Ignet

Gene Information

Gene symbol: RAB3C

Gene name: RAB3C, member RAS oncogene family

HGNC ID: 30269

Related Genes

#	Gene Symbol	Number of hits
1	INS	1 hits
2	RAB3B	1 hits
3	RAB4A	1 hits
4	SLC2A1	1 hits
5	SLC2A4	1 hits

Related Sentences

#	PMID	Sentence
1	8543030	Insulin-dependent translocation of the small GTP-binding protein rab3C in cardiac muscle: studies on insulin-resistant Zucker rats.
2	8543030	The failure of insulin-regulated recruitment of the GLUT4 glucose transporter in cardiac muscle of obese Zucker rats is associated with alterations of the subcellular distribution of the small-molecular-mass GTP-binding protein rab4A.
3	8543030	Here, we show by subcellular fractionation and Western blotting a translocation of the small-molecular-mass GTP-binding protein rab3C from microsomal membranes to plasma membranes in lean control rats following in vivo insulin stimulation.
4	8543030	In GLUT4-enriched membrane vesicles, obtained from cardiac microsomes of the obese group as well as of lean controls, rab3C was not detectable.
5	8543030	It is suggested that the altered behaviour of rab3C may contribute to an impaired trafficking of GLUT4 in the insulin-resistant state.
6	8543030	Insulin-dependent translocation of the small GTP-binding protein rab3C in cardiac muscle: studies on insulin-resistant Zucker rats.
7	8543030	The failure of insulin-regulated recruitment of the GLUT4 glucose transporter in cardiac muscle of obese Zucker rats is associated with alterations of the subcellular distribution of the small-molecular-mass GTP-binding protein rab4A.
8	8543030	Here, we show by subcellular fractionation and Western blotting a translocation of the small-molecular-mass GTP-binding protein rab3C from microsomal membranes to plasma membranes in lean control rats following in vivo insulin stimulation.
9	8543030	In GLUT4-enriched membrane vesicles, obtained from cardiac microsomes of the obese group as well as of lean controls, rab3C was not detectable.
10	8543030	It is suggested that the altered behaviour of rab3C may contribute to an impaired trafficking of GLUT4 in the insulin-resistant state.
11	8543030	Insulin-dependent translocation of the small GTP-binding protein rab3C in cardiac muscle: studies on insulin-resistant Zucker rats.
12	8543030	The failure of insulin-regulated recruitment of the GLUT4 glucose transporter in cardiac muscle of obese Zucker rats is associated with alterations of the subcellular distribution of the small-molecular-mass GTP-binding protein rab4A.
13	8543030	Here, we show by subcellular fractionation and Western blotting a translocation of the small-molecular-mass GTP-binding protein rab3C from microsomal membranes to plasma membranes in lean control rats following in vivo insulin stimulation.
14	8543030	In GLUT4-enriched membrane vesicles, obtained from cardiac microsomes of the obese group as well as of lean controls, rab3C was not detectable.
15	8543030	It is suggested that the altered behaviour of rab3C may contribute to an impaired trafficking of GLUT4 in the insulin-resistant state.
16	8543030	Insulin-dependent translocation of the small GTP-binding protein rab3C in cardiac muscle: studies on insulin-resistant Zucker rats.
17	8543030	The failure of insulin-regulated recruitment of the GLUT4 glucose transporter in cardiac muscle of obese Zucker rats is associated with alterations of the subcellular distribution of the small-molecular-mass GTP-binding protein rab4A.
18	8543030	Here, we show by subcellular fractionation and Western blotting a translocation of the small-molecular-mass GTP-binding protein rab3C from microsomal membranes to plasma membranes in lean control rats following in vivo insulin stimulation.
19	8543030	In GLUT4-enriched membrane vesicles, obtained from cardiac microsomes of the obese group as well as of lean controls, rab3C was not detectable.
20	8543030	It is suggested that the altered behaviour of rab3C may contribute to an impaired trafficking of GLUT4 in the insulin-resistant state.
21	8886977	Rab3B and Rab3C were identified by western blotting in rat and in human pancreatic islets, in two rat insulin-secreting cell lines, RINm5F and INS-1, as well as in the hamster cell line HIT-T15.
22	8886977	In contrast, Rab3A was detected in rat pancreatic islets as well as in the two insulin-secreting rat cell lines but not in human pancreatic islets and was only barely discernible in HIT-T15 cells.
23	8886977	Northern blotting analysis revealed that Rab3D is expressed in the same insulin-secreting cells as Rab3A.
24	8886977	Rab3A was found to be associated with insulin-containing secretory granules both by immunofluorescence, immunoelectron microscopy and after sucrose density gradient.
25	8886977	Overexpression in HIT-T15 cells of a Rab3A mutant deficient in GTP hydrolysis inhibited insulin secretion stimulated by a mixture of nutrients and bombesin.
26	8886977	Insulin release triggered by these secretagogues was also slightly decreased by the overexpression of wild-type Rab3A but not by the overexpression of wild-type Rab5A and of a Rab5A mutant deficient in GTP hydrolysis.
27	8886977	Finally, we studied the expression in insulin-secreting cells of rabphilin-3A, a putative effector protein that associates with the GTP-bound form of Rab3A.
28	8886977	Taken together these results indicate an involvement of Rab3A in the control of insulin release in rat and hamster.
29	10768829	Regulation of subcellular distribution of GLUT4 in cardiomyocytes: Rab4A reduces basal glucose transport and augments insulin responsiveness.
30	10768829	Members of the Rab subfamily of small-GTP binding proteins have been suggested to be involved in insulin-regulated translocation of the glucose transporter GLUT4.
31	10768829	To directly study this process in muscle tissue, we have established an insulin-sensitive cardiac cell line (H9K6) stably overexpressing GLUT4, which was derived from H9c2 cardiac myoblasts.
32	10768829	H9K6-cells were transiently transfected with rab4A and rab3C with an efficiency of 65% and glucose uptake and the cellular distribution and expression of the transporter isoforms GLUT1 and GLUT4 was subsequently determined.
33	10768829	Rab3C-overexpression caused no significant change in both basal and insulin-stimulated 2-deoxyglucose uptake compared to control cells transfected with the blank vector.
34	10768829	Total expression of GLUT1 and GLUT4 was not affected by Rab4-overexpression.
35	10768829	Cell surface biotinylation was used to quantify the abundance of GLUT1 and GLUT4 in the plasma membrane.
36	10768829	A decrease of cell surface GLUT4 by about 40% compared to control cells was found in Rab4-overexpressing cells Insulin treatment increased cell surface-GLUT4 by 100% compared to only 26% in control cells.
37	10768829	Our data show that Rab4A but not Rab3C is able to reduce basal glucose uptake and cell surface content of GLUT4 in cardiac muscle cells.
38	10768829	This results in an increased stimulation of glucose uptake by insulin which can be fully explained by enhanced translocation of GLUT4.
39	10768829	We suggest that Rab4A participates in the redistribution of GLUT4 to intracellular pools and represents an essential determinant of the insulin responsiveness of GLUT4 translocation in cardiac muscle cells.
40	10768829	Regulation of subcellular distribution of GLUT4 in cardiomyocytes: Rab4A reduces basal glucose transport and augments insulin responsiveness.
41	10768829	Members of the Rab subfamily of small-GTP binding proteins have been suggested to be involved in insulin-regulated translocation of the glucose transporter GLUT4.
42	10768829	To directly study this process in muscle tissue, we have established an insulin-sensitive cardiac cell line (H9K6) stably overexpressing GLUT4, which was derived from H9c2 cardiac myoblasts.
43	10768829	H9K6-cells were transiently transfected with rab4A and rab3C with an efficiency of 65% and glucose uptake and the cellular distribution and expression of the transporter isoforms GLUT1 and GLUT4 was subsequently determined.
44	10768829	Rab3C-overexpression caused no significant change in both basal and insulin-stimulated 2-deoxyglucose uptake compared to control cells transfected with the blank vector.
45	10768829	Total expression of GLUT1 and GLUT4 was not affected by Rab4-overexpression.
46	10768829	Cell surface biotinylation was used to quantify the abundance of GLUT1 and GLUT4 in the plasma membrane.
47	10768829	A decrease of cell surface GLUT4 by about 40% compared to control cells was found in Rab4-overexpressing cells Insulin treatment increased cell surface-GLUT4 by 100% compared to only 26% in control cells.
48	10768829	Our data show that Rab4A but not Rab3C is able to reduce basal glucose uptake and cell surface content of GLUT4 in cardiac muscle cells.
49	10768829	This results in an increased stimulation of glucose uptake by insulin which can be fully explained by enhanced translocation of GLUT4.
50	10768829	We suggest that Rab4A participates in the redistribution of GLUT4 to intracellular pools and represents an essential determinant of the insulin responsiveness of GLUT4 translocation in cardiac muscle cells.
51	10768829	Regulation of subcellular distribution of GLUT4 in cardiomyocytes: Rab4A reduces basal glucose transport and augments insulin responsiveness.
52	10768829	Members of the Rab subfamily of small-GTP binding proteins have been suggested to be involved in insulin-regulated translocation of the glucose transporter GLUT4.
53	10768829	To directly study this process in muscle tissue, we have established an insulin-sensitive cardiac cell line (H9K6) stably overexpressing GLUT4, which was derived from H9c2 cardiac myoblasts.
54	10768829	H9K6-cells were transiently transfected with rab4A and rab3C with an efficiency of 65% and glucose uptake and the cellular distribution and expression of the transporter isoforms GLUT1 and GLUT4 was subsequently determined.
55	10768829	Rab3C-overexpression caused no significant change in both basal and insulin-stimulated 2-deoxyglucose uptake compared to control cells transfected with the blank vector.
56	10768829	Total expression of GLUT1 and GLUT4 was not affected by Rab4-overexpression.
57	10768829	Cell surface biotinylation was used to quantify the abundance of GLUT1 and GLUT4 in the plasma membrane.
58	10768829	A decrease of cell surface GLUT4 by about 40% compared to control cells was found in Rab4-overexpressing cells Insulin treatment increased cell surface-GLUT4 by 100% compared to only 26% in control cells.
59	10768829	Our data show that Rab4A but not Rab3C is able to reduce basal glucose uptake and cell surface content of GLUT4 in cardiac muscle cells.
60	10768829	This results in an increased stimulation of glucose uptake by insulin which can be fully explained by enhanced translocation of GLUT4.
61	10768829	We suggest that Rab4A participates in the redistribution of GLUT4 to intracellular pools and represents an essential determinant of the insulin responsiveness of GLUT4 translocation in cardiac muscle cells.