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B. Davies, J. Waxman, Harpret Wasan, P. Abel, G. Williams, T. Krausz, D. Neal, David Thomas, A. Hanby, F. Balkwill (1993)
Levels of matrix metalloproteases in bladder cancer correlate with tumor grade and invasion.Cancer research, 53 22
Hiroaki Kinoh, Hiroshi Sato, Y. Tsunezuka, T. Takino, A. Kawashima, Y. Okada, M. Seiki (1996)
MT-MMP, the cell surface activator of proMMP-2 (pro-gelatinase A), is expressed with its substrate in mouse tissue during embryogenesis.Journal of cell science, 109 ( Pt 5)
C. Pollitt (1996)
Basement membrane pathology: a feature of acute equine laminitis.Equine veterinary journal, 28 1
D. Kleiner, W. Stetler-Stevenson (1994)
Quantitative zymography: detection of picogram quantities of gelatinases.Analytical biochemistry, 218 2
C. Pollitt (1995)
Color Atlas of the Horse's Foot
L. Cornelius, L. Nehring, J. Roby, W. Parks, H. Welgus (1995)
Human dermal microvascular endothelial cells produce matrix metalloproteinases in response to angiogenic factors and migration.The Journal of investigative dermatology, 105 2
(1994)
Matrilysin expression by human phagocytes
B. Himelstein, R. Cañete‐soler, E. Bernhard, Dilks Dw, R. Muschel (1994)
Metalloproteinases in tumor progression: the contribution of MMP-9.Invasion & metastasis, 14 1-6
Chambers (1985)
Mammalian colagenase predisposes bone surfaces to osteoclastic resorptionCell Tiss. Res., 241
H. Birkedal‐Hansen, W. Moore, M. Bodden, L. Windsor, B. Birkedal‐Hansen, A. Decarlo, J. Engler (1993)
Matrix metalloproteinases: a review.Critical reviews in oral biology and medicine : an official publication of the American Association of Oral Biologists, 4 2
H. Birkedal‐Hansen (1995)
Proteolytic remodeling of extracellular matrix.Current opinion in cell biology, 7 5
E. Morris, B. Treadwell (1994)
Effect of interleukin 1 on articular cartilage from young and aged horses and comparison with metabolism of osteoarthritic cartilage.American journal of veterinary research, 55 1
(1993)
Cell typespecific regulation of SL-1 and SL-2 genes
C. Ries, P. Petrides (1995)
Cytokine regulation of matrix metalloproteinase activity and its regulatory dysfunction in disease.Biological chemistry Hoppe-Seyler, 376 6
R. Goldfarb, L. Liotta (1986)
Proteolytic Enzymes in Cancer Invasion and MetastasisSeminars in Thrombosis and Hemostasis, 12
Maria Jeziorska, H. Nagase, L. Salamonsen, D. Woolley (1996)
Immunolocalization of the matrix metalloproteinases gelatinase B and stromelysin 1 in human endometrium throughout the menstrual cycle.Journal of reproduction and fertility, 107 1
Brown (1993)
Expression of activated gelatinase in human invasive breast carcinomaClin. expt. Metastasis., 11
(1995)
Y-79 cell culture
D. Busiek, V. Baragi, L. Nehring, William Parks, H. Welgus (1995)
Matrilysin expression by human mononuclear phagocytes and its regulation by cytokines and hormones.Journal of immunology, 154 12
L. Windsor, H. Grenett, B. Birkedal‐Hansen, M. Bodden, Jeffrey Engler, H. Birkedal-Hansen, H. Birkedal-Hansen (1993)
Cell type-specific regulation of SL-1 and SL-2 genes. Induction of the SL-2 gene but not the SL-1 gene by human keratinocytes in response to cytokines and phorbolesters.The Journal of biological chemistry, 268 23
L. Matrisian (1992)
The matrix‐degrading metalloproteinasesBioEssays, 14
Davies (1993)
Levels of matrixproteinases in bladder cancer correlate with tumor grade and invasionCancer Res., 53
C. Pollitt (1994)
The basement membrane at the equine hoof dermal epidermal junction.Equine veterinary journal, 26 5
S. Watson, T. Morris, G. Robinson, M. Crimmin, P. Brown, J. Hardcastle (1995)
Inhibition of organ invasion by the matrix metalloproteinase inhibitor batimastat (BB-94) in two human colon carcinoma metastasis models.Cancer research, 55 16
E. Karran, T. Young, R. Markwell, G. Harper (1995)
In vivo model of cartilage degradation--effects of a matrix metalloproteinase inhibitor.Annals of the Rheumatic Diseases, 54
W. Stetler-Stevenson, S. Aznavoorian, L. Liotta (1993)
Tumor cell interactions with the extracellular matrix during invasion and metastasis.Annual review of cell biology, 9
B. Jones, P. Moshyedi, S. Gallo, J. Tombran-Tink, G. Arand, D. Reid, E. Thompson, G. Chader, R. Waldbillig (1994)
Characterization and novel activation of 72-kDa metalloproteinase in retinal interphotoreceptor matrix and Y-79 cell culture medium.Experimental eye research, 59 3
Tuula Salo, J. Lyons, F. Rahemtulla, H. Birkedal-Hansen, Hannu Larjava (1991)
Transforming growth factor-beta 1 up-regulates type IV collagenase expression in cultured human keratinocytes.The Journal of biological chemistry, 266 18
Busiek (1994)
Matrilysin expression by human phagocytes and its regulation by cytokines and hormonesJ. Immunol., 154
H. Crawford, L. Matrisian (1994)
Tumor and stromal expression of matrix metalloproteinases and their role in tumor progression.Invasion & metastasis, 14 1-6
P. Brown, R. Giavazzi (1995)
Matrix metalloproteinase inhibition: a review of anti-tumour activity.Annals of oncology : official journal of the European Society for Medical Oncology, 6 10
Summary A method for culturing explants of lamellar hoof was developed to investigate the process of lamellar separation that occurs in laminitis. Explants, consisting of hoof wall, dermal and epidermal lamellae and the adjacent sub‐lamellar connective tissue remained intact when cultured in tissue culture medium for 2 days. However, when cultured in the presence of the matrix metalloproteinase (MMP) activator aminophenylmercuric acetate (APMA), the lamellae separated when tension was applied by pulling the hoof wall in an opposite direction to the connective tissue. The separation occurred between the epidermal basal cells and the basement membrane therefore mimicking the lesion of laminitis. Electrophoresis of culture medium from control hoof explants into gradient polyacrylamide gels co‐polymerised with gelatin revealed that the explants had produced 2 gelatinases of molecular weight 92 and 72 kDa corresponding to EqMMP‐9 and EqMMP‐2 respectively. Minor bands of lower molecular weight were the active forms of these enzymes. The zymograms of culture medium from APMA treated explants revealed an increase in the amount of active MMPs. Equine polymorphs cultured for 2 days produced only EqMMP‐9. Lamellar explant medium from horses with acute laminitis contained increased amounts of zymogen and active EqMMP‐2 and EqMMP‐9 particularly in explants from the fore hooves. Zymography of homogenates of normal lamellar hoof tissue revealed only EqMMP‐2 and a minor active band. However, homogenates of lamellar tissue from horses with laminitis showed that EqMMP‐9 was present as well as increased EqMMP‐2 in both zymogen and active forms. Addition of the MMP inhibitor batimastat (BB‐94) to the culture medium of APMA treated explants prevented lamellar separation. BB‐94 incubated with polyacrylamide strips containing the MMPs from laminitis affected lamellar explants inhibited enzymatic activity at a concentration of 1 mmol/l. It is concluded that activation of MMPs may be responsible for the lamellar separation seen in laminitis and that MMP inhibitors may be useful clinically for preventing this process.
Equine Veterinary Journal – Wiley
Published: Sep 1, 1998
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