Publication: Ectopeptidases in tumour biology: A review
Authors
Carl-McGrath, S. ; Lendeckel, U. ; Ebert, M. ; Röcken, C.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Cell membrane-bound proteolytic enzymes
(ectopeptidases) are integral membrane proteins,
orientated asymmetrically with the catalytic site exposed
to the extracellular surface, which enables a versatile
range of physiological and pathological functions.
Ectopeptidases may regulate the release of many growth
factors and their receptors into the circulation, as well as
activating or inactivating circulating signalling
molecules, thereby regulating the availability of ligands
for the corresponding receptors. Additionally, many of
these ectopeptidases have functions not limited to
proteolysis, but are able in themselves to function as
receptors, transducing intracellular signals. A versatile
range of functions, such as the modulation of cellsignalling,
matrix degradation, cell adhesion and
migration, which are particularly important for tumour
cell growth and dissemination, are attributed largely to
the ectopeptidases. Even a minor disruption in the
normal proteolytic equilibrium can influence tumor
progression, and a range of ectopeptidases, including
neutral endopeptidase 24.11, aminopeptidase N,
dipeptidyl peptidase IV, angiotensin-converting enzyme,
and the disintegrin-metalloproteinases, have been shown
to be involved in tumour development and metastasis.
The ability to degrade and inactivate peptide hormones and growth factors, with the resultant modulation of the
tumour-host interface, may play an important role in the
pathogenesis, development or progression of a range of
cancers, and the extracellular orientation of the
ectopeptidases makes them particularly accessible, and
therefore interesting, with regard to therapeutical
applications.
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