Immunolocalization of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human subconjunctival tissues

References

• Clark, R. A. F. and Henson, P. M. (1988) Overview and general considerations of repair. In The Molecular and Cellular Biology of Wound Repair. pp. 3–33. Plenum Press, New York
   Google Scholar
• Clark, R. A. F., Lanigan, J. M., Dellapelle, P., Manseau, E., Dvorak, H. and Colvin, H. (1982) Fibronectin and fibrin provide a provisional matrix for epidermal cell migration during wound re-epithelialization. J. Invest. Dermatol. 79, 264–269.
   PubMed Web of Science ®Google Scholar
• Grinell, F. (1989) Fibronectin and wound healing. J. Cell. Biochem. 26, 107–116.
   Web of Science ®Google Scholar
• Diegelmann, R. F., Rothkopf, L. C. and Cohen, I. K. (1975) Measurement of collagen biosynthesis during wound healing. J. Surg. Res. 19, 239–243.
   PubMed Web of Science ®Google Scholar
• Kurkiunen, M., Vaheri, A., Roberts, P. J. and Stenman, S. (1980) Sequential appearance of fibronectin and collagen in experimental granulation tissue. Lab. Invest. 43, 47–51.
   PubMed Web of Science ®Google Scholar
• Colier, I. E., Wilhelm, S. M., Eisen, A. Z., Marmer, B. L., Grant, G. A., Seltzer, J. L., Kronberger, A., He, C., Bauer, A. E. and Goldberg, G. I. (1988) H-ras oncogene-trans-formed human bronchial epithelial cells (TBE-1) secrete a single metalloproteinase capable of degrading basement membrane collagen. J. Biol. Chem. 263, 6579–6587.
   PubMed Web of Science ®Google Scholar
• Wilhelm, S. M., Colier, I. E., Marnier, B. L., Eisen, A. Z., Grant, G. A. and Goldberg, G. I. (1989) Sv-40-transformed human lung fibroblasts secrete 92-kD type IV collagenase which is indentical to that secreted by normal human macrophages. J. Biol. Chem. 264, 17213–17221.
   PubMed Web of Science ®Google Scholar
• Birkedal-Hansen, H., Moore, W. G. I., Bodden, M. K., Windsor, L. J., Birkedal-Hansen, B., DeCarlo, A. and Engler, J. A. (1993) Matrix metalloproteinases, a review. Crit. Rev., Oral Biol. Med. 4, 197–250.
   Google Scholar
• Howard, E. W., Bullen, E. C. and Banda, M. J. (1991) Human alveolar macrophages produce a fibroblast-like collagenase and collagenase inhibitor. J. Biol. Chem. 266, 13070–13075.
   PubMed Web of Science ®Google Scholar
• Striklin, G. P. (1986) Human fibroblast tissue inhibitor of metalloproteinases: glycosylation and function. J. Biol. Chem. 260, 3079–3083.
   Google Scholar
• Murphy, G., Reynolds, J. and Werb, Z. (1985) Biosynthesis of tissue inhibitor of metalloproteinases by human fibroblasts in culture. J. Biol. Chem. 260, 3079–3083.
   PubMed Web of Science ®Google Scholar
• Bertaux, B., Hornebeck, W., Eisen, A. Z. and Dubertret, L. (1991) Growth stimulation of human keratinocytes by tissue inhibitor of metalloproteinases. J. Investig. Dermatol. 97, 679–685.
   PubMed Web of Science ®Google Scholar
• Saika, S., Ooshima, A., Tonoe, O., Okada, Y., Ohnishi, Y., Kimura, M. and Yamanaka, O. (1996) Immunolocalization of prolyl 4-hydroxylase in fibroblasts cultured from Tenon's capsule of humans. Graefe's Arch. Clin. Exp. Ophthalmol. 234, 251–257.
   PubMed Web of Science ®Google Scholar
• Birk, D. E., Fitch, J. M. and Linsenmayer, T. F. (1986) Organization of collagen types I and V in the embryonic chicken cornea. Invest. Ophthalmol. Vis. Sci. 27, 1470–1477.
   PubMed Web of Science ®Google Scholar
• Brik, D. E., Fitch, J. M., Babiarz, J. P. and Linsenmayer, T. F. (1988) Collagen type I and type V are present in the same fibril in the avian corneal stroma. J. Cell. Biol. 106, 999–1008.
   PubMed Web of Science ®Google Scholar
• Linsenmayer, T. F., Fitch, J. M. and Mayne, R. (1984) Extracellular matrices in the developing avian eye: type V collagen in corneal and noncorneal tissue. Invest. Ophthalmol. Vis. Sci. 25, 41–47.
   PubMed Web of Science ®Google Scholar
• Linsenmayer, T. F., Gibney, E., Igoe, F., Gordon, M. K., Fitch, J. M., Fessler, L. I. and Birk, D. E. (1993) Type V collagen: molecular structure and fibrillar organization of chicken a1(V)NH2-terminal domain, a putative regulator of corneal fibrillogenesis. J. Cell. Biol. 121, 1181–1189.
   PubMed Web of Science ®Google Scholar
• Tonoe, O., Yamanaka, O., Okada, Y., Kobata, S. and Saika, S. (1995) Collagen biosynthesis and cellular proliferation after filtering surgery in rabbits. Folia Ophthalmol. Jpn. 46, 242–245.
   Google Scholar
• McLean, I. W. and Nakane, P. K. (1974) Periodate-lysine-paraformaldehyde fixative: a new fixative for immunoelectron microscopy. J. Histochem. Cytochem. 22, 1077–1083.
   PubMed Web of Science ®Google Scholar
• Costa, V. P., Spaeth, G. L., Eiferman, R. A. and Orengo-Nania, S. (1993) Wound healing modulation in glaucoma filtration surgery. Ophthalmic Surg. 24, 152–170.
   PubMedGoogle Scholar
• Vartiot, Laitinen, L., NarvanenO., Cutolo, M., Thornell L.-E., Zardi L. and Virtanen M. (1987) Differential expression of the ED sequence-containing form of cellular fibronectin in embryonic and adult human tissue. J. Cell Sci. 88, 419–439.
   PubMed Web of Science ®Google Scholar
• Wossener, J. F. (1985) Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5, 2145–2154.
   Web of Science ®Google Scholar
• Edwards, D. R., Murphy, G., Reynolds, J. J., Whitham, S. E., Docherty, A. J. P., Angel, P. and Heath, J. K. (1987) Transforming growth factor beta modulates the expression of collagenase and metalloproteinase inhibitor. EMBO J. 6, 1899–1904.
   PubMed Web of Science ®Google Scholar
• Edwards, D. R., Waterhouse, P., Holman, M. L. and Denhardt, D. T. (1986) A growth-responsive gene (16C8) in normal mouse fibroblasts homologous to human collagenase inhibitor with erythroid-potentiating activity. Nucleic Acids Res. 14, 8863–8878.
   PubMed Web of Science ®Google Scholar
• Hayakawa, T., Yamashita, K., Tanzawa, K., Uchijima, E. and Iwata, K. (1992) Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells: a possible new growth factor in serum. FEBS Lett. 298, 29–32.
   PubMed Web of Science ®Google Scholar
• Welgus, H. G., Jeffrey, J. J., Eisen, A. Z., Roswit, W. T. and Stericklin, G. P. (1985) Human skin fibroblast collagenase: interaction with collagen and collagenase inhibitor. Collagen Relat. Res. 5, 167–170.
   PubMedGoogle Scholar
• Vance, B. A., Kowalski, C. G. and Brinckerhoff, C. E. (1989) Heat shock of rabbit synovial fibroblasts increases expression of mRNAs for two metalloproteinases, collagenase and stromelysin. J. Cell. Biol. 108, 2037–2043.
   PubMed Web of Science ®Google Scholar
• Saika, S., Kawashima, Y., Okada, Y., Tanaka, S., Yamanaka, O., Ohnishi, Y. and Ooshima, A. (1998) Recombinant TIMP-1 and −2 enhances the proliferation of rabbit corneal epithelial cells in vitro and the spreading of rabbit corneal epithelium in situ. Curr. Eye Res. 17, 47–52.
   PubMed Web of Science ®Google Scholar
• Desjardins, D. C., Parrish, R. K., II, Folberg, R., Nevarez, J., Heuer, D. K. and Gressel, M. G. (1986) Wound healing after filtering surgery in owl monkeys. Arch. Ophthalmol. 104, 1835–1839.
   PubMedGoogle Scholar
• Rockwood, E. J., Parrish, R. K., Heuner, D. K., Sukuta, G. L., Hodapp, E., Palmberg, P. F., Gressel, M. G. and Feuer, W. (1987) Glaucoma filtering surgery with 5-fluorouracil.; Ophthalmology, 94, 1071–1078.
   PubMed Web of Science ®Google Scholar
• Kitazawa, Y., Suemori-Matsusita, H., Yamamoto, T. and Kawase, K. (1993) Low-dose and high-dose mitomycin trabeculectomy as an initial surgery in primary open-angle glaucoma. Ophthalmology, 100, 1624–1628.
   PubMed Web of Science ®Google Scholar