Ignet

Gene Information

Gene symbol: PKM2

Gene name: pyruvate kinase, muscle

HGNC ID: 9021

Related Genes

#	Gene Symbol	Number of hits
1	BRCA2	1 hits
2	CCKBR	1 hits
3	CDX2	1 hits
4	FABP2	1 hits
5	GCG	1 hits
6	GCKR	1 hits
7	GLP1R	1 hits
8	GPD2	1 hits
9	GYG1	1 hits
10	HK1	1 hits
11	HK2	1 hits
12	IL6	1 hits
13	INS	1 hits
14	ISL1	1 hits
15	KCNJ3	1 hits
16	KCNJ6	1 hits
17	LDLR	1 hits
18	PCSK2	1 hits
19	PDK2	1 hits
20	PDK4	1 hits
21	PDLIM5	1 hits
22	PFKL	1 hits
23	PKLR	1 hits
24	PPM2C	1 hits
25	PPP1CB	1 hits
26	PPP1R3C	1 hits
27	PPP5C	1 hits
28	PTPN1	1 hits
29	PYGM	1 hits
30	RORC	1 hits
31	TRIM63	1 hits
32	TTR	1 hits

Related Sentences

#	PMID	Sentence
1	1323058	Effects of interleukin-6 on the expression of thyroid hormone-binding protein genes in cultured human hepatoblastoma-derived (Hep G2) cells.
2	1323058	T4-binding globulin (TBG) shares a high degree of homology with two serpin antiproteases, alpha 1-antichymotrypsin (ACT) and alpha 1-antitrypsin (AT), whose synthesis is increased during the acute phase phenomenon, which accompanies trauma, infections, and neoplasms.
3	1323058	When evaluated in human hepatoblastoma-derived (Hep G2) cells exposed to different doses of the recombinant human cytokine for variable time intervals, IL-6 caused a dose- and time-dependent decrease in the secretion of [35S]methionine-labeled TBG, transthyretin (TTR), and albumin.
4	1323058	IL-6 did, however, cause a decrease in the steady state levels of mRNA for TTR, TBG, and albumin and an increase in ACT and AT mRNAs.
5	1323058	In addition, nuclear run-off assay demonstrated a decrease in the transcription of TTR, TBG, and albumin genes and an increased transcription of the ACT gene.
6	1323058	Quantitation of the results showed that changes in the secretion of proteins, in steady state mRNA levels, and in gene transcription were superimposable for each protein, indicating that IL-6 exerts its effect on thyroid hormone-binding proteins mostly at the transcriptional level and that TTR is the thyroid hormone-binding protein showing the most pronounced negative regulation by IL-6.
7	1323058	The opposite effect of IL-6 on TBG and the antiproteases, despite their structural homology, underscores gene divergence among these proteins.
8	1323058	Effects of interleukin-6 on the expression of thyroid hormone-binding protein genes in cultured human hepatoblastoma-derived (Hep G2) cells.
9	1323058	T4-binding globulin (TBG) shares a high degree of homology with two serpin antiproteases, alpha 1-antichymotrypsin (ACT) and alpha 1-antitrypsin (AT), whose synthesis is increased during the acute phase phenomenon, which accompanies trauma, infections, and neoplasms.
10	1323058	When evaluated in human hepatoblastoma-derived (Hep G2) cells exposed to different doses of the recombinant human cytokine for variable time intervals, IL-6 caused a dose- and time-dependent decrease in the secretion of [35S]methionine-labeled TBG, transthyretin (TTR), and albumin.
11	1323058	IL-6 did, however, cause a decrease in the steady state levels of mRNA for TTR, TBG, and albumin and an increase in ACT and AT mRNAs.
12	1323058	In addition, nuclear run-off assay demonstrated a decrease in the transcription of TTR, TBG, and albumin genes and an increased transcription of the ACT gene.
13	1323058	Quantitation of the results showed that changes in the secretion of proteins, in steady state mRNA levels, and in gene transcription were superimposable for each protein, indicating that IL-6 exerts its effect on thyroid hormone-binding proteins mostly at the transcriptional level and that TTR is the thyroid hormone-binding protein showing the most pronounced negative regulation by IL-6.
14	1323058	The opposite effect of IL-6 on TBG and the antiproteases, despite their structural homology, underscores gene divergence among these proteins.
15	7553078	This paper reviews knowledge on the structure and function and evolution of the thyroid hormone binding protein transthyretin (TTR), with particular reference to factors affecting thyroid hormone distribution and delivery to the brain.
16	9166680	Loci included the G-protein-coupled inwardly rectifying potassium channels expressed in beta-cells (KCNJ3 and KCNJ7), glucagon (GCG), glucokinase regulatory protein (GCKR), glucagon-like peptide I receptor (GLP1R), LIM/homeodomain islet-1 (ISL1), caudal-type homeodomain 3 (CDX3), proprotein convertase 2 (PCSK2), cholecystokinin B receptor (CCKBR), hexokinase 1 (HK1), hexokinase 2 (HK2), mitochondrial FAD-glycerophosphate dehydrogenase (GPD2), liver and muscle forms of pyruvate kinase (PKL, PKM), fatty acid-binding protein 2 (FABP2), hepatic phosphofructokinase (PFKL), protein serine/threonine phosphatase 1 beta (PPP1CB), and low-density lipoprotein receptor (LDLR).
17	18468620	Under various pathophysiological muscle-wasting conditions, such as diabetes and starvation, a family of ubiquitin ligases, including muscle-specific RING-finger protein 1 (MuRF1), are induced to target muscle proteins for degradation via ubiquitination.
18	18468620	Comparison of quadriceps from MuRF1-TG and wild type mice did not reveal elevated multi-ubiquitination of myosin as observed in human patients with muscle wasting.
19	18468620	Instead, MuRF1-TG mice expressed lower levels of pyruvate dehydrogenase (PDH), a mitochondrial key enzyme in charge of glycolysis, and of its regulator PDK2.
20	18468620	Furthermore, yeast two-hybrid interaction studies demonstrated the interaction of MuRF1 with PDH, PDK2, PDK4, PKM2 (all participating in glycolysis) and with phosphorylase beta (PYGM) and glycogenin (both regulating glycogen metabolism).
21	18468620	Consistent with the idea that MuRF1 may regulate carbohydrate metabolism, MuRF1-TG mice had twofold elevated insulin blood levels and lower hepatic glycogen contents.
22	18468620	Taken together, our data demonstrate that MuRF1 expression in skeletal muscle re-directs glycogen synthesis to the liver and stimulates pancreatic insulin secretion, thereby providing a regulatory feedback loop that connects skeletal muscle metabolism with the liver and the pancreas during metabolic stress.
23	23640882	Protein tyrosine phosphatase 1B regulates pyruvate kinase M2 tyrosine phosphorylation.
24	23640882	Here we identify pyruvate kinase M2 (PKM2) as a novel PTP1B substrate in adipocytes.
25	23640882	PTP1B deficiency leads to increased PKM2 total tyrosine and Tyr(105) phosphorylation in cultured adipocytes and in vivo.
26	23640882	Importantly, PTP1B pharmacological inhibition increased PKM2 Tyr-105 phosphorylation and decreased PKM2 activity.
27	23640882	Further, decreased PKM2 Tyr-105 phosphorylation correlates with the development of glucose intolerance and insulin resistance in rodents, non-human primates, and humans.
28	23640882	Together, these findings identify PKM2 as a novel substrate of PTP1B and provide new insights into the regulation of adipose PKM2 activity.
29	23640882	Protein tyrosine phosphatase 1B regulates pyruvate kinase M2 tyrosine phosphorylation.
30	23640882	Here we identify pyruvate kinase M2 (PKM2) as a novel PTP1B substrate in adipocytes.
31	23640882	PTP1B deficiency leads to increased PKM2 total tyrosine and Tyr(105) phosphorylation in cultured adipocytes and in vivo.
32	23640882	Importantly, PTP1B pharmacological inhibition increased PKM2 Tyr-105 phosphorylation and decreased PKM2 activity.
33	23640882	Further, decreased PKM2 Tyr-105 phosphorylation correlates with the development of glucose intolerance and insulin resistance in rodents, non-human primates, and humans.
34	23640882	Together, these findings identify PKM2 as a novel substrate of PTP1B and provide new insights into the regulation of adipose PKM2 activity.
35	23640882	Protein tyrosine phosphatase 1B regulates pyruvate kinase M2 tyrosine phosphorylation.
36	23640882	Here we identify pyruvate kinase M2 (PKM2) as a novel PTP1B substrate in adipocytes.
37	23640882	PTP1B deficiency leads to increased PKM2 total tyrosine and Tyr(105) phosphorylation in cultured adipocytes and in vivo.
38	23640882	Importantly, PTP1B pharmacological inhibition increased PKM2 Tyr-105 phosphorylation and decreased PKM2 activity.
39	23640882	Further, decreased PKM2 Tyr-105 phosphorylation correlates with the development of glucose intolerance and insulin resistance in rodents, non-human primates, and humans.
40	23640882	Together, these findings identify PKM2 as a novel substrate of PTP1B and provide new insights into the regulation of adipose PKM2 activity.
41	23640882	Protein tyrosine phosphatase 1B regulates pyruvate kinase M2 tyrosine phosphorylation.
42	23640882	Here we identify pyruvate kinase M2 (PKM2) as a novel PTP1B substrate in adipocytes.
43	23640882	PTP1B deficiency leads to increased PKM2 total tyrosine and Tyr(105) phosphorylation in cultured adipocytes and in vivo.
44	23640882	Importantly, PTP1B pharmacological inhibition increased PKM2 Tyr-105 phosphorylation and decreased PKM2 activity.
45	23640882	Further, decreased PKM2 Tyr-105 phosphorylation correlates with the development of glucose intolerance and insulin resistance in rodents, non-human primates, and humans.
46	23640882	Together, these findings identify PKM2 as a novel substrate of PTP1B and provide new insights into the regulation of adipose PKM2 activity.
47	23640882	Protein tyrosine phosphatase 1B regulates pyruvate kinase M2 tyrosine phosphorylation.
48	23640882	Here we identify pyruvate kinase M2 (PKM2) as a novel PTP1B substrate in adipocytes.
49	23640882	PTP1B deficiency leads to increased PKM2 total tyrosine and Tyr(105) phosphorylation in cultured adipocytes and in vivo.
50	23640882	Importantly, PTP1B pharmacological inhibition increased PKM2 Tyr-105 phosphorylation and decreased PKM2 activity.
51	23640882	Further, decreased PKM2 Tyr-105 phosphorylation correlates with the development of glucose intolerance and insulin resistance in rodents, non-human primates, and humans.
52	23640882	Together, these findings identify PKM2 as a novel substrate of PTP1B and provide new insights into the regulation of adipose PKM2 activity.
53	23640882	Protein tyrosine phosphatase 1B regulates pyruvate kinase M2 tyrosine phosphorylation.
54	23640882	Here we identify pyruvate kinase M2 (PKM2) as a novel PTP1B substrate in adipocytes.
55	23640882	PTP1B deficiency leads to increased PKM2 total tyrosine and Tyr(105) phosphorylation in cultured adipocytes and in vivo.
56	23640882	Importantly, PTP1B pharmacological inhibition increased PKM2 Tyr-105 phosphorylation and decreased PKM2 activity.
57	23640882	Further, decreased PKM2 Tyr-105 phosphorylation correlates with the development of glucose intolerance and insulin resistance in rodents, non-human primates, and humans.
58	23640882	Together, these findings identify PKM2 as a novel substrate of PTP1B and provide new insights into the regulation of adipose PKM2 activity.
59	23762265	Insulin promotes glucose consumption via regulation of miR-99a/mTOR/PKM2 pathway.
60	23762265	In this study, we showed that insulin decreased miR-99a expression levels, but induced glucose consumption and lactate production, and increased the expression of mTOR, HIF-1α and PKM2 in HepG2 and HL7702 cells.
61	23762265	Forced expression of miR-99a or rapamycin treatment blocked insulin-induced PKM2 and HIF-1α expression, and glucose consumption and lactate production.
62	23762265	Meanwhile, knockdown of HIF-1α inhibited PKM2 expression and insulin-induced glucose consumption.