Analysis of cellular proteins in maxilla and oral squamous cell carcinoma by two-dimensional gel electrophoresis.

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The cellular proteins of 12 specimens of maxilla and oral squamous cell carcinoma were analyzed by two dimensional isoelectric focusing-sodium dodecyl sulfate gel electro-phoresis. The number of polypeptide spots detectable in individual gels was about 110 per 200μg of proteins with pIs from 4.5 to 8.5 and MWs from 22, 000 to 72, 000. Many of the polypeptides were common to these lesions. However, there were nine main polypeptides which showed differences between normal tongue mucosa and squamous cell carcinoma. In the carcinoma, two polypeptides (7.0/45 K, 7.2/47 K, pI/MW) were decreased and four polypeptides (4.8/33 K, 6.9/49 K, 7.1/38 K, 7.4/59 K) were increased in an amount but only polypeptide, 7.9/38 K was varied in an amount by differentiation of carcinoma. This polypeptide was increased in moderately and lower differentiation and decreased in well differentiation. The remaining two polypeptides (4.8/38 K, 4.9/37 K) that were not normally present appeared in carcinoma, but these two new polypeptides were not specific to carcinoma because they were also present in dysplastic lesion. These results suggest that two dimensional electrophoresis may be useful in biochemical diagnosis of maxilla and oral squamous cell carcinoma.
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