Properties of the extracellular calcium binding module of the proteoglycan testican

The extracellular calcium-binding (EC) module of human testican (115 residues) was obtained in native form by recombinant production in mammalian cell culture and thus shown to represent an independently folding domain. This module showed a large loss in α-helix upon calcium depletion. Apparently on...

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Bibliographic Details
Published in:FEBS letters 1997-09, Vol.414 (3), p.557-561
Main Authors: Kohfeldt, Eddie, Maurer, Patrik, Vannahme, Christian, Timpl, Rupert
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Calcium - metabolism
Calcium binding
EF hand
Enzyme-Linked Immunosorbent Assay
Extracellular matrix
Genetic Vectors - genetics
Humans
Immune Sera
Molecular Sequence Data
Osteonectin - chemistry
Osteonectin - genetics
Osteonectin - metabolism
Plasmids - genetics
Proteoglycans - chemistry
Proteoglycans - genetics
Proteoglycans - metabolism
Rabbits
Recombinant protein
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Sequence Deletion
Sequence Homology, Amino Acid
X-Ray Diffraction
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Summary:The extracellular calcium-binding (EC) module of human testican (115 residues) was obtained in native form by recombinant production in mammalian cell culture and thus shown to represent an independently folding domain. This module showed a large loss in α-helix upon calcium depletion. Apparently only one of the two EF hands binds calcium, with a moderate affinity ( K d=68 μM) about 100-fold lower than in the homologous BM-40 protein. No clear evidence was obtained for collagen binding, indicating that EC modules found in different proteins may not share similar functions.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)01070-3