Kee, Wai Jing; (1999) Expression and function of the beta1B integrin subunit in human keratinocytes. Doctoral thesis (Ph.D), UCL (University College London).

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Abstract

The epidermis is the stratified epithelium that forms the outer covering of the skin. Keratinocytes within the basal layer of the epidermis undergo terminal differentiation and move out of the basal layer, towards the surface of the skin. The integrins are a family of cell surface adhesive receptors and their expression is confined to the basal layer of keratinocytes. Experiments with cultured human epidermal keratinocytes have shown that members of the β1 integrin family have important functions in the epidermis. Keratinocytes express two forms of the β1 integrin subunit, β1A, and a splice variant, β1B. I have shown that within the cytoplasmic domain of the β1B integrin subunit there is an ER retention/retrieval motif. When expressed as a CDS chimera in HeLa cells, the transport of CD8β1B to the cell surface was delayed when compared to that of CD8β1A. Using antibodies specific to the β1B integrin subunit which I generated, I have shown that only low levels of expression are detected in cultured keratinocytes and in the epidermis. Antibodies specific to the β1B integrin subunit immunoprecipitated 2 bands of 110 kD and 120 kD but there was no evidence that either band was one of the β integrin subunits known to form heterodimers with the pi β integrin subunit. There was no increased synthesis of the β1B integrin subunit or association with a integrin subunits at the time of commitment in keratinocytes induced to undergo terminal differentiation, although the half-life of the β1B integrin subunit was increased. I have also examined the expression of the β1B integrin subunit in a small sample of oral squamous cell carcinomas and have found elevated but patchy expression in moderately- and poorly-differentiated tumours.

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