Cloning of a novel membrane-linked metalloproteinase from human myeloma cells.
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.
McKie
N
N
Department of Human Metabolism and Clinical Biochemistry, University of Sheffield Medical School, U.K.
Dallas
D J
DJ
Edwards
T
T
Apperley
J F
JF
Russell
R G
RG
Croucher
P I
PI
D000595:Amino Acid Sequence; D001483:Base Sequence; D015152:Blotting, Northern; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology; D003001:Cloning, Molecular; D017931:DNA Primers; D019483:Disintegrins / Q000737:chemistry; D005260:Female; D015723:Gene Library; D006801:Humans; D008666:Metalloendopeptidases / Q000096:biosynthesis* / Q000737:chemistry; D008969:Molecular Sequence Data; D009101:Multiple Myeloma; D010920:Placenta / Q000201:enzymology; D016133:Polymerase Chain Reaction; D011247:Pregnancy; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D014407:Tumor Cells, Cultured
D017931:DNA Primers; D019483:Disintegrins; D011994:Recombinant Proteins; D008666:Metalloendopeptidases