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Electrostatic cell-to-cell adhesion by a non-proteolytic component in a protease preparation
T Yamamoto1, T Ohno-Shosaku, E Furukawa-Uenoyama
1Department of Physiology, Faculty of Medicine, Kyoto University, Japan.
Cell Structure and Function
|June 1, 1994
Summary
Papaya protease induces reversible cell adhesion via electrostatic interactions. The adhesion molecules are identified as 28 kDa cationic protein dimers, separate from the enzyme itself.
Area of Science:
- Cell biology
- Biochemistry
- Proteomics
Background:
- Cell adhesion is crucial for tissue development and function.
- Understanding the molecular mechanisms of cell-cell interactions is essential.
Purpose of the Study:
- To investigate the role of papaya protease in inducing cell adhesion.
- To characterize the molecules responsible for protease-mediated cell adhesion.
Main Methods:
- Enzyme preparation from papaya (Protease Type III, Sigma).
- Cell adhesion assays with various cell types (lymphoid, epithelial, fibroblastic).
- Analysis of adhesion activity dependence on ionic strength, Ca2+, Mg2+, and pH.
- Ion-exchanger and gel-filtration chromatography for molecular characterization.
Main Results:
- Papaya protease induced reversible cell adhesion at low ionic strength (<100 mM).
- Adhesion was sensitive to ionic strength, Ca2+, Mg2+, and pH, suggesting electrostatic interactions.
- Chromatographic methods indicated the adhesion molecules are 28 kDa cationic protein dimers, distinct from the protease activity.
Conclusions:
- Papaya protease contains molecules that mediate cell adhesion through electrostatic interactions.
- These adhesion molecules are dimers of a 28 kDa cationic protein, separate from the proteolytic activity.