Expression of Members of a Novel Membrane Linked Metalloproteinase Family (ADAM) in Human Articular Chondrocytes

Using resting chondrocytes derived from human articular femoral head and a conditionally immortalised human articular chondrocyte cell line we have studied the expression of members of the novel metalloproteinase/disintegrin family termed ADAM. Using RT-PCR we can detect the expression of ADAM-12 a...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-01, Vol.230 (2), p.335-339
Main Authors: McKie, Norman, Edwards, Tracy, Dallas, Donna J., Houghton, Adam, Stringer, Bradley, Graham, R., Russell, G., Croucher, Peter I.
Format: Article
Language:English
Subjects:
ADAM Proteins
ADAM10 Protein
ADAM12 Protein
Aged
Aged, 80 and over
Alternative Splicing
Amino Acid Sequence
Amyloid Precursor Protein Secretases
Animals
Base Sequence
Brain - enzymology
Cartilage, Articular - cytology
Cartilage, Articular - enzymology
Cattle
Cell Line, Transformed
Cell Membrane - enzymology
Cells, Cultured
DNA Primers
Female
Humans
Membrane Proteins - biosynthesis
Membrane Proteins - chemistry
Metalloendopeptidases - biosynthesis
Metalloendopeptidases - chemistry
Molecular Sequence Data
Polymerase Chain Reaction
Sequence Homology, Amino Acid
Transcription, Genetic
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Summary:Using resting chondrocytes derived from human articular femoral head and a conditionally immortalised human articular chondrocyte cell line we have studied the expression of members of the novel metalloproteinase/disintegrin family termed ADAM. Using RT-PCR we can detect the expression of ADAM-12 a novel family member isolated from myeloma cells [1]. We also find expression of ADAM 10 a functional metalloproteinase/disintegrin first isolated from bovine brain and ADAM-15 a metallodisintegrin isolated from mammary derived epithelial cells. Northern blotting was used to confirm expression. One main transcript is visible for ADAM-12 whereas both ADAM-10 and ADAM-15 have multiple transcripts indicating possible RNA variants potentially derived from alternative splicing or alternative use of polyadenylation sites. Since chondrocytes are proposed as an important source of metalloproteinase enzymes involved in joint pathology the potential relevance of the expression of these molecules to connective tissue disorders is discussed.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.5957