Ignet

Gene Information

Gene symbol: PSPH

Gene name: phosphoserine phosphatase

HGNC ID: 9577

Related Genes

#	Gene Symbol	Number of hits
1	ADIPOQ	1 hits
2	CYP51A1	1 hits
3	INS	1 hits
4	INSR	1 hits
5	PPA1	1 hits
6	PPP1R3C	1 hits
7	REG1A	1 hits
8	SLC2A4	1 hits

Related Sentences

#	PMID	Sentence
1	1328294	Insulin treatment of diabetic animals for 5 d restored glucose transport activity, GLUT-4 protein, and GLUT-4 phosphorylation to control levels whereas vanadate and phlorizin were ineffective.
2	1328294	In control adipocytes, insulin promoted GLUT-4 translocation from the low density microsomal (LDM) pool to the plasma membranes (PM) and decreased the state of GLUT-4 phosphorylation.
3	1328294	In adipocytes isolated from the diabetic rats, insulin failed to stimulate GLUT-4 translocation and to decrease GLUT-4 phosphorylation.
4	1328294	To explore the mechanism of the diabetes-induced increases in the GLUT-4 phosphorylation, we investigated phosphoserine phosphatase (PSPase) activities using 32P-labeled GLUT-4 and phosphorylase "a" as substrates.
5	1328294	Although reduced cytosolic PSPase activity correlated with an inadequate dephosphorylation of LDM GLUT-4, the existence of highly phosphorylated PM GLUT-4 in the presence of increased particulate PSPase activity required additional explanation.
6	1328294	Highly active diabetic particulate PSPase, which dephosphorylated control GLUT-4 and phosphorylase a, failed to dephosphorylate PM GLUT-4 from diabetic rats.
7	1328294	These data suggest that PM GLUT-4 from diabetic rats is unable to interact with PSPase or that its phosphorylation sites are not accessible to PSPase action.
8	1328294	In contrast to normal cells, insulin failed to promote GLUT-4 recruitment to the plasma membranes and its dephosphorylation in diabetic adipocytes.
9	1328294	Insulin treatment of diabetic animals for 5 d restored glucose transport activity, GLUT-4 protein, and GLUT-4 phosphorylation to control levels whereas vanadate and phlorizin were ineffective.
10	1328294	In control adipocytes, insulin promoted GLUT-4 translocation from the low density microsomal (LDM) pool to the plasma membranes (PM) and decreased the state of GLUT-4 phosphorylation.
11	1328294	In adipocytes isolated from the diabetic rats, insulin failed to stimulate GLUT-4 translocation and to decrease GLUT-4 phosphorylation.
12	1328294	To explore the mechanism of the diabetes-induced increases in the GLUT-4 phosphorylation, we investigated phosphoserine phosphatase (PSPase) activities using 32P-labeled GLUT-4 and phosphorylase "a" as substrates.
13	1328294	Although reduced cytosolic PSPase activity correlated with an inadequate dephosphorylation of LDM GLUT-4, the existence of highly phosphorylated PM GLUT-4 in the presence of increased particulate PSPase activity required additional explanation.
14	1328294	Highly active diabetic particulate PSPase, which dephosphorylated control GLUT-4 and phosphorylase a, failed to dephosphorylate PM GLUT-4 from diabetic rats.
15	1328294	These data suggest that PM GLUT-4 from diabetic rats is unable to interact with PSPase or that its phosphorylation sites are not accessible to PSPase action.
16	1328294	In contrast to normal cells, insulin failed to promote GLUT-4 recruitment to the plasma membranes and its dephosphorylation in diabetic adipocytes.
17	1328294	Insulin treatment of diabetic animals for 5 d restored glucose transport activity, GLUT-4 protein, and GLUT-4 phosphorylation to control levels whereas vanadate and phlorizin were ineffective.
18	1328294	In control adipocytes, insulin promoted GLUT-4 translocation from the low density microsomal (LDM) pool to the plasma membranes (PM) and decreased the state of GLUT-4 phosphorylation.
19	1328294	In adipocytes isolated from the diabetic rats, insulin failed to stimulate GLUT-4 translocation and to decrease GLUT-4 phosphorylation.
20	1328294	To explore the mechanism of the diabetes-induced increases in the GLUT-4 phosphorylation, we investigated phosphoserine phosphatase (PSPase) activities using 32P-labeled GLUT-4 and phosphorylase "a" as substrates.
21	1328294	Although reduced cytosolic PSPase activity correlated with an inadequate dephosphorylation of LDM GLUT-4, the existence of highly phosphorylated PM GLUT-4 in the presence of increased particulate PSPase activity required additional explanation.
22	1328294	Highly active diabetic particulate PSPase, which dephosphorylated control GLUT-4 and phosphorylase a, failed to dephosphorylate PM GLUT-4 from diabetic rats.
23	1328294	These data suggest that PM GLUT-4 from diabetic rats is unable to interact with PSPase or that its phosphorylation sites are not accessible to PSPase action.
24	1328294	In contrast to normal cells, insulin failed to promote GLUT-4 recruitment to the plasma membranes and its dephosphorylation in diabetic adipocytes.
25	1328294	Insulin treatment of diabetic animals for 5 d restored glucose transport activity, GLUT-4 protein, and GLUT-4 phosphorylation to control levels whereas vanadate and phlorizin were ineffective.
26	1328294	In control adipocytes, insulin promoted GLUT-4 translocation from the low density microsomal (LDM) pool to the plasma membranes (PM) and decreased the state of GLUT-4 phosphorylation.
27	1328294	In adipocytes isolated from the diabetic rats, insulin failed to stimulate GLUT-4 translocation and to decrease GLUT-4 phosphorylation.
28	1328294	To explore the mechanism of the diabetes-induced increases in the GLUT-4 phosphorylation, we investigated phosphoserine phosphatase (PSPase) activities using 32P-labeled GLUT-4 and phosphorylase "a" as substrates.
29	1328294	Although reduced cytosolic PSPase activity correlated with an inadequate dephosphorylation of LDM GLUT-4, the existence of highly phosphorylated PM GLUT-4 in the presence of increased particulate PSPase activity required additional explanation.
30	1328294	Highly active diabetic particulate PSPase, which dephosphorylated control GLUT-4 and phosphorylase a, failed to dephosphorylate PM GLUT-4 from diabetic rats.
31	1328294	These data suggest that PM GLUT-4 from diabetic rats is unable to interact with PSPase or that its phosphorylation sites are not accessible to PSPase action.
32	1328294	In contrast to normal cells, insulin failed to promote GLUT-4 recruitment to the plasma membranes and its dephosphorylation in diabetic adipocytes.
33	1661692	Differential effects of diabetes on adipocyte and liver phosphotyrosine and phosphoserine phosphatase activities.
34	1661692	PTPase activity was assessed with [32P]tyrosine-phosphorylated insulin receptor (IR), whereas PSPase activity was assayed with [32P]serine-phosphorylated glycogen synthase.
35	1661692	Insulin therapy for 14 or 30 days restored PTPase and PSPase activities in both fractions.
36	1661692	Differential effects of diabetes on adipocyte and liver phosphotyrosine and phosphoserine phosphatase activities.
37	1661692	PTPase activity was assessed with [32P]tyrosine-phosphorylated insulin receptor (IR), whereas PSPase activity was assayed with [32P]serine-phosphorylated glycogen synthase.
38	1661692	Insulin therapy for 14 or 30 days restored PTPase and PSPase activities in both fractions.
39	1661692	Differential effects of diabetes on adipocyte and liver phosphotyrosine and phosphoserine phosphatase activities.
40	1661692	PTPase activity was assessed with [32P]tyrosine-phosphorylated insulin receptor (IR), whereas PSPase activity was assayed with [32P]serine-phosphorylated glycogen synthase.
41	1661692	Insulin therapy for 14 or 30 days restored PTPase and PSPase activities in both fractions.
42	8189325	In order to study the mechanism and origin of urine pancreatic stone protein (PSP), PSP was analyzed in the urine and sera from healthy subjects, patients with renal disease, and intensive care patients by Mono S chromatography and Western blotting.
43	8482198	Recent literature indicates that a decrease in the activity of pancreatic stone protein (PSP), which inhibits CaCO3 crystal formation in pancreatic juice, is closely related to the development of chronic calcifying pancreatitis.
44	16307847	In rodent studies, measures which increase [Ca2+]i in adipocytes and skeletal muscle are associated with impaired insulin signaling, attributable at least in part to diminished ability of insulin to activate phosphoserine phosphatase-1 (PP-1).
45	16307847	Clinical insulin resistance is associated with increased levels of triglycerides and other fatty acid metabolites in muscle fibers; this can give rise to diacylglycerol-mediated activation of PKC, which in turn compromises insulin signaling by triggering kinase cascades that phosphorylate IRS-1 on key serine residues.
46	16307847	Thus, the PKC activation associated with fat overexposure might be expected to boost basal [Ca2+]i in skeletal muscle, potentially impeding insulin-mediated activation of PP-1.
47	16307847	Since parathyroid hormone can act on adipocytes and muscle to boost [Ca2+]i, mild secondary hyperparathyroidism associated with low calcium intakes and poor vitamin D status may contribute to insulin resistance, consistent with certain clinical and epidemiological findings.