Effect of matrix metalloproteinases activity on outflow in perfused human organ culture

Investigative Ophthalmology and Visual Science

Volumn 39, Issue 13, 1998, Pages 2649-2658

  Bradley, John M B ^a   Vranka, Janice ^a,b   Colvis, Christine M ^a,b   Conger, Dean M ^a   Alexander, J Preston ^a   Fisk, Aurelie S ^a   Samples, John R ^a   Acott, Ted S ^a,b,c  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^c OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE;

ANTERIOR EYE SEGMENT; AQUEOUS HUMOR OUTFLOW; ARTICLE; CELL VIABILITY; ENZYME ACTIVITY; EXTRACELLULAR MATRIX; HUMAN; HUMAN TISSUE; PRIORITY JOURNAL; PROTEIN EXPRESSION;

AQUEOUS HUMOR; CELL SURVIVAL; EXTRACELLULAR MATRIX; HUMANS; INTERLEUKIN-1; METALLOENDOPEPTIDASES; MODELS, BIOLOGICAL; ORGAN CULTURE TECHNIQUES; PERFUSION; RECOMBINANT PROTEINS; TISSUE INHIBITOR OF METALLOPROTEINASES; TRABECULAR MESHWORK;

EID: 0031768664     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (78)

1. Nagase H. Matrix metalloproteinases. A mini-review. Contrib Nephrol. 1994;107:85-93.
2. Matrisian LM. The matrix-degrading metalloproteinases. Bioessays. 1992;14:455-463.
3. Birkedal-Hansen H, Moore WG, Bodden MK, et al. Matrix metalloproteinases: a review. Crit Rev Oral Biol Med. 1993;4:197-250.
4. Murphy G, Docherty AJ. The matrix metalloproteinases and their inhibitors. Am J Respir Cell Mol Biol. 1992;7:120-125.
5. Murphy G, Willenbrock F, Crabbe T, et al. Regulation of matrix metalloproteinase activity. Ann NY Acad Sci. 1994;732:31-41.
6. Woessner JFJ. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 1991;5:2145-2154.
7. Alexander CM, Werb Z. Extracellular matrix degradation. In: Hay ED, ed. Cell Biology of Extracellular Matrix. 2nd ed. New York: Plenum; 1991:255-302.
8. 37 active-site zinc complex in latency and a "cysteine switch" mechanism for activation. Proc Natl Acad Sci USA. 1990;87:364-368.
9. Van Wart HE, Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA. 1990;87:5578-5582.
10. Nagase H, Enghild JJ, Suzuki K, Salvesen G. Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl) mercuric acetate. Biochemistry. 1990;29:5783-5789.
11. Murphy G, Ward R, Gavrilovic J, Atkinson S. Physiological mechanisms for metalloproteinase activation. Matrix Suppl. 1992;1: 224-230.
12. Murphy G, Willenbrock F, Ward RV, et al. The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases. Biochem J. 1992;283:637-641.
13. Murphy G, Atkinson S, Ward R, Gavrilovic J, Reynolds JJ. The role of plasminogen activators in the regulation of connective tissue metalloproteinases. Ann NY Acad Sci. 1992;667:1-12.
14. Will H, Atkinson SJ, Butler GS, Smith B, Murphy G. The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. J Biol Chem. 1996;271:17119-17123.
15. Strongin AY, Collier I, Bannikov G, et al. Mechanism of cell surface activation of 72-kDa type IV collagenase: isolation of the activated form of the membrane metalloprotease. J Biol Chem. 1995;270: 5331-5338.
16. Brown PD, Kleiner DE, Unsworth EJ, Stetler-Stevenson WG. Cellular activation of the 72 kDa type IV procollagenase/TIMP-2 complex. Kidney Int. 1993;43:163-170.
17. Ogata Y, Enghild JJ, Nagase H. Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9. J Biol Chem. 1992;267:3581-3584.
18. Denhardt DT, Feng B, Edwards DR, Cocuzzi ET, Malyankar UM. Tissue inhibitor of metalloproteinases (TIMP, aka EPA): structure, control of expression and biological functions. Pharmacol Ther. 1993;59:329-341.
19. Kleiner DEJ, Tuuttila A, Tryggvason K, Stetler-Stevenson WG. Stability analysis of latent and active 72-kDa type IV collagenase: the role of tissue inhibitor of metalloproteinases-2 (TIMP-2). Biochemistry. 1993;32:1583-1592.
20. Stetler-Stevenson WG, Liotta LA, Kleiner DEJ. Extracellular matrix 6: role of matrix metalloproteinases in tumor invasion and metastasis. FASEB J. 1993;7:1434-1441.
21. Willenbrock F, Crabbe T, Slocombe PM, et al. The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A. Biochemistry. 1993;32:4330-4337.
22. O'Connell JP, Willenbrock F, Docherty AJ, Eaton D, Murphy G. Analysis of the role of the COOH-terminal domain in the activation, proteolytic activity, and tissue inhibitor of metalloproteinase interactions of gelatinase B. J Biol Chem. 1994;269:14967-14973.
23. Howard EW, Banda MJ. Binding of tissue inhibitor of metalloproteinases 2 to two distinct sites on human 72-kDa gelatinase. J Biol Chem. 1991;266:17972-17977.
24. Goldberg GI, Strongin A, Collier IE, Genrich LT, Marmer BL. Interaction of 92-kDa type FV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin. J Biol Chem. 1992;267:4583-4591.
25. Becker JW, Marcy AI, Rokosz LL, et al. Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Protein Sci. 1995;4:1966-1976.
26. Van Doren SR, Kurochkin AV, Hu W, et al. Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor. Protein Sci. 1995;4:2487-2498.
27. Gooley PR, O'Connell JF, Marcy AI, et al. The NMR structure of the inhibited catalytic domain of human stromelysin-1. Nature Struct Biol. 1994;1:111-118.
28. Williamson RA, Martorell G, Carr MD, et al. Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family. Biochemistry. 1994; 33:11745-11759.
29. Quigley HA. Open-angle glaucoma. N Engl J Med. 1993;328:1097-1106.
30. Quigley HA, Vitale S. Models of open-angle glaucoma prevalence and incidence in the United States. Invest Ophthalmol Vis Sci. 1997;38:83-91.
31. Quigley HA. Number of people with glaucoma worldwide. Br J Ophthalmol. 1996;80:389-393.
32. Shields MB. Textbook of Glaucoma. 3rd ed. Baltimore: Williams & Wilkins; 1992.
33. Brubaker RF. Flow of aqueous humor in humans. Invest Ophthalmol Vis Sci. 1991;32:3145-3166.
34. Larsson L-I, Rettig ES, Brubaker RF. Aqueous flow in open-angle glaucoma. Arch Ophthalmol. 1995;113:283-286.
35. Kaufman PL. Pressure-dependent outflow. In: Ritch R, Shields MB, Krupin T, eds. The Glaucomas. Vol. I. 2nd ed. St. Louis: Mosby; 1996;307-335.
36. Bárany EH, Scotchbrook S. Influence of testicular hyaluronidase on the resistance to flow through the angle of the anterior chamber. Acta Physiol Scand. 1954;30:240-248.
37. Acott TS. Trabecular extracellular matrix regulation. In: Drance SM, Van Buskirk EM, Neufeld AH, eds. Pharmacology of Glaucoma. Baltimore: Williams & Wilkins; 1992:125-157.
38. Acott TS. Biochemistry of aqueous humor outflow. In: Kaufman PL, Mittag TW, eds. Textbook of Ophthalmology. London: Mosby; 1994;7:1.47-41.78.
39. Acott TS, Wirtz MK. Biochemistry of aqueous outflow. In Ritch R, Shields MB, Krupin T, eds. The Glaucomas. Vol. 1. 2nd ed. St Louis: Mosby Year Book; 1996;281-305.
40. Lütjen-Drecoll E, Tamm E. Differences in the amount of "plaque-material" in the outflow system of eyes with chronic simple and exfoliation glaucoma. In: Krieglstein GK, ed. Glaucoma Update III. Berlin, Heidelberg: Springer-Verlag; 1987:17-22.
41. Lütjen-Drecoll E, Rohen JW. Morphology of aqueous outflow pathways in normal and glaucomatous eyes. In: Ritch R, Shields MB, Krupin T, eds. The Glaucomas. 2nd ed. St. Louis: Mosby Year Book; 1996;1:89-124.
42. Lütjen-Drecoll E, Shimizu T, Rohrbach M, Rohen JW. Quantitative analysis of "plaque material" in the inner- and outer wall of Schlemm's canal in normal and glaucomatous eyes. Exp Eye Res. 1986;42:443-455.
43. Murphy CG, Johnson M, Alvarado JA. Juxtacanalicular tissue in pigmentary and primary open angle glaucoma. Arch Ophthalmol. 1992;110:1779-1785.
44. Knepper PA, Goossens W, Hvizd M, Palmberg PF. Glycosaminoglycans of the human trabecular meshwork in primary open-angle glaucoma. Invest Ophthalmol Vis Sci. 1996;37:1360-1367.
45. Knepper PA, Goossens W, Palmberg PF. Glycosaminoglycan stratification of the juxtacanalicular tissue in normal and primary open-angle glaucoma. Invest Ophthalmol Vis Sci. 1996;37:2414-2425.
46. Acott TS, Truesdale AT, Samples JR. Van Buskirk EM. Trabecular extracellular matrix synthesis in human explant organ culture [ARVO Abstract]. Invest Ophthalmol Vis Sci. 1986;26:S211.
47. Alexander JP, Samples JR, Van Buskirk EM, Acott TS. Expression of matrix metalloproteinases and inhibitor by human trabecular meshwork. Invest Ophthalmol Vis Sci. 1991;32:172-180.
48. Samples JR, Alexander JP, Acott TS. Regulation of the levels of human trabecular matrix metalloproteinases and inhibitor by interleukin-1 and dexamethasone. Invest Ophthalmol Vis Sci. 1993; 34:3386-3395.
49. Parshley DE, Bradley JMB, Samples JR, Van Buskirk EM, Acott TS. Early changes in matrix metalloproteinases and inhibitors after in vivo laser treatment to the trabecular meshwork. Curr Eye Res. 1995;14:537-544.
50. Parshley DE, Bradley JMB, Fisk A, et al. Laser trabeculoplasty induces stromelysin expression by trabecular juxtacanalicular cells. Invest Ophthalmol Vis Sci. 1996;37:795-804.
51. Wirtz MK, Samples JR, Kramer PL, et al. Mapping a gene for adult-onset primary open-angle glaucoma to chromosome 3q. Am J Hum Genet. 1997;60:296-304.
52. Stone EM, Fingert JH, Alward WLM, et al. Identification of a gene that causes primary open angle glaucoma. Science. 1997;275:668-670.
53. Stoilova D, Child A, Trifan OC, et al. Localization of a locus (GLC1B) for adult-onset primary open angle glaucoma to the 2cenq13 region. Genomics. 1996;36:142-150.
54. Acott TS, Kingsley PD, Samples JR, Van Buskirk EM. Human trabecular meshwork organ culture: morphology and glycosaminoglycan synthesis. Invest Ophthalmol Vis Sci. 1988;29:90-100.
55. Johnson DH, Tschumper RC. The effect of organ culture on human trabecular meshwork. Exp Eye Res. 1989;49:113-127.
56. Johnson DH, Tschumper RC. Human trabecular meshwork organ culture. Invest Ophthalmol Vis Sci. 1987;28:945-953.
57. Johnson DH, Bradley JMB, Acott TS. The effect of dexamethasone on glycosaminoglycans of human trabecular meshwork in perfusion organ culture. Invest Ophthalmol Vis Sci. 1990;31:2568-2571.
58. Johnson DH, Knepper PA. Microscale analysis of the glycosaminoglycans of human trabecular meshwork: a study in perfusion cultured eyes. J Glaucoma. 1994;3:58-69.
59. Tschumper RC, Johnson DH, Bradley JMB, Acott TS. Glycosaminoglycans of human trabecular meshwork in perfusion organ culture. Curr Eye Res 1990;9:363-369.
60. Erickson-Lamy K. The perfused human ocular anterior segment as a model for aqueous outflow physiology. J Glaucoma. 1992;1:44-53.
61. Erickson-Lamy K, Rohen JW, Grant WM. Outflow facility studies in the perfused bovine aqueous outflow pathways. Curr Eye Res. 1988;7:799-807.
62. Clark AF, Wilson K, de Kater AW, Allingham RR, McCartney MD. Dexamethasone-induced ocular hypertension in perfusion-cultured human eyes. Invest Ophthalmol Vis Sci. 1995;36:478-489.
63. Kaufman PL. Aqueous humor dynamics. In: Duane TD, Jaeger EA, eds. Clinical Ophthalmology. Philadelphia: JB Lippincott; 1988;3: 45.41-45.24.
64. Johnson DH. Human trabecular meshwork cell survival is dependent on perfusion rate. Invest Ophthalmol Vis Sci. 1996;37:1204-1208.
65. Alexander JP, Bradley JMB, Gabourel JD, Acott TS. Expression of matrix metalloproteinases and inhibitor by human retinal pigment epithelium. Invest Ophthalmol Vis Sci. 1990;31:2520-2528.
66. Twining SS. Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes. Anal Biochem. 1984;143:30-34.
67. Nagase H, Fields CG, Fields GB. Design and characterization of a fluorogenic substrate selectively hydrolyzed by stromelysin 1 (matrix metalloproteinase-3). J Biol Chem. 1994;269:20952-20957.
68. Cornish-Bowden A. Analysis of Enzyme Kinetic Data. Oxford: Oxford Scientific Publications; 1995.
69. Gonzalez-Avila G, Ginebra M, Hayakawa T, et al. Collagen metabolism in human aqueous humor from primary open-angle glaucoma: decreased degradation and increased biosynthesis play a role in its pathogenesis. Arch Ophthalmol 1995;113:1319-1323.
70. Golub LM, Ramamurthy NS, McNamara TF, Greenwald RA, Rifkin BR. Tetracyclines inhibit connective tissue breakdown: new therapeutic implications for an old family of drugs. Crit Rev Oral Biol Med. 1991;2:297-322.
71. Wallace I, Krupin T, Stone RA, Moolchandani J. The ocular hypotensive effects of demeclocycline, tetracycline and other tetracycline derivatives. Invest Ophthalmol Vis Sci. 1989;30:1594-1598.
72. Qi-Zhuang Y, Johnson LL, Nordan I, Hupe D, Hupe L. A recombinant human stromelysin catalytic domain identifying tryptophan derivatives as human stromelysin inhibitors. J Med Chem. 1994; 37:206-209.
73. Hanglow AC, Lugo A, Walsky R, et al. Peptides based on the conserved predomain sequence of matrix metalloproteinases inhibit human stromelysin and collagenase. Agents Actions. 1993; 39:C148-C150.
74. Hanglow AC, Lugo A, Walsky R, et al. Inhibition of human stromelysin by peptides based on the N-terminal domain of tissue inhibitor of metalloproteinases-1. Biochem Biophys Res Commun. 1994;205:1156-1163.
75. Bradley JMB, Conger DM, Fisk AS, Samples JR, Acott TS. Matrix metalloproteinases increase outflow facility in perfused anterior segment explants [ARVO Abstract]. Invest Ophthalmol Vis Sci. 1995;36(4):S727. Abstract nr 3357.
76. Colvis CM, Bradley JMB, Vranka J, Acott TS. Minocycline inhibits matrix metalloproteinases and perfused anterior segment outflow facility. Invest Ophthalmol Vis Sci. 1995;36(4):S728. Abstract nr 3358.
77. Vranka J, Bradley JMB, Colvis CM, Alexander JP, Acott TS. Matrix metalloproteinase inhibitors decrease perfused anterior segment outflow facility. Invest Ophthalmol Vis Sci. 1995;36(4):S728. Abstract nr 3359.
78. Vranka JA, Acott TS, Gelatinase. A and B inhibition kinetics using inhibitors which cause glaucoma in a model system (Abstract). FASEB J. 1996;10:A1405. Abstract nr 2341.