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(American Journal of Pathology. 2001;158:1129-1135.)
© 2001 American Society for Investigative Pathology

Regular Articles

Investigation into the Mechanism of the Loss of Laminin 5 (3ß32) Expression in Prostate Cancer

Junshan Hao^*, Lorren Jackson^*, Robert Calaluce^*, Kathy McDaniel^*, Bruce L. Dalkin and Ray B. Nagle^*

From the Departments of Pathology^*
and Surgery
and the Arizona Cancer Center,
University of Arizona, Tucson, Arizona

Laminin 5 is a pivotal hemidesmosomal protein involved in cell stability, migration, and anchoring filament formation. Protein and gene expression of the 3, ß3, and 2 chains of laminin 5 were investigated in normal and invasive prostate carcinoma using immunohistochemistry, Northern analysis, and in situ hybridization. Laser capture microdissection of normal and carcinomatous glands, in conjunction with RNA amplification and reverse Northern analysis, were used to confirm the gene expression data. Protein and mRNA expression of all three laminin 5 chains were detected in the basal cells of normal glands. In contrast, invasive prostate carcinoma showed a loss of ß3 and 2 protein expression with variable expression of 3 chains. Despite the loss of protein expression, there was retention of ß3 and 2 mRNA expression as detected by in situ hybridization, Northern and reverse Northern analysis. Our findings imply that an altered mechanism of translation of ß3 or 2 mRNAs into functional proteins contributes to failure of anchoring filaments and hemidesmosomal formation. The resultant hemidesmosome instability or loss would suggest a less stable epithelial-stromal junction, increased invasion and migration of malignant cells, and disruption of normal integrin signaling pathways.

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