Abstract
We have isolated a novel cDNA from human myeloma cells encoding a member of the reprolysin family of metalloproteinases. Derived amino acid sequence predicts a protein of approx. 76 kDa. The open reading frame predicts the presence of a leader peptide, a pro-peptide with a 'cysteine switch', a metalloproteinase domain, a disintegrin-like domain, a cysteine-rich domain, an epidermal growth factor-like domain and a putative transmembrane sequence. Expression of the mRNA for this metalloproteinase has been demonstrated in human myeloma cells.
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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Base Sequence
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Blotting, Northern
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Cell Line
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Cell Membrane / enzymology
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Cloning, Molecular
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DNA Primers
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Disintegrins / chemistry
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Female
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Gene Library
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Humans
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Metalloendopeptidases / biosynthesis*
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Metalloendopeptidases / chemistry
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Molecular Sequence Data
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Multiple Myeloma
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Placenta / enzymology
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Polymerase Chain Reaction
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Pregnancy
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Sequence Homology, Amino Acid
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Tumor Cells, Cultured
Substances
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DNA Primers
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Disintegrins
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Recombinant Proteins
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Metalloendopeptidases