Ignet

Gene Information

Gene symbol: OSM

Gene name: oncostatin M

HGNC ID: 8506

Synonyms: MGC20461

Related Genes

#	Gene Symbol	Number of hits
1	AKT1	1 hits
2	CSF3	1 hits
3	FGF1	1 hits
4	GCK	1 hits
5	HGF	1 hits
6	IL12A	1 hits
7	IL15	1 hits
8	IL6	1 hits
9	INS	1 hits
10	LEP	1 hits
11	LIF	1 hits
12	OSMR	1 hits
13	PRL	1 hits
14	PTGS2	1 hits
15	SOCS3	1 hits

Related Sentences

#	PMID	Sentence
1	12065229	Differential effects of interleukin-6 receptor activation on intracellular signaling and bone resorption by isolated rat osteoclasts.
2	12065229	The effects of the related cytokines interleukin-6 (IL-6), leukemia inhibitory factor (LIF) and oncostatin-M on bone resorption and cytosolic Ca(2+) signaling were compared in isolated rat osteoclasts.
3	12065229	In the traditional disaggregated osteoclast (pit) assay, IL-6 and LIF, but not oncostatin-M, conserved the bone resorption otherwise inhibited by high extracellular [Ca(2+)] (15 mM).
4	12065229	In contrast, the IL-6 receptor (IL-6R)-specific agonist antibody MT-18 inhibited bone resorption in a concentration-dependent manner (1:500 to 1:500 000).
5	12065229	The inclusion of either IL-6 or soluble human (sh) IL-6R specifically reversed both the above effects of MT-18, confirming that both effects were specific for the IL-6R.
6	12065229	The findings suggest that IL-6R activation by IL-6 stimulates osteoclastic bone resorption either by reversing the inhibitory effect of high extracellular Ca(2+) in stromal-containing systems or itself stimulating bone resorption along with Ca(2+) by micro-isolated osteoclasts.
7	12065229	Differential effects of interleukin-6 receptor activation on intracellular signaling and bone resorption by isolated rat osteoclasts.
8	12065229	The effects of the related cytokines interleukin-6 (IL-6), leukemia inhibitory factor (LIF) and oncostatin-M on bone resorption and cytosolic Ca(2+) signaling were compared in isolated rat osteoclasts.
9	12065229	In the traditional disaggregated osteoclast (pit) assay, IL-6 and LIF, but not oncostatin-M, conserved the bone resorption otherwise inhibited by high extracellular [Ca(2+)] (15 mM).
10	12065229	In contrast, the IL-6 receptor (IL-6R)-specific agonist antibody MT-18 inhibited bone resorption in a concentration-dependent manner (1:500 to 1:500 000).
11	12065229	The inclusion of either IL-6 or soluble human (sh) IL-6R specifically reversed both the above effects of MT-18, confirming that both effects were specific for the IL-6R.
12	12065229	The findings suggest that IL-6R activation by IL-6 stimulates osteoclastic bone resorption either by reversing the inhibitory effect of high extracellular Ca(2+) in stromal-containing systems or itself stimulating bone resorption along with Ca(2+) by micro-isolated osteoclasts.
13	15642335	Leptin can be considered as a pro-inflammatory cytokine that belongs to the family of long-chain helical cytokines and has structural similarity with interleukin-6, prolactin, growth hormone, IL-12, IL-15, granulocyte colony-stimulating factor and oncostatin M.
14	16410783	OSM and its specific OSM receptor subunit beta (OSMRbeta) were induced upon injury.
15	16410783	OSM protein was localized in PMN in very early wounds, whereas OSMRbeta could be detected on macrophages, keratinocytes, and fibroblasts later in repair.
16	16410783	PMN-depleted wounds were characterized by a nearly complete loss of OSM but not OSMRbeta mRNA and protein expression within the initial 16-24 hours after injury.
17	16410783	Moreover, a leptin-mediated improvement of chronic wounds in ob/ob mice was paralleled by a complete inhibition of PMN influx associated again with a dramatic loss of OSM expression at the wound site.
18	16410783	OSM and its specific OSM receptor subunit beta (OSMRbeta) were induced upon injury.
19	16410783	OSM protein was localized in PMN in very early wounds, whereas OSMRbeta could be detected on macrophages, keratinocytes, and fibroblasts later in repair.
20	16410783	PMN-depleted wounds were characterized by a nearly complete loss of OSM but not OSMRbeta mRNA and protein expression within the initial 16-24 hours after injury.
21	16410783	Moreover, a leptin-mediated improvement of chronic wounds in ob/ob mice was paralleled by a complete inhibition of PMN influx associated again with a dramatic loss of OSM expression at the wound site.
22	16410783	OSM and its specific OSM receptor subunit beta (OSMRbeta) were induced upon injury.
23	16410783	OSM protein was localized in PMN in very early wounds, whereas OSMRbeta could be detected on macrophages, keratinocytes, and fibroblasts later in repair.
24	16410783	PMN-depleted wounds were characterized by a nearly complete loss of OSM but not OSMRbeta mRNA and protein expression within the initial 16-24 hours after injury.
25	16410783	Moreover, a leptin-mediated improvement of chronic wounds in ob/ob mice was paralleled by a complete inhibition of PMN influx associated again with a dramatic loss of OSM expression at the wound site.
26	16410783	OSM and its specific OSM receptor subunit beta (OSMRbeta) were induced upon injury.
27	16410783	OSM protein was localized in PMN in very early wounds, whereas OSMRbeta could be detected on macrophages, keratinocytes, and fibroblasts later in repair.
28	16410783	PMN-depleted wounds were characterized by a nearly complete loss of OSM but not OSMRbeta mRNA and protein expression within the initial 16-24 hours after injury.
29	16410783	Moreover, a leptin-mediated improvement of chronic wounds in ob/ob mice was paralleled by a complete inhibition of PMN influx associated again with a dramatic loss of OSM expression at the wound site.
30	21255810	After embryoid body (EB) formation from mESC, the EBs were cultured in the presence of dexamethasone (DEX) and insulin for 4 days then was added acidic fibroblast growth factor (aFGF), hepatocyte growth factor (HGF) and oncostatin M (OSM) for 10 days, respectively.
31	21519329	Oncostatin M produced in Kupffer cells in response to PGE2: possible contributor to hepatic insulin resistance and steatosis.
32	21519329	In a recent study, PGE(2) produced in Kupffer cells attenuated insulin-dependent glucose utilization by interrupting the intracellular signal chain downstream of the insulin receptor in hepatocytes.
33	21519329	OSM in turn attenuated insulin-dependent Akt activation and, as a downstream target, glucokinase induction in hepatocytes, most likely by inducing suppressor of cytokine signaling 3 (SOCS3).
34	21519329	COX-2 and OSM mRNA were induced early in the course of the development of non-alcoholic steatohepatitis (NASH) in mice.
35	21519329	Thus, induction of OSM production in Kupffer cells by an autocrine PGE(2)-dependent feed-forward loop may be an additional, thus far unrecognized, mechanism contributing to hepatic insulin resistance and the development of NASH.
36	21519329	Oncostatin M produced in Kupffer cells in response to PGE2: possible contributor to hepatic insulin resistance and steatosis.
37	21519329	In a recent study, PGE(2) produced in Kupffer cells attenuated insulin-dependent glucose utilization by interrupting the intracellular signal chain downstream of the insulin receptor in hepatocytes.
38	21519329	OSM in turn attenuated insulin-dependent Akt activation and, as a downstream target, glucokinase induction in hepatocytes, most likely by inducing suppressor of cytokine signaling 3 (SOCS3).
39	21519329	COX-2 and OSM mRNA were induced early in the course of the development of non-alcoholic steatohepatitis (NASH) in mice.
40	21519329	Thus, induction of OSM production in Kupffer cells by an autocrine PGE(2)-dependent feed-forward loop may be an additional, thus far unrecognized, mechanism contributing to hepatic insulin resistance and the development of NASH.
41	21519329	Oncostatin M produced in Kupffer cells in response to PGE2: possible contributor to hepatic insulin resistance and steatosis.
42	21519329	In a recent study, PGE(2) produced in Kupffer cells attenuated insulin-dependent glucose utilization by interrupting the intracellular signal chain downstream of the insulin receptor in hepatocytes.
43	21519329	OSM in turn attenuated insulin-dependent Akt activation and, as a downstream target, glucokinase induction in hepatocytes, most likely by inducing suppressor of cytokine signaling 3 (SOCS3).
44	21519329	COX-2 and OSM mRNA were induced early in the course of the development of non-alcoholic steatohepatitis (NASH) in mice.
45	21519329	Thus, induction of OSM production in Kupffer cells by an autocrine PGE(2)-dependent feed-forward loop may be an additional, thus far unrecognized, mechanism contributing to hepatic insulin resistance and the development of NASH.
46	21519329	Oncostatin M produced in Kupffer cells in response to PGE2: possible contributor to hepatic insulin resistance and steatosis.
47	21519329	In a recent study, PGE(2) produced in Kupffer cells attenuated insulin-dependent glucose utilization by interrupting the intracellular signal chain downstream of the insulin receptor in hepatocytes.
48	21519329	OSM in turn attenuated insulin-dependent Akt activation and, as a downstream target, glucokinase induction in hepatocytes, most likely by inducing suppressor of cytokine signaling 3 (SOCS3).
49	21519329	COX-2 and OSM mRNA were induced early in the course of the development of non-alcoholic steatohepatitis (NASH) in mice.
50	21519329	Thus, induction of OSM production in Kupffer cells by an autocrine PGE(2)-dependent feed-forward loop may be an additional, thus far unrecognized, mechanism contributing to hepatic insulin resistance and the development of NASH.