Calcium-dependent interaction between the epidermal growth factor precursor-like region of human protein C and a monoclonal antibody

Protein C, like the other vitamin K-dependent plasma proteins that participate in blood coagulation, except prothrombin, has at least one high affinity calcium-binding site that is independent of gamma-carboxyglutamic acid. Calcium binding to this site is required for activation of protein C by the...

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Bibliographic Details
Published in:The Journal of biological chemistry 1987-10, Vol.262 (28), p.13798-13804
Main Authors: Ohlin, A K, Stenflo, J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Antibodies, Monoclonal
Biological and medical sciences
Blood coagulation. Blood cells
calcium
Calcium - metabolism
Coagulation factors
epidermal growth factor
Epidermal Growth Factor - immunology
Epidermal Growth Factor - metabolism
Epitopes - immunology
Fundamental and applied biological sciences. Psychology
Humans
Molecular and cellular biology
Molecular Weight
Peptide Fragments - analysis
protein C
Protein C - immunology
Protein C - metabolism
Protein Conformation
Protein Precursors - immunology
Protein Precursors - metabolism
Trypsin - metabolism
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Summary:Protein C, like the other vitamin K-dependent plasma proteins that participate in blood coagulation, except prothrombin, has at least one high affinity calcium-binding site that is independent of gamma-carboxyglutamic acid. Calcium binding to this site is required for activation of protein C by the thrombin-thrombomodulin complex. In an attempt to localize this calcium-binding site, we subjected protein C to limited tryptic digestion. A monoclonal antibody that recognizes a calcium-dependent epitope both in intact protein C, in gamma-carboxyglutamic acid-domainless protein C, and in activated protein C, was used to isolate a fragment from the tryptic digest. The fragment was derived from the light chain of protein C and consisted of the two domains that are homologous to the epidermal growth factor precursor. Half-maximal binding of the intact protein and of the isolated fragment by the antibody occurred at 100-200 microM Ca2+. The results suggest the presence of a Ca2+-binding site in the epidermal growth factor homology region of protein C.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)76496-5