What question did this study set out to answer?

To identify and characterize a novel cell-surface protein that selectively associates with specific integrin complexes.

Specific Association Of CD63 with the VLA-3 and VLA-6 Integrins

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In vitro study reveals specific complex formation between CD63 and VLA-3 or VLA-6 integrins, indicating specialized roles in cellular adhesion.

To identify and characterize a novel cell-surface protein that selectively associates with specific integrin complexes.
Screened monoclonal antibodies against cell-surface proteins to isolate mAb 6H1 and coprecipitate associated complexes from cell lysates.
Purified the target 45–60 kDa protein using mAb 6H1 affinity chromatography and analyzed its amino-terminal sequence.
Assessed colocalization with lysosomal markers and cellular footprints, and tested the requirement of the alpha 3 cytoplasmic tail.
Sequencing identified the 45–60 kDa protein as CD63, which selectively coprecipitated with alpha 3 beta 1 and alpha 6 beta 1, but not alpha 2 beta 1 or alpha 5 beta 1.
CD63 colocalized with VLA-3 in cellular footprints and with cathepsin D in lysosomal granules.
The cytoplasmic domain of alpha 3 was neither necessary nor sufficient for association with CD63, indicating interaction occurs elsewhere in the integrin heterodimer.

Berditchevski et al. (1995) studied this question.

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In vitro study reveals specific complex formation between CD63 and VLA-3 or VLA-6 integrins, indicating specialized roles in cellular adhesion.