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Crystal matrix protein is related to human prothrombin
A M Stapleton1, R J Simpson, R L Ryall
1Department of Surgery, Flinders Medical Centre, Australia.
Biochemical and Biophysical Research Communications
|September 30, 1993
Summary
Crystal matrix protein (CMP), a kidney stone inhibitor found in calcium oxalate crystals, shows significant N-terminal sequence identity to human prothrombin. This suggests a potential link between CMP and prothrombin in kidney stone formation.
Area of Science:
- Biochemistry
- Nephrology
- Molecular Biology
Background:
- Crystal matrix protein (CMP) is a key component of calcium oxalate (CaOx) crystals in human urine.
- CMP acts as a potent inhibitor of crystal aggregation, suggesting a role in kidney stone disease etiology.
Purpose of the Study:
- To isolate and characterize Crystal matrix protein (CMP) from human calcium oxalate crystals.
- To investigate the relationship between CMP and human prothrombin.
Main Methods:
- Isolation of CMP from CaOx crystals using EDTA dissolution.
- Purification via Sephacryl S-200 column chromatography and reversed-phase HPLC.
- N-terminal amino acid sequencing by Edman degradation and Western blotting using anti-prothrombin antibodies.
Main Results:
- Edman degradation revealed 81.8% sequence identity between CMP's N-terminus and human prothrombin.
- Western blotting confirmed cross-reactivity between CMP and an antibody to human prothrombin.
Conclusions:
- Crystal matrix protein (CMP) shares significant sequence homology with human prothrombin.
- This structural similarity suggests a potential functional or developmental relationship between CMP and prothrombin in the context of kidney stone formation.