Gene/Protein
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Enzyme
Compound
Pivot Concepts:
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Target Concepts:
Gene/Protein
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Query: UNIPROT:P17931 (
galectin-3
)
2,860
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Nucling is a novel apoptosis-associated molecule, which is involved with cytochrome c /
Apaf-1
/caspase-9 apoptosome induction following pro-apoptotic stress. In the present study, we show first that Nucling is able to interact with
galectin-3
.
Galectin-3
is known to participate in many biological processes, including apoptotic cell death. Nucling was found to down-regulate the expression level of
galectin-3
mRNA/protein. Nucling-deficient cells, in which
galectin-3
expression is up-regulated, appeared to be resistant to some forms of pro-apoptotic stress as compared with wild-type cells. In addition, the preputial gland from Nucling-deficient mice expressed a significant level of
galectin-3
and exhibited a high incidence of inflammatory lesions, indicating that Nucling plays a crucial role in the homoeostasis of this gland by interacting with the
galectin-3
molecule and regulating the expression level of
galectin-3
. Up-regulation of
galectin-3
was also observed in the heart, kidney, lung, testis and ovary of the Nucling-deficient mice. In order to confirm the functional interaction between Nucling and
galectin-3
, a well-documented candidate for the mediator of
galectin-3
expression, NF-kappaB (nuclear factor kappaB), was investigated as well. Nucling was shown to interfere with NF-kappaB activation via the nuclear translocation process of NF-kappaB/p65, thus inhibiting the expression of
galectin-3
. Taken together, we propose that Nucling mediates apoptosis by interacting and inhibiting expression of
galectin-3
.
...
PMID:Nucling mediates apoptosis by inhibiting expression of galectin-3 through interference with nuclear factor kappaB signalling. 1496 64
Apoptosis is a process of cellular suicide executed by caspases. Impaired activation of caspase-9 may contribute to chemoresistance in cancer. Activation of caspase-9 occurs after binding to
Apaf-1
and formation of the apoptosome in the presence of cytochrome c/(d)ATP. We used a proteomics approach to identify proteins in caspase-9-protein complexes in extracts derived from NSCLC cells with(out) cytochrome c/dATP. Using co-immunoprecipitation, one-dimensional gel electrophoresis and tandem mass spectrometry, 38 proteins were identified of which 24 differential interactors. The differential interactors can be functionally assigned to cytoskeletal (re)organization and cell motility, catalytic activity, and transcriptional processes and apoptosis. The interaction of caspase-9 with
Apaf-1
was confirmed and acetylserotonin-O-methyltransferase-like protein was identified as a candidate substrate of caspase-9. Novel interactors were found including
galectin-3
, swiprosin-1 and the membrane-cytoskeleton linkers Ezrin/Radixin/Moesin. Co-immunoprecipitation and Western blot experiments confirmed the interaction of caspase-9 with several identified binding partners. A large number of cytoskeletal proteins associated with unprocessed caspase-9 may indicate a scaffold function of this structure and/or may act as caspase substrates during apoptosis. Together, our results indicate that proteomic analysis of the caspase-9-associated protein complexes is a powerful exploratory approach to identify novel caspase substrates and/or regulators of caspase-9-dependent apoptosis.
...
PMID:Comparative proteomics analysis of caspase-9-protein complexes in untreated and cytochrome c/dATP stimulated lysates of NSCLC cells. 1911 55
