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Nucleus translocation of APP c‐terminal proteolytic fragment functions as a cryptic oncogenic protein
Author(s) -
Yu weihsuan,
Liao LiWei,
Hsiao JongKai
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.lb76
Subject(s) - autocrine signalling , microbiology and biotechnology , paracrine signalling , amyloid precursor protein , juxtacrine signalling , biology , neurite , chemistry , receptor , biochemistry , alzheimer's disease , medicine , disease , pathology , in vitro
Post‐translational proteolytic processing for several membrane‐anchored precursors of growth factors, neurontrophic factors, and cell surface adhesion molecules has been implicated in modulating neuron cell differentiation, neurite out‐growth, protection from apoptosis and degeneration, synapse formation and tumorigenesis. This abstract is focusing on investigating the roles of matrix etalloprotease‐7(MMP‐7) in neuroblastoma formation. Through the proteolytic processing can release the membrane bound precursor of growth factors, cytokines and neurotrophins from membrane tethering to a mature secreted proteins and altering ligands to their receptors from juxtacrine to paracrine or even autocrine loop. Interestingly, Over expression of Amyloid precursor proteins (APP) in SH‐SY5Y can up‐regulating MMP‐7 expression. MMP‐7 can process APP and generate ~ 12~14 kDa fragments, which can traffic into nucleus and potentially turn MMP‐7 promoter and induce MMP‐7 expression. This tumorigenitic autocrine loop confirms the anchorage‐independent growth of SH‐SY5y and implicating the possible MMP‐7 mediated oncogenic signaling pathway in neuroblastoma formation. ? C011 ? ? ? ?