Dystroglycan complex in cancer.
Abnormalities in the interactions between tumour cells, adhesion molecules and extracellular matrix proteins are often implicated in the behaviour of carcinoma cells. The alpha- and beta-dystroglycan (DG) proteins form part of the large dystrophin-associated protein (DAP) complex. They are involved in epithelial cell development, formation of the basement membrane and maintenance of tissue integrity. Specific changes and reduction or loss of DG expression have been reported in human breast, colon, head and neck, and prostate cancers, implicating it in tumour invasion and dissemination. Degradation of beta-DG by matrix metalloproteinase (MMP) enzymes may assist tumour dissemination. We report the present knowledge of the DG interactions in solid tumour biology.
Brennan
P A
PA
Maxillofacial Unit, Department of Head and Neck Surgery, Queen Alexandra Hospital, Portsmouth PO6 3LY, UK. peter.brennan@porthosp.nhs.uk
Jing
J
J
Ethunandan
M
M
Górecki
D
D
D003598:Cytoskeletal Proteins / Q000378:metabolism*; D049030:Dystroglycans; D006801:Humans; D020782:Matrix Metalloproteinases / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism*; D009361:Neoplasm Invasiveness / Q000503:physiopathology; D009362:Neoplasm Metastasis / Q000503:physiopathology; D009369:Neoplasms / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology
D003598:Cytoskeletal Proteins; C483081:DAG1 protein, human; D008562:Membrane Glycoproteins; D049030:Dystroglycans; D020782:Matrix Metalloproteinases