Please use this identifier to cite or link to this item: http://hdl.handle.net/10201/67060

Title: The extended ppGalNAc-T family and their functional involvement in the metastatic cascade
Issue Date: 2014
Publisher: F. Hernández y Juan F. Madrid. Universidad de Murcia. Departamento de Biología Celular e Histología
Citation: Histology and Histopathology, vol. 29, nº 3 (2014)
ISSN: 1699-5848
0213-3911
Related subjects: CDU::5 - Ciencias puras y naturales::57 - Biología::576 - Biología celular y subcelular. Citología
Keywords: Metastasis
Cancer
Abstract: O-linked glycosylation of proteins begins with the attachment of a single N-acetylgalactosamine (GalNAc) residue to a serine or threonine residue of the polypeptide and glycosylation of proteins can dramatically change their properties, interactions and activities. This initial attachment is catalysed by members of a family of 20 isoenzymes, the UDP-N-α- D-galactosamine: polypeptide N-acetylgalactosaminyltransferases or ppGalNAc-Ts. Why such a large family of isoenzymes are required to perform, apparently, a single function has been the subject of intense interest. The ppGalNAc-Ts, in fact, have overlapping, but distinct, substrate specificities and are differentially expressed in different cells and tissues and under different conditions of differentiation and development, allowing subtle and complex control of cellular glycosylation. Intriguingly, there is a growing body of evidence showing that altered expression of members of this transferase family are a common feature of many types of cancer and, crucially, that the resulting aberrant glycosylation has functional effects. Here, we review what is known of the expression and distribution of these intriguing transferases in health and in malignancy and, for the first time, bring together what is known of the functional and molecular effects of their disregulation in each step of the complex cascade of cancer metastasis.
Primary author: Beaman, Ellie-May
Brooks, Susan A.
URI: http://hdl.handle.net/10201/67060
Document type: info:eu-repo/semantics/article
Number of pages / Extensions: 12
Rights: info:eu-repo/semantics/openAccess
Appears in Collections:Vol.29, nº 3 (2014)

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