMed Web of Science ®Google Scholar
• FEHRENBACH H: Animal models of chronic obstructive pulmonary disease: some critical remarks. Pathobiology (2002) 70:277–283.
   PubMed Web of Science ®Google Scholar
• WRIGHT JL, CHURG A: Animal models of cigarette smoke-induced COPD. Chest (2002) 122:301S–306S.
   Google Scholar
• JONES PW, QUIRK FH, BAVEYSTOCK CM: The St George's respiratory questionnaire. Respir: Med. (1991) 85\(Supp1.13):25–31.
   Google Scholar
• NEWELL JD Jr: CT of emphysema. Radial. Clin. North Am. (2002) 40:31-42v1i.
   Google Scholar
• KHARITONOV SA, BARNES PJ: Exhaled markers of pulmonary disease. Am. J. Respir: Grit. Care Med. (2001) 163:1693–1722.
   PubMed Web of Science ®Google Scholar