Aberrant expression of α-dystroglycan in cervical and vulvar cancer

Dystroglycan expression is reduced during prostate tumorigenesis and is regulated by androgens in prostate cancer cells

“…Thus, it has been hypothesized that loss of DG expression and/ or function might play an important role in tumor development by altering the interactions between cells and the surrounding matrix (Weir and Muschler, 2003;Brennan et al, 2004;Raz, 2004;Sgambato and Brancaccio, 2005). Downregulation and/or alteration of the DG complex has been reported in a variety of human cancer cell lines (Losasso et al, 2000;Muschler et al, 2002;Sgambato et al, 2003) and primary cancers (Losasso et al, 2000;Henry et al, 2001;Muschler et al, 2002;Sgambato et al, 2003Sgambato et al, , 2006bHerzog et al, 2004;Jing et al, 2004;Singh et al, 2004;Calogero et al, 2006). Henry et al (2001) previously reported a reduced expression of DG, which was most pronounced in high-grade diseases, in a limited number of surgically resected prostate cancers (n ¼ 15) compared with benign prostatic epithelium.…”

“…We and others recently demonstrated that DG expression, and mainly a-DG, is reduced or lost in a variety of human cancer cell lines and primary tumors, including prostate cancer (Losasso et al, 2000;Henry et al, 2001;Muschler et al, 2002;Sgambato et al, 2003Sgambato et al, , 2006bHerzog et al, 2004;Jing et al, 2004;Singh et al, 2004;Calogero et al, 2006). A reduction in the expression levels of DG was shown to be most pronounced in high-grade diseases Sgambato et al, 2003) and to have a prognostic significance in breast cancer patients (Sgambato et al, 2003).…”

Expression of dystroglycan correlates with tumor grade and predicts survival in renal cell carcinoma

“…However, evidence has grown for the importance of non-integrin receptors such as dystroglycan (DG), a ubiquitously expressed cell-surface receptor responsible for crucial interactions between ECM and the cytoplasmic compartment, whose expression has been shown to be reduced or lost in a variety of human cancer cell lines and primary tumors. 15,18,19,[21][22][23][24] DG is expressed in podocytes at the base of foot processes and DG-laminin interaction has been shown to be essential for epithelium development in kidney organ culture (Durbeej, 1995 #969). Moreover, it has been demonstrated that the DG complex undergoes changes in human glomerular diseases in which flattening of foot processes is directly associated with dissociation of laminin-DG complexes.…”

“…Immunohistochemical analyses were performed on routinely processed, formalin-fixed, paraffin-embedded tissues employing an avidin-biotin complex immunoperoxidase technique (Vectastain ABC kit, Vector Laboratories, Burlingame, CA), as previously described. 21,24 Briefly, successive 5 mm tissue sections were cut from blocks selected for the presence of representative lesions and mounted on charged and precleaned slides. Sections were dewaxed, rehydrated and then microwave pretreated (10 min at 750W in 1 mM EDTA buffer, PH 8.0), followed by incubation with 0.3% hydrogen peroxide in methanol for 30 min to block endogenous peroxidase.…”

“…7,15,16 We and others recently demonstrated that DG expression, and mainly aDG, is reduced or lost in a variety of human cancer cell lines and primary tumors. 15,[17][18][19][20][21][22][23][24] A reduction in the expression levels of DG was shown to be most pronounced in high-grade diseases 17,21 and to have a prognostic significance in breast cancer patients. 21 We also recently demonstrated that expression of an exogenous DG cDNA inhibits proliferation of both normal and cancer breast epithelial cells and reduces the anchorage-independent growth and tumorigenicity of breast cancer cells, thus confirming an important role of this molecule in the maintenance of the transformed phenotype of these cells.…”