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Hyaluronate appears to be covalently linked to the cell surface
1Department of Anatomy and Cell Biology, Georgetown University Medical Center, Washington, DC 20007.
Journal of Cellular Physiology
|March 1, 1988
Summary
Cell-surface hyaluronate is covalently linked to hydrophobic plasma membrane proteins. This linkage is stable under various conditions but can be disrupted by proteases, suggesting a direct interaction with membrane proteins.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Hyaluronan (HA) is a major component of the extracellular matrix and cell surface.
- The precise mechanism of HA attachment to the plasma membrane is not fully understood.
Purpose of the Study:
- To investigate the nature of the linkage between cell-surface hyaluronate and the plasma membrane.
- To determine the stability and interactions of cell-surface hyaluronate.
Main Methods:
- Isotopic labeling of hyaluronate with [3H]-acetate in rat fibrosarcoma cells.
- Glutaraldehyde fixation to stabilize cells for manipulation.
- Assay of cell-surface hyaluronate using Streptomyces hyaluronidase digestion.
- Extraction with guanidine HCl, detergents, and varying ionic strengths.
- pH stability assays and protease treatments.
- Triton X-114 phase separation to differentiate soluble and hydrophobic proteins.
Main Results:
- Cell-surface hyaluronate remained stable under various conditions, including high salt concentrations and detergents.
- Hyaluronate was released outside the pH range of 4-11 and upon protease treatment.
- Triton X-114 extraction showed significantly more hyaluronate associated with hydrophobic proteins.
Conclusions:
- Cell-surface hyaluronate is likely covalently linked to a protein component of the plasma membrane.
- The linkage involves a hydrophobic core protein integrated within the plasma membrane.
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