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Extensive disulfide bonding at the mammalian cell surface.
Summary
Cell surface proteins, especially the large external transformation-sensitive (LETS) protein, are extensively disulfide bonded. Viral transformation disrupts these crucial protein complexes, altering cell surface characteristics.
Area of Science:
- Cell Biology
- Biochemistry
- Proteomics
Background:
- Cell surface proteins play critical roles in cell adhesion and communication.
- Disulfide bonds are essential for protein structure and function, particularly for extracellular proteins.
Purpose of the Study:
- To investigate the extent and nature of disulfide bonding in cell surface proteins.
- To examine alterations in cell surface protein disulfide bonding upon viral transformation.
Main Methods:
- Analysis of disulfide-bonded protein complexes in cultured cells.
- Comparison of protein profiles between normal and virally transformed cells.
Main Results:
- Cell surface proteins exhibit a higher degree of disulfide bonding compared to total cellular proteins.
- The large external transformation-sensitive (LETS) protein is predominantly found in disulfide-bonded homodimers and higher-order aggregates.
- Viral transformation leads to the absence of LETS protein and its disulfide complexes, along with other affected disulfide-bonded proteins.
Conclusions:
- Disulfide bonding is a significant feature of cell surface protein organization.
- LETS protein and its complex formation are sensitive to viral transformation, suggesting a role in altered cellular phenotypes.