Abstract
We examined the metalloproteinase activity from normal and keratoconus corneal extracts. No differences were detected in the total amount of the metalloproteinase or its physical form of activation. However, there was a significant elevation in enzymatic activity in the keratoconus extracts after chemical modification of inhibitory elements. This suggests either a difference in the enzymatic capabilities of keratoconus corneas or, as suggested previously, a decrease in the amount of TIMP (tissue inhibitor of metalloproteinase) present in the tissue.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Cells, Cultured
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Cornea / enzymology*
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Electrophoresis, Polyacrylamide Gel
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Glycoproteins / metabolism
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Humans
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Immunoenzyme Techniques
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In Situ Hybridization
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Keratoconus / enzymology*
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Matrix Metalloproteinase 2
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Matrix Metalloproteinase Inhibitors
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Metalloendopeptidases / genetics
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Metalloendopeptidases / metabolism*
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Neoplasm Proteins / metabolism
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Phenylmercuric Acetate / analogs & derivatives
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Phenylmercuric Acetate / pharmacology
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RNA, Messenger / metabolism
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Tissue Inhibitor of Metalloproteinase-2
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Tissue Inhibitor of Metalloproteinases
Substances
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Glycoproteins
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Matrix Metalloproteinase Inhibitors
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Neoplasm Proteins
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RNA, Messenger
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Tissue Inhibitor of Metalloproteinases
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Tissue Inhibitor of Metalloproteinase-2
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4-aminophenylmercuriacetate
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Metalloendopeptidases
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Matrix Metalloproteinase 2
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Phenylmercuric Acetate