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Thrombomodulin is preferentially expressed in Balb/c lung microvessels
V A Ford1, C Stringer, S J Kennel
1Oak Ridge Graduate School of Biomedical Sciences, University of Tennessee, Oak Ridge.
The Journal of Biological Chemistry
|March 15, 1992
Summary
The murine glycoprotein P112 is identified as thrombomodulin (TM), an endothelial anticoagulant protein. Lung tissue shows significantly higher TM expression due to increased mRNA production, suggesting its importance in continuous endothelium.
Area of Science:
- Endothelial Biology
- Protein Biochemistry
- Molecular Biology
Background:
- Two rat monoclonal antibodies were developed targeting murine glycoprotein P112.
- P112 is expressed predominantly in lung capillary endothelium.
Purpose of the Study:
- To identify the murine glycoprotein P112.
- To characterize the expression levels and regulation of P112/thrombomodulin in different organs.
Main Methods:
- Amino acid analysis and gel electrophoresis to compare P112 and thrombomodulin (TM).
- Monoclonal antibody cross-reactivity assays.
- Protein C activation cofactor assays.
- cDNA sequencing and Northern blot analysis for gene expression.
Main Results:
- P112 shares high homology with TM and exhibits identical biochemical and immunological properties.
- Purified P112 functions as a cofactor for protein C activation, similar to TM.
- Quantitative assays reveal significantly higher TM (P112) levels in lung compared to kidney and liver.
- Northern blot analysis confirms increased TM mRNA levels in the lung, indicating higher production.
Conclusions:
- Murine glycoprotein P112 is identical to thrombomodulin (TM).
- Lung exhibits the highest expression of TM, driven by increased mRNA production.
- TM expression is likely highest in continuous endothelium.