Ignet

Gene Information

Gene symbol: MBTPS1

Gene name: membrane-bound transcription factor peptidase, site 1

HGNC ID: 15456

Synonyms: S1P, KIAA0091, SKI-1, PCSK8

Related Genes

#	Gene Symbol	Number of hits
1	AKT1	1 hits
2	ALB	1 hits
3	CBX4	1 hits
4	CNTN4	1 hits
5	CTGF	1 hits
6	DUSP6	1 hits
7	HHAT	1 hits
8	INS	1 hits
9	KCNN1	1 hits
10	LPHN2	1 hits
11	MAPK3	1 hits
12	MAPK8	1 hits
13	NFATC1	1 hits
14	NOS3	1 hits
15	ORAI1	1 hits
16	PCSK1	1 hits
17	PCSK9	1 hits
18	POMC	1 hits
19	RAC1	1 hits
20	S1PR1	1 hits
21	S1PR2	1 hits
22	S1PR3	1 hits
23	S1PR4	1 hits
24	SCG5	1 hits
25	SGPL1	1 hits
26	SGPP1	1 hits
27	SKI	1 hits
28	SKIV2L	1 hits
29	SPHK1	1 hits
30	SPHK2	1 hits
31	SREBF1	1 hits
32	STIM1	1 hits
33	XRN1	1 hits

Related Sentences

#	PMID	Sentence
1	7739557	We show that this cap binding also occurs in vivo and that, while this activity is required for expression of viral information (killer toxin mRNA level and toxin production) in a wild-type strain, this requirement is suppressed by deletion of SKI1/XRN1/SEP1.
2	7739557	Thus, L-A decoys the SKI1/XRN1/SEP1 exonuclease directed at 5' uncapped ends, but translation of the L-A poly(A)- mRNA is repressed by Ski2,3,8p.
3	8982451	SKI1/XRN1 is a 5'--> 3' exoribonuclease that degrades uncapped mRNAs.
4	10074137	The ski7 antiviral protein is an EF1-alpha homolog that blocks expression of non-Poly(A) mRNA in Saccharomyces cerevisiae.
5	10074137	Our experiments showed that Ski7p is part of the Ski2p-Ski3p-Ski8p antiviral system because a single ski7 mutation derepresses the expression of non-poly(A) mRNA as much as a quadruple ski2 ski3 ski7 ski8 mutation, and the effect of the overexpression of Ski7p is not obtained unless other SKI genes are functional. ski1/xrn1Delta ski2Delta and ski1/xrn1Delta ski7Delta mutants were viable but temperature sensitive for growth.
6	10816641	Emphasis on PC1, PC2/7B2, POMC and the novel enzyme SKI-1.
7	10816641	Processing of POMC at dibasic residues is tissue-specific and is performed by either PC1 alone (resulting in ACTH and beta LPH, anterior pituitary corticotrophes) or by a combination of PC1 and PC2 (yielding alpha MSH and beta END, pituitary neurointermediate lobe and hypothalamus).
8	10816641	Structure-function studies of these enzymes demonstrated the presence of N- and C-terminal domains, as well as specific amino acids within the catalytic segment that influence the degree of activity of each enzyme and the interaction of PC2 with 7B2.
9	10816641	The phenotypic consequences of the absence of genetic expression of either PC1 or PC2 are now explored using knockout mice and in human patients suffering from obesity and diabetes.
10	12270137	Phytosphingosine 1-phosphate: a high affinity ligand for the S1P(4)/Edg-6 receptor.
11	12270137	The S1P(4) receptor has generated interest due to its lymphoid tissue distribution.
12	12270137	While the S1P(4) receptor binds the prototypical ligand, S1P, a survey of other lysosphingolipids demonstrated that 4D-hydroxysphinganine 1-phosphate, more commonly known as phytosphingosine 1-phosphate (PhS1P), binds to S1P(4) with higher affinity.
13	12270137	Using radiolabeled S1P (S133P), the affinity of PhS1P for the S1P(4) receptor is 1.6nM, while that of S1P is nearly 50-fold lower (119+/-20nM).
14	12270137	The present study demonstrates the utility of a novel radiolabeled probe, PhS133P, for in vitro studies of the S1P(4) receptor pharmacology.
15	12270137	Phytosphingosine 1-phosphate: a high affinity ligand for the S1P(4)/Edg-6 receptor.
16	12270137	The S1P(4) receptor has generated interest due to its lymphoid tissue distribution.
17	12270137	While the S1P(4) receptor binds the prototypical ligand, S1P, a survey of other lysosphingolipids demonstrated that 4D-hydroxysphinganine 1-phosphate, more commonly known as phytosphingosine 1-phosphate (PhS1P), binds to S1P(4) with higher affinity.
18	12270137	Using radiolabeled S1P (S133P), the affinity of PhS1P for the S1P(4) receptor is 1.6nM, while that of S1P is nearly 50-fold lower (119+/-20nM).
19	12270137	The present study demonstrates the utility of a novel radiolabeled probe, PhS133P, for in vitro studies of the S1P(4) receptor pharmacology.
20	12270137	Phytosphingosine 1-phosphate: a high affinity ligand for the S1P(4)/Edg-6 receptor.
21	12270137	The S1P(4) receptor has generated interest due to its lymphoid tissue distribution.
22	12270137	While the S1P(4) receptor binds the prototypical ligand, S1P, a survey of other lysosphingolipids demonstrated that 4D-hydroxysphinganine 1-phosphate, more commonly known as phytosphingosine 1-phosphate (PhS1P), binds to S1P(4) with higher affinity.
23	12270137	Using radiolabeled S1P (S133P), the affinity of PhS1P for the S1P(4) receptor is 1.6nM, while that of S1P is nearly 50-fold lower (119+/-20nM).
24	12270137	The present study demonstrates the utility of a novel radiolabeled probe, PhS133P, for in vitro studies of the S1P(4) receptor pharmacology.
25	12270137	Phytosphingosine 1-phosphate: a high affinity ligand for the S1P(4)/Edg-6 receptor.
26	12270137	The S1P(4) receptor has generated interest due to its lymphoid tissue distribution.
27	12270137	While the S1P(4) receptor binds the prototypical ligand, S1P, a survey of other lysosphingolipids demonstrated that 4D-hydroxysphinganine 1-phosphate, more commonly known as phytosphingosine 1-phosphate (PhS1P), binds to S1P(4) with higher affinity.
28	12270137	Using radiolabeled S1P (S133P), the affinity of PhS1P for the S1P(4) receptor is 1.6nM, while that of S1P is nearly 50-fold lower (119+/-20nM).
29	12270137	The present study demonstrates the utility of a novel radiolabeled probe, PhS133P, for in vitro studies of the S1P(4) receptor pharmacology.
30	12270137	Phytosphingosine 1-phosphate: a high affinity ligand for the S1P(4)/Edg-6 receptor.
31	12270137	The S1P(4) receptor has generated interest due to its lymphoid tissue distribution.
32	12270137	While the S1P(4) receptor binds the prototypical ligand, S1P, a survey of other lysosphingolipids demonstrated that 4D-hydroxysphinganine 1-phosphate, more commonly known as phytosphingosine 1-phosphate (PhS1P), binds to S1P(4) with higher affinity.
33	12270137	Using radiolabeled S1P (S133P), the affinity of PhS1P for the S1P(4) receptor is 1.6nM, while that of S1P is nearly 50-fold lower (119+/-20nM).
34	12270137	The present study demonstrates the utility of a novel radiolabeled probe, PhS133P, for in vitro studies of the S1P(4) receptor pharmacology.
35	15855330	Sphingosine kinase (SPHK) and S1P were characterized in INS-1 insulinoma cells and isolated rat islets of Langerhans.
36	15855330	SPHK activity increased in INS-1 cell homogenates treated with interleukin-1beta (IL-1beta) or tumor necrosis factor-alpha (TNF-alpha), and responses were additive.
37	15855330	IL-1beta or TNF-alpha increased islet SPHK activity within 15 min to 1 h; activity remained elevated after 8 h.
38	15855330	SPHK2 was the predominant active isoform in INS-1 cells; little or no SPHK1 activity was detected.
39	15855330	Compared with basal values, IL-1beta and TNF-alpha induced increases in SPHK1a mRNA levels relative to 18S ribosomal RNA in INS-1 cells within 1 h; relative SPHK2 mRNA levels were unchanged after cytokine treatment.
40	15855330	IL-1beta, but not TNF-alpha, induced relative SPHK1a mRNA expression levels within 1 h in islets, whereas SPHK2 mRNA levels were unchanged.
41	15855330	Thus, IL-1beta and TNF-alpha induced an early and sustained increase in SPHK activity in INS-1 cells and isolated islets, suggesting that S1P plays a role in the pathological response of pancreatic beta-cells to cytokines.
42	16215768	Two additional PC subtypes--called subtilisin kexin isozyme 1 (SKI-1) or site 1 protease (S1P) and neural apoptosis regulated convertase 1 (NARC-1), also known as PCSK9--that cleave at the carboxy terminus of nonbasic amino acids were discovered later.
43	16234413	In endothelial cells, S1P has been shown to modulate the activity of the endothelial nitric-oxide synthase (eNOS) through phosphorylation operated by Akt.
44	16234413	Nitric oxide (NO) produced by neuronal nitric-oxide synthase and eNOS plays a central role in triggering and maintaining penile erection.
45	16234413	This study has assessed the possibility of a similar cross-talk between eNOS and S1P in human corpus cavernosum and whether this interaction is connected to penile vascular response.
46	16234413	Quantitative reverse transcription-polymerase chain reaction demonstrated the presence of S1P(1), S1P(2), and S1P(3) receptors in both the human corpus cavernosum (HCC) and the penile artery.
47	16234413	In human tissue, S1P seems to be the possible candidate for the activation of the eNOS calcium-independent pathway.
48	16234413	In endothelial cells, S1P has been shown to modulate the activity of the endothelial nitric-oxide synthase (eNOS) through phosphorylation operated by Akt.
49	16234413	Nitric oxide (NO) produced by neuronal nitric-oxide synthase and eNOS plays a central role in triggering and maintaining penile erection.
50	16234413	This study has assessed the possibility of a similar cross-talk between eNOS and S1P in human corpus cavernosum and whether this interaction is connected to penile vascular response.
51	16234413	Quantitative reverse transcription-polymerase chain reaction demonstrated the presence of S1P(1), S1P(2), and S1P(3) receptors in both the human corpus cavernosum (HCC) and the penile artery.
52	16234413	In human tissue, S1P seems to be the possible candidate for the activation of the eNOS calcium-independent pathway.
53	16234413	In endothelial cells, S1P has been shown to modulate the activity of the endothelial nitric-oxide synthase (eNOS) through phosphorylation operated by Akt.
54	16234413	Nitric oxide (NO) produced by neuronal nitric-oxide synthase and eNOS plays a central role in triggering and maintaining penile erection.
55	16234413	This study has assessed the possibility of a similar cross-talk between eNOS and S1P in human corpus cavernosum and whether this interaction is connected to penile vascular response.
56	16234413	Quantitative reverse transcription-polymerase chain reaction demonstrated the presence of S1P(1), S1P(2), and S1P(3) receptors in both the human corpus cavernosum (HCC) and the penile artery.
57	16234413	In human tissue, S1P seems to be the possible candidate for the activation of the eNOS calcium-independent pathway.
58	16234413	In endothelial cells, S1P has been shown to modulate the activity of the endothelial nitric-oxide synthase (eNOS) through phosphorylation operated by Akt.
59	16234413	Nitric oxide (NO) produced by neuronal nitric-oxide synthase and eNOS plays a central role in triggering and maintaining penile erection.
60	16234413	This study has assessed the possibility of a similar cross-talk between eNOS and S1P in human corpus cavernosum and whether this interaction is connected to penile vascular response.
61	16234413	Quantitative reverse transcription-polymerase chain reaction demonstrated the presence of S1P(1), S1P(2), and S1P(3) receptors in both the human corpus cavernosum (HCC) and the penile artery.
62	16234413	In human tissue, S1P seems to be the possible candidate for the activation of the eNOS calcium-independent pathway.
63	17012247	Proteolysis occurring at basic residues is mediated by the basic amino acid-specific proprotein convertases, namely: PC1/3, PC2, furin, PACE4, PC4, PC5/6, and PC7.
64	17012247	In contrast, proteolysis at nonbasic residues is performed by the subtilisin/kexin-like isozyme-1 (SKI-1/S1P) and the newly identified neural apoptosis-regulated convertase-1 (PCSK9/NARC-1).
65	18424450	Sphingosine kinase 1/S1P receptor signaling axis controls glial proliferation in mice with Sandhoff disease.
66	18424450	A similar result of milder disease course and reduced astroglial proliferation was obtained by deletion of the gene for the S1P(3) receptor, a G protein-coupled receptor enriched in astrocytes.
67	18424450	Because astrocyte responses are involved in many types of neurodegeneration, the Sphk1/S1P receptor signaling axis may be generally important during the pathogenesis of neurodegenerative diseases.
68	18424450	Sphingosine kinase 1/S1P receptor signaling axis controls glial proliferation in mice with Sandhoff disease.
69	18424450	A similar result of milder disease course and reduced astroglial proliferation was obtained by deletion of the gene for the S1P(3) receptor, a G protein-coupled receptor enriched in astrocytes.
70	18424450	Because astrocyte responses are involved in many types of neurodegeneration, the Sphk1/S1P receptor signaling axis may be generally important during the pathogenesis of neurodegenerative diseases.
71	18424450	Sphingosine kinase 1/S1P receptor signaling axis controls glial proliferation in mice with Sandhoff disease.
72	18424450	A similar result of milder disease course and reduced astroglial proliferation was obtained by deletion of the gene for the S1P(3) receptor, a G protein-coupled receptor enriched in astrocytes.
73	18424450	Because astrocyte responses are involved in many types of neurodegeneration, the Sphk1/S1P receptor signaling axis may be generally important during the pathogenesis of neurodegenerative diseases.
74	18775682	As a consequence of the prolonged intracellular Ca2+ rise following preincubation with glycated albumin, the S1P-induced activation of the Ca2+-dependent phosphatase, calcineurin (CaN) was increased.
75	18775682	This resulted in increased S1P-induced activation of the Ca2+-dependent transcription factor, nuclear factor of activated T cells (NFATc).
76	18775682	As a consequence of the prolonged intracellular Ca2+ rise following preincubation with glycated albumin, the S1P-induced activation of the Ca2+-dependent phosphatase, calcineurin (CaN) was increased.
77	18775682	This resulted in increased S1P-induced activation of the Ca2+-dependent transcription factor, nuclear factor of activated T cells (NFATc).
78	19091959	Sphingosine-1-phosphate inhibits high glucose-mediated ERK1/2 action in endothelium through induction of MAP kinase phosphatase-3.
79	19091959	We previously reported that Type 1 diabetic NOD mice have increased endothelial activation, with increased production of monocyte chemoattractant protein (MCP)-1 and IL-6, and a 30% increase of surface VCAM-1 expression leading to a fourfold increase in monocyte adhesion to the endothelium.
80	19091959	MKP-3 selectively regulates ERK1/2 activity through dephosphorylation.
81	19091959	Incubation of diabetic NOD EC with S1P and the S1P(1)-selective agonist SEW2871 significantly increased expression of MKP-3 and reduced ERK1/2 phosphorylation, while incubation with the S1P(1)/S1P(3) antagonist VPC23019 decreased the expression of MKP-3, both results supporting a role for S1P(1) in MKP-3 regulation.
82	19091959	Overexpression of MKP-3 in glucose-cultured HAEC decreased ERK1/2 phosphorylation and resulted in decreased monocyte:endothelial interactions in a static monocyte adhesion assay.
83	19091959	Thus, one mechanism for the anti-inflammatory action of S1P in diabetic EC is inhibition of ERK1/2 phosphorylation through induction of MKP-3 expression via the S1P-S1P(1) receptor axis.
84	19139947	The S1P(2) receptor expressed in human platelets is linked to the RhoA-Rho kinase pathway and is down regulated in type 2 diabetes.
85	19139947	S1P(2) receptor expression (Western blotting) was detected in washed human platelets from healthy volunteers.
86	19139947	The S1P-induced increase in Ca(2+) was sensitive to the S1P(2) receptor antagonist JTE-013 but not the S1P(1/3) antagonist VPC23019.
87	19139947	Platelets from patients with type 2 diabetes demonstrated an attenuated aggregability to S1P as well as decreased levels of the full-length S1P(2) protein.
88	19139947	The S1P(2) antibody used identified a 45 kDa receptor cleavage product in patients with diabetes that could also be generated from healthy human platelet lysates by the addition of the Ca(2+)-activated protease, mu-calpain.
89	19139947	These results indicate that the S1P(2) receptor is involved in S1P-induced platelet aggregation and Rho kinase activation.
90	19139947	Moreover, in platelets from patients with type 2 diabetes, responses to S1P are attenuated via a phenomenon attributed to the calpain-dependent cleavage of the S1P(2) receptor.
91	19139947	The S1P(2) receptor expressed in human platelets is linked to the RhoA-Rho kinase pathway and is down regulated in type 2 diabetes.
92	19139947	S1P(2) receptor expression (Western blotting) was detected in washed human platelets from healthy volunteers.
93	19139947	The S1P-induced increase in Ca(2+) was sensitive to the S1P(2) receptor antagonist JTE-013 but not the S1P(1/3) antagonist VPC23019.
94	19139947	Platelets from patients with type 2 diabetes demonstrated an attenuated aggregability to S1P as well as decreased levels of the full-length S1P(2) protein.
95	19139947	The S1P(2) antibody used identified a 45 kDa receptor cleavage product in patients with diabetes that could also be generated from healthy human platelet lysates by the addition of the Ca(2+)-activated protease, mu-calpain.
96	19139947	These results indicate that the S1P(2) receptor is involved in S1P-induced platelet aggregation and Rho kinase activation.
97	19139947	Moreover, in platelets from patients with type 2 diabetes, responses to S1P are attenuated via a phenomenon attributed to the calpain-dependent cleavage of the S1P(2) receptor.
98	19139947	The S1P(2) receptor expressed in human platelets is linked to the RhoA-Rho kinase pathway and is down regulated in type 2 diabetes.
99	19139947	S1P(2) receptor expression (Western blotting) was detected in washed human platelets from healthy volunteers.
100	19139947	The S1P-induced increase in Ca(2+) was sensitive to the S1P(2) receptor antagonist JTE-013 but not the S1P(1/3) antagonist VPC23019.
101	19139947	Platelets from patients with type 2 diabetes demonstrated an attenuated aggregability to S1P as well as decreased levels of the full-length S1P(2) protein.
102	19139947	The S1P(2) antibody used identified a 45 kDa receptor cleavage product in patients with diabetes that could also be generated from healthy human platelet lysates by the addition of the Ca(2+)-activated protease, mu-calpain.
103	19139947	These results indicate that the S1P(2) receptor is involved in S1P-induced platelet aggregation and Rho kinase activation.
104	19139947	Moreover, in platelets from patients with type 2 diabetes, responses to S1P are attenuated via a phenomenon attributed to the calpain-dependent cleavage of the S1P(2) receptor.
105	19139947	The S1P(2) receptor expressed in human platelets is linked to the RhoA-Rho kinase pathway and is down regulated in type 2 diabetes.
106	19139947	S1P(2) receptor expression (Western blotting) was detected in washed human platelets from healthy volunteers.
107	19139947	The S1P-induced increase in Ca(2+) was sensitive to the S1P(2) receptor antagonist JTE-013 but not the S1P(1/3) antagonist VPC23019.
108	19139947	Platelets from patients with type 2 diabetes demonstrated an attenuated aggregability to S1P as well as decreased levels of the full-length S1P(2) protein.
109	19139947	The S1P(2) antibody used identified a 45 kDa receptor cleavage product in patients with diabetes that could also be generated from healthy human platelet lysates by the addition of the Ca(2+)-activated protease, mu-calpain.
110	19139947	These results indicate that the S1P(2) receptor is involved in S1P-induced platelet aggregation and Rho kinase activation.
111	19139947	Moreover, in platelets from patients with type 2 diabetes, responses to S1P are attenuated via a phenomenon attributed to the calpain-dependent cleavage of the S1P(2) receptor.
112	19139947	The S1P(2) receptor expressed in human platelets is linked to the RhoA-Rho kinase pathway and is down regulated in type 2 diabetes.
113	19139947	S1P(2) receptor expression (Western blotting) was detected in washed human platelets from healthy volunteers.
114	19139947	The S1P-induced increase in Ca(2+) was sensitive to the S1P(2) receptor antagonist JTE-013 but not the S1P(1/3) antagonist VPC23019.
115	19139947	Platelets from patients with type 2 diabetes demonstrated an attenuated aggregability to S1P as well as decreased levels of the full-length S1P(2) protein.
116	19139947	The S1P(2) antibody used identified a 45 kDa receptor cleavage product in patients with diabetes that could also be generated from healthy human platelet lysates by the addition of the Ca(2+)-activated protease, mu-calpain.
117	19139947	These results indicate that the S1P(2) receptor is involved in S1P-induced platelet aggregation and Rho kinase activation.
118	19139947	Moreover, in platelets from patients with type 2 diabetes, responses to S1P are attenuated via a phenomenon attributed to the calpain-dependent cleavage of the S1P(2) receptor.
119	19139947	The S1P(2) receptor expressed in human platelets is linked to the RhoA-Rho kinase pathway and is down regulated in type 2 diabetes.
120	19139947	S1P(2) receptor expression (Western blotting) was detected in washed human platelets from healthy volunteers.
121	19139947	The S1P-induced increase in Ca(2+) was sensitive to the S1P(2) receptor antagonist JTE-013 but not the S1P(1/3) antagonist VPC23019.
122	19139947	Platelets from patients with type 2 diabetes demonstrated an attenuated aggregability to S1P as well as decreased levels of the full-length S1P(2) protein.
123	19139947	The S1P(2) antibody used identified a 45 kDa receptor cleavage product in patients with diabetes that could also be generated from healthy human platelet lysates by the addition of the Ca(2+)-activated protease, mu-calpain.
124	19139947	These results indicate that the S1P(2) receptor is involved in S1P-induced platelet aggregation and Rho kinase activation.
125	19139947	Moreover, in platelets from patients with type 2 diabetes, responses to S1P are attenuated via a phenomenon attributed to the calpain-dependent cleavage of the S1P(2) receptor.
126	19139947	The S1P(2) receptor expressed in human platelets is linked to the RhoA-Rho kinase pathway and is down regulated in type 2 diabetes.
127	19139947	S1P(2) receptor expression (Western blotting) was detected in washed human platelets from healthy volunteers.
128	19139947	The S1P-induced increase in Ca(2+) was sensitive to the S1P(2) receptor antagonist JTE-013 but not the S1P(1/3) antagonist VPC23019.
129	19139947	Platelets from patients with type 2 diabetes demonstrated an attenuated aggregability to S1P as well as decreased levels of the full-length S1P(2) protein.
130	19139947	The S1P(2) antibody used identified a 45 kDa receptor cleavage product in patients with diabetes that could also be generated from healthy human platelet lysates by the addition of the Ca(2+)-activated protease, mu-calpain.
131	19139947	These results indicate that the S1P(2) receptor is involved in S1P-induced platelet aggregation and Rho kinase activation.
132	19139947	Moreover, in platelets from patients with type 2 diabetes, responses to S1P are attenuated via a phenomenon attributed to the calpain-dependent cleavage of the S1P(2) receptor.
133	19150609	Chemical lead 2 (CL2) is the first non-sphingosine-1-phosphate (Sph-1-P) analog type antagonist of endothelial differentiation gene-1 (Edg-1/S1P(1)), which is a member of the Sph-1-P receptor family.
134	19150609	It significantly inhibited angiogenesis induced by vascular endothelial growth factor in a rabbit cornea model as well as the swelling of mouse feet in an anti-type II collagen antibody-induced arthritis model.
135	19662499	In skeletal muscle cells S1P, through engagement of its S1P(2) receptor, is found to produce a transient burst of reactive oxygen species through a calcium-dependent activation of the small GTPase Rac1.
136	19662499	S1P-induced redox-signaling is sensed by protein tyrosine phosphatase-1B, the main negative regulator of insulin receptor phosphorylation, which undergoes oxidation and enzymatic inhibition.
137	20060809	In this study, we investigated the potential role of S1P(2) in streptozotocin (STZ)-induced apoptosis of pancreatic beta-cells and progression of diabetes.
138	20060809	S1P(2)(-/-) mice showed higher insulin/glucose ratios (an index of relative insulin deficiency) and larger insulin-positive islet areas to administration of a low dose of STZ than WT mice.
139	20060809	Our findings indicate that blockade of S1P(2) signaling attenuates STZ-induced apoptosis of pancreatic beta-cells and decreases the incidence of diabetes.
140	20060809	In this study, we investigated the potential role of S1P(2) in streptozotocin (STZ)-induced apoptosis of pancreatic beta-cells and progression of diabetes.
141	20060809	S1P(2)(-/-) mice showed higher insulin/glucose ratios (an index of relative insulin deficiency) and larger insulin-positive islet areas to administration of a low dose of STZ than WT mice.
142	20060809	Our findings indicate that blockade of S1P(2) signaling attenuates STZ-induced apoptosis of pancreatic beta-cells and decreases the incidence of diabetes.
143	20060809	In this study, we investigated the potential role of S1P(2) in streptozotocin (STZ)-induced apoptosis of pancreatic beta-cells and progression of diabetes.
144	20060809	S1P(2)(-/-) mice showed higher insulin/glucose ratios (an index of relative insulin deficiency) and larger insulin-positive islet areas to administration of a low dose of STZ than WT mice.
145	20060809	Our findings indicate that blockade of S1P(2) signaling attenuates STZ-induced apoptosis of pancreatic beta-cells and decreases the incidence of diabetes.
146	21270296	SOCE was observed in VSMCs lacking either S1P(2) or S1P(3) receptors, suggesting that S1P acts via multiple signaling pathways.
147	21270296	Finally, S1P-induced SOCE was larger in proliferative than in contractile VSMCs, correlating with increases in STIM1, Orai1, S1P(1), and S1P(3) receptor mRNA.
148	21270296	SOCE was observed in VSMCs lacking either S1P(2) or S1P(3) receptors, suggesting that S1P acts via multiple signaling pathways.
149	21270296	Finally, S1P-induced SOCE was larger in proliferative than in contractile VSMCs, correlating with increases in STIM1, Orai1, S1P(1), and S1P(3) receptor mRNA.
150	22031849	Site 1 protease was required, since its inhibition by AEBSF prevented SREBP-1 activation.
151	22031849	SCAP, the ER-associated chaperone for SREBP-1, was also necessary since its inhibitor fatostatin also blocked SREBP-1 activation.
152	22031849	Signaling through the EGFR/phosphatidylinositol 3-kinase (PI3K) pathway, which we previously showed mediates HG-induced TGF-β1 upregulation, and through RhoA, were upstream of SREBP-1 activation (Wu D, Peng F, Zhang B, Ingram AJ, Gao B, Krepinsky JC.
153	22031849	Thus HG-induced SREBP-1 activation requires EGFR/PI3K/RhoA signaling and SCAP-mediated transport to the Golgi for its proteolytic cleavage.
154	22389505	Moreover, knockdown of SphK2 alone results in decreased GSIS, whereas knockdown of the S1P phosphatase, Sgpp1, leads to a rise in GSIS.
155	22422617	In these cells, treatment with pertussis toxin abolished LDL-stimulated activation of ERK1/2 and c-Jun N-terminal kinase (JNK), indicating the involvement of heterotrimeric G proteins in LDL signaling.
156	22422617	Treatment with LDL promoted activation and translocation of endogenous sphingosine kinase 1 (SK1) from the cytosol to the plasma membrane concomitant with production of sphingosine-1-phosphate (S1P).
157	22422617	Pretreating cells with SK inhibitor, dimethylsphinogsine or down-regulation of SK1 and SK2 revealed that LDL-dependent activation of ERK1/2 and JNK is mediated by SK1.
158	22422617	Pretreating cells with S1P₁/S1P₃ receptor antagonist VPC23019 significantly inhibited activation of ERK1/2 and JNK by LDL, suggesting that LDL elicits G protein-dependent activation of ERK1/2 and JNK by stimulating SK1-dependent transactivation of S1P receptors.
159	22422617	Furthermore, S1P stimulation induced expression of CTGF in a dose-dependent manner that was markedly inhibited by blocking the ERK1/2 and JNK signaling pathways.
160	22422617	Our data suggest that SK1-dependent S1P receptor transactivation is upstream of ERK1/2 and JNK and that all three steps are required for LDL-regulated expression of CTGF in mesangial cells.
161	22422617	In these cells, treatment with pertussis toxin abolished LDL-stimulated activation of ERK1/2 and c-Jun N-terminal kinase (JNK), indicating the involvement of heterotrimeric G proteins in LDL signaling.
162	22422617	Treatment with LDL promoted activation and translocation of endogenous sphingosine kinase 1 (SK1) from the cytosol to the plasma membrane concomitant with production of sphingosine-1-phosphate (S1P).
163	22422617	Pretreating cells with SK inhibitor, dimethylsphinogsine or down-regulation of SK1 and SK2 revealed that LDL-dependent activation of ERK1/2 and JNK is mediated by SK1.
164	22422617	Pretreating cells with S1P₁/S1P₃ receptor antagonist VPC23019 significantly inhibited activation of ERK1/2 and JNK by LDL, suggesting that LDL elicits G protein-dependent activation of ERK1/2 and JNK by stimulating SK1-dependent transactivation of S1P receptors.
165	22422617	Furthermore, S1P stimulation induced expression of CTGF in a dose-dependent manner that was markedly inhibited by blocking the ERK1/2 and JNK signaling pathways.
166	22422617	Our data suggest that SK1-dependent S1P receptor transactivation is upstream of ERK1/2 and JNK and that all three steps are required for LDL-regulated expression of CTGF in mesangial cells.
167	22422617	In these cells, treatment with pertussis toxin abolished LDL-stimulated activation of ERK1/2 and c-Jun N-terminal kinase (JNK), indicating the involvement of heterotrimeric G proteins in LDL signaling.
168	22422617	Treatment with LDL promoted activation and translocation of endogenous sphingosine kinase 1 (SK1) from the cytosol to the plasma membrane concomitant with production of sphingosine-1-phosphate (S1P).
169	22422617	Pretreating cells with SK inhibitor, dimethylsphinogsine or down-regulation of SK1 and SK2 revealed that LDL-dependent activation of ERK1/2 and JNK is mediated by SK1.
170	22422617	Pretreating cells with S1P₁/S1P₃ receptor antagonist VPC23019 significantly inhibited activation of ERK1/2 and JNK by LDL, suggesting that LDL elicits G protein-dependent activation of ERK1/2 and JNK by stimulating SK1-dependent transactivation of S1P receptors.
171	22422617	Furthermore, S1P stimulation induced expression of CTGF in a dose-dependent manner that was markedly inhibited by blocking the ERK1/2 and JNK signaling pathways.
172	22422617	Our data suggest that SK1-dependent S1P receptor transactivation is upstream of ERK1/2 and JNK and that all three steps are required for LDL-regulated expression of CTGF in mesangial cells.
173	22422617	In these cells, treatment with pertussis toxin abolished LDL-stimulated activation of ERK1/2 and c-Jun N-terminal kinase (JNK), indicating the involvement of heterotrimeric G proteins in LDL signaling.
174	22422617	Treatment with LDL promoted activation and translocation of endogenous sphingosine kinase 1 (SK1) from the cytosol to the plasma membrane concomitant with production of sphingosine-1-phosphate (S1P).
175	22422617	Pretreating cells with SK inhibitor, dimethylsphinogsine or down-regulation of SK1 and SK2 revealed that LDL-dependent activation of ERK1/2 and JNK is mediated by SK1.
176	22422617	Pretreating cells with S1P₁/S1P₃ receptor antagonist VPC23019 significantly inhibited activation of ERK1/2 and JNK by LDL, suggesting that LDL elicits G protein-dependent activation of ERK1/2 and JNK by stimulating SK1-dependent transactivation of S1P receptors.
177	22422617	Furthermore, S1P stimulation induced expression of CTGF in a dose-dependent manner that was markedly inhibited by blocking the ERK1/2 and JNK signaling pathways.
178	22422617	Our data suggest that SK1-dependent S1P receptor transactivation is upstream of ERK1/2 and JNK and that all three steps are required for LDL-regulated expression of CTGF in mesangial cells.
179	22528439	Antibody-based techniques to identify and localize S1P and SphK-1 within cells and tissue specimens represent powerful tools not only to understand the biological role of these molecules but also to validate these unique in-class targets in multiple state diseases.
180	22528439	Here, we describe two staining procedures for identification of S1P and SphK-1 in human frozen tissue samples and the challenges encountered in the process of localization in tissue samples of lipid molecules, such as S1P.
181	22528439	Antibody-based techniques to identify and localize S1P and SphK-1 within cells and tissue specimens represent powerful tools not only to understand the biological role of these molecules but also to validate these unique in-class targets in multiple state diseases.
182	22528439	Here, we describe two staining procedures for identification of S1P and SphK-1 in human frozen tissue samples and the challenges encountered in the process of localization in tissue samples of lipid molecules, such as S1P.
183	23756681	As results, we discovered that 4-deoxypyridoxine (DOP), which inhibits the degradation of intracellular S1P by inhibiting S1P lyase (SPL) activity, minimized the chemically induced apoptosis of insulinoma cell lines as S1P did.
184	23904439	Gene expression arrays in S1P lyase-deficient MCs and MCs treated with S1P continuously revealed increased expression of numerous genes, including the adhesion molecule CNTN4,which contributed to the enhanced responses.