+ |
S100A9 | up-regulates quantity by stabilization
binding
|
Tubulin |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261936 |
|
|
Homo sapiens |
Monocyte |
pmid |
sentence |
16690079 |
Calcium-induced complexes of S100A8 and S100A9 have been shown to colocalize with microtubules (MTs) during activation of monocytes. Functional analyses demonstrated that the complexes are involved in cytoskeletal organization and that they directly bind to tubulin and promote tubulin polymerization in a calcium-dependent manner |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
S100A9 | down-regulates
|
Macrophage_differentiation |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261933 |
|
|
Mus musculus |
|
pmid |
sentence |
18809714 |
We report here that up-regulation of S100A9 in myeloid precursors in cancer inhibits DC and macrophage differentiation and induces accumulation of MDSCs. This may represent a universal molecular mechanism of tumor-induced abnormalities in myeloid cells in cancer, directly linking inflammation and immune suppression. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
CEBPB | up-regulates quantity by expression
transcriptional regulation
|
S100A9 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254044 |
|
|
Homo sapiens |
THP-1 Cell |
pmid |
sentence |
9706399 |
Among several known transcription factor binding motifs, nuclear protein(s) of VD3-treated HL-60 cells and THP-1 cells bound to the CCAAT/enhancer binding protein (C/EBP)-binding motif that was located in the upstream region of the MRP14 gene (-81), as evidenced by the competitive gel mobility-shift assay.|Thus, it was concluded that C/EBP alpha and -beta were able to bind to the C/EBP motif, and that C/EBP alpha bound to the motif in THP-1 cells and C/EBP beta bound to that in the VD3-treated HL-60 cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | FLT3-ITD signaling |
+ |
S100A9 | down-regulates
|
Differentiation |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261932 |
|
|
Mus musculus |
Myeloid Progenitor Cell |
pmid |
sentence |
18809714 |
We report here that up-regulation of S100A9 in myeloid precursors in cancer inhibits DC and macrophage differentiation and induces accumulation of MDSCs. This may represent a universal molecular mechanism of tumor-induced abnormalities in myeloid cells in cancer, directly linking inflammation and immune suppression. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
S100A9 | up-regulates activity
binding
|
TLR4 |
0.527 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261918 |
|
|
Homo sapiens |
|
pmid |
sentence |
28137827 |
RAGE and TLR4 are well-characterized S100A8 and S100A9 receptors and expressed in AML cells. S100A9 binds to TLR4 and induces signaling pathways,promoting leukemic cell differentiation and proliferation arrest. Binding of S100A9 to TLR4 stimulates the phosphorylation of JNK, ERK1/2, and p38 MAPK, which leads to the activation of c-Jun, CREB, and NF-kB. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | FLT3-ITD signaling |
+ |
S100A9 | up-regulates
|
Differentiation |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261922 |
|
|
Homo sapiens |
Acute Myeloid Leukemia Cell |
pmid |
sentence |
28137827 |
S100A9 induces differentiation of acute myeloid leukemia cells through TLR4. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
S100A9 | form complex
binding
|
Calprotectin complex |
0.717 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262828 |
|
|
|
|
pmid |
sentence |
9867828 |
Using the two-hybrid system we analyzed the dimerization of MRP8 (S100A8) and MRP14 (S100A9), two S100 proteins expressed in myeloid cells. It is reported that the MRP8-MRP14 heteromer is the clearly preferred complex in both man and mouse. |
|
Publications: |
1 |
+ |
calcium(2+) | up-regulates activity
chemical activation
|
S100A9 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261934 |
|
|
Homo sapiens |
Phagocyte |
pmid |
sentence |
16690079 |
S100 proteins comprise the largest family of calcium-binding proteins. Members of this family usually form homo- or heterodimers, which may associate to higher-order oligomers in a calcium-dependent manner. The heterodimers of S100A8 and S100A9 represent the major calcium-binding proteins in phagocytes. Both proteins regulate migration of these cells via modulation of tubulin polymerization. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CEBPA | up-regulates quantity by expression
transcriptional regulation
|
S100A9 |
0.228 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254041 |
|
|
Homo sapiens |
THP-1 Cell |
pmid |
sentence |
9706399 |
Among several known transcription factor binding motifs, nuclear protein(s) of VD3-treated HL-60 cells and THP-1 cells bound to the CCAAT/enhancer binding protein (C/EBP)-binding motif that was located in the upstream region of the MRP14 gene (-81), as evidenced by the competitive gel mobility-shift assay.|Thus, it was concluded that C/EBP alpha and -beta were able to bind to the C/EBP motif, and that C/EBP alpha bound to the motif in THP-1 cells and C/EBP beta bound to that in the VD3-treated HL-60 cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
S100A9 | up-regulates activity
binding
|
AGER |
0.354 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261920 |
|
|
Homo sapiens |
Acute Myeloid Leukemia Cell |
pmid |
sentence |
28137827 |
RAGE and TLR4 are well-characterized S100A8 and S100A9 receptors and expressed in AML cells Once secreted, S100A8 and S100A9 induce immune and inflammatory responses9 through interaction with receptors such as Toll-like receptor 4 (TLR4), receptor for advanced glycation end-product (RAGE), and CD33 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
STAT3 | up-regulates quantity by expression
transcriptional regulation
|
S100A9 |
0.381 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261931 |
|
|
Mus musculus |
|
pmid |
sentence |
18809714 |
Accumulation of myeloid-derived suppressor cells (MDSCs) associated with inhibition of dendritic cell (DC) differentiation is one of the major immunological abnormalities in cancer and leads to suppression of antitumor immune responses. The molecular mechanism of this phenomenon remains unclear. We report here that STAT3-inducible up-regulation of the myeloid-related protein S100A9 enhances MDSC production in cancer. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | FLT3-ITD signaling |