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CD146: biosynthesis and production of a soluble form in human cultured endothelial cells
N Bardin1, V Francès, V Combes
1Laboratoire d'Hématologie et d'Immunologie, U.F.R. de Pharmacie, Marseille, France.
Insights
Researchers studied the biosynthesis of CD146, an endothelial cell antigen. They found CD146 is processed into mature and soluble forms, suggesting soluble CD146 may regulate cell functions.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- CD146 (S-Endo 1-associated antigen) is an endothelial cell surface glycoprotein belonging to the immunoglobulin superfamily.
- It possesses a distinctive V-V-C2-C2-C2 Ig domain structure, crucial for its function.
Purpose of the Study:
- To investigate the biosynthesis and processing of CD146 in cultured human endothelial cells.
- To characterize the mature and soluble forms of CD146.
- To explore the potential functional implications of soluble CD146.
Main Methods:
- Immunoprecipitation was employed to isolate CD146.
- Pulse-chase labeling was utilized to track protein synthesis and processing.
- Analysis of secreted proteins in culture media identified soluble CD146 forms.
Main Results:
- CD146 is synthesized as a 100 kDa precursor.
- The precursor is processed into a 120 kDa mature, cell-associated form.
- A soluble form of CD146, approximately 10 kDa smaller than the cell-associated form, was detected in the culture media.
Conclusions:
- CD146 undergoes post-translational modification and processing within endothelial cells.
- The release of soluble CD146 into the extracellular environment suggests a regulatory role.
- Soluble CD146 may modulate the functions of cell-associated CD146, similar to other immunoglobulin superfamily members.
Abstract:
We previously identified the S-Endo 1-associated antigen (CD146), an endothelial member of the immunoglobulin superfamily with a characteristic V-V-C2-C2-C2 Ig domain structure. In cultured human endothelial cells, we investigated its biosynthesis by immunoprecipitation and pulse-chase labeling. CD146 was synthesized as a 100 kDa precursor form, which was processed into a 120 kDa mature form. In the culture media of endothelial cells, we observed a CD146 soluble form that was about 10 kDa smaller than cell-associated CD146. In parallel with soluble forms of other members of the immunoglobulin superfamily, soluble CD146 could modulate and control the functions of the molecule.