Abstract
Fibrillin molecules form the structural framework of elastic fibrillin-rich microfibrils of the extracellular matrix. We have investigated the proteolysis of recombinant fibrillin molecules by five matrix metalloproteinases. Cleavage sites were defined at the carboxy-terminal end of the fibrillin-1 proline-rich region and the corresponding fibrillin-2 glycine-rich region (exon 10), and within exon 49 towards the carboxy-terminus of fibrillin-1. Cleavage at these sites is predicted to disrupt the structure and function of the fibrillin-rich microfibrils.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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COS Cells
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Calcium-Binding Proteins / chemistry
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Calcium-Binding Proteins / metabolism
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Cloning, Molecular
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DNA, Complementary
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Extracellular Matrix Proteins / chemistry
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Extracellular Matrix Proteins / metabolism
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Fibrillins
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Metalloendopeptidases / metabolism*
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Microfilament Proteins / chemistry*
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Microfilament Proteins / genetics
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Microfilament Proteins / metabolism*
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Transcription, Genetic
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Transfection
Substances
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Calcium-Binding Proteins
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DNA, Complementary
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Extracellular Matrix Proteins
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Fibrillins
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Microfilament Proteins
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Peptide Fragments
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Recombinant Proteins
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Metalloendopeptidases