Publication: The extended ppGalNAc-T family and their
functional involvement in the metastatic cascade
Authors
Beaman, Ellie-May ; Brooks, Susan A.
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Publisher
F. Hernández y Juan F. Madrid. Universidad de Murcia. Departamento de Biología Celular e Histología
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DOI
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info:eu-repo/semantics/article
Description
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.
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Citation
Histology and Histopathology, vol. 29, nº 3 (2014)
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