Ignet

Gene Information

Gene symbol: NEU1

Gene name: sialidase 1 (lysosomal sialidase)

HGNC ID: 7758

Related Genes

#	Gene Symbol	Number of hits
1	ADA	1 hits
2	AKT1	1 hits
3	ALPI	1 hits
4	ALPP	1 hits
5	AVP	1 hits
6	B3GALTL	1 hits
7	ELN	1 hits
8	F2RL1	1 hits
9	FUCA1	1 hits
10	GHRH	1 hits
11	GLA	1 hits
12	GRPR	1 hits
13	IDDM2	1 hits
14	IGFBP6	1 hits
15	INS	1 hits
16	INSR	1 hits
17	JTB	1 hits
18	NAGLU	1 hits
19	NEU2	1 hits
20	NEU3	1 hits
21	NEU4	1 hits
22	NMBR	1 hits
23	RET	1 hits
24	UMOD	1 hits

Related Sentences

#	PMID	Sentence
1	698217	Other lectins (wheat germ agglutinin, Dolichos) and enzymes (alpha-L-fucosidase, beta-N-acetyl-hexosaminidase and neuraminidase) are without effect on insulin binding.
2	1100459	When cerebrospinal fluid glucose was lowered by injecting pneumococcal neuraminidase intracisternally, no peripheral hyperinsulinemia resulted, indicating that increased spinal fluid insulin and its consequent increase of glucose uptake, rather than decreased spinal fluid glucose, is necessary to elicit the vagally mediated insulin secretion and hypoglycemia.
3	1424153	We adapted the electrophoretic method of bone alkaline phosphatase (ALP) determination using neuraminidase from Vibrio cholerae to separate bone and liver ALP on cellulose acetate membrane.
4	1424153	Treatment of separator plus serum (1:8, neuraminidase 111 U/l in final) for 10 min at room temperature (25 +/- 1 degree C) and subsequent electrophoresis made it possible to quantify bone ALP activity simply and rapidly.
5	1424153	We adapted the electrophoretic method of bone alkaline phosphatase (ALP) determination using neuraminidase from Vibrio cholerae to separate bone and liver ALP on cellulose acetate membrane.
6	1424153	Treatment of separator plus serum (1:8, neuraminidase 111 U/l in final) for 10 min at room temperature (25 +/- 1 degree C) and subsequent electrophoresis made it possible to quantify bone ALP activity simply and rapidly.
7	1568315	We investigated the prevalence and characteristics of intestinal alkaline phosphatase (ALP; EC 3.1.3.1) identified in human serum by cellulose acetate electrophoresis in 8% of fasting serum samples from hospital patients (n = 500) and in 35% of fasting serum samples from patients with diabetes mellitus (n = 106; not differentiated between types 1 and 2).
8	1568315	Isoelectric focusing of intestinal-ALP-positive serum treated with levamisole and neuraminidase (EC 3.2.1.18) revealed two distinct regions of enzymatic activity that comigrated with ALP extracted from small intestinal and colonic mucosa.
9	1568315	Anodic intestinal ALP was resistant to treatment with levamisole and neuraminidase and comigrated with ALP from small intestinal mucosa.
10	1568315	The more-cathodic intestinal ALP, which comigrated with ALP from colonic mucosa, was completely inhibited by levamisole and converted by neuraminidase to a species with a more basic pI than that of neuraminidase-digested tissue-nonspecific form.
11	1568315	We investigated the prevalence and characteristics of intestinal alkaline phosphatase (ALP; EC 3.1.3.1) identified in human serum by cellulose acetate electrophoresis in 8% of fasting serum samples from hospital patients (n = 500) and in 35% of fasting serum samples from patients with diabetes mellitus (n = 106; not differentiated between types 1 and 2).
12	1568315	Isoelectric focusing of intestinal-ALP-positive serum treated with levamisole and neuraminidase (EC 3.2.1.18) revealed two distinct regions of enzymatic activity that comigrated with ALP extracted from small intestinal and colonic mucosa.
13	1568315	Anodic intestinal ALP was resistant to treatment with levamisole and neuraminidase and comigrated with ALP from small intestinal mucosa.
14	1568315	The more-cathodic intestinal ALP, which comigrated with ALP from colonic mucosa, was completely inhibited by levamisole and converted by neuraminidase to a species with a more basic pI than that of neuraminidase-digested tissue-nonspecific form.
15	1568315	We investigated the prevalence and characteristics of intestinal alkaline phosphatase (ALP; EC 3.1.3.1) identified in human serum by cellulose acetate electrophoresis in 8% of fasting serum samples from hospital patients (n = 500) and in 35% of fasting serum samples from patients with diabetes mellitus (n = 106; not differentiated between types 1 and 2).
16	1568315	Isoelectric focusing of intestinal-ALP-positive serum treated with levamisole and neuraminidase (EC 3.2.1.18) revealed two distinct regions of enzymatic activity that comigrated with ALP extracted from small intestinal and colonic mucosa.
17	1568315	Anodic intestinal ALP was resistant to treatment with levamisole and neuraminidase and comigrated with ALP from small intestinal mucosa.
18	1568315	The more-cathodic intestinal ALP, which comigrated with ALP from colonic mucosa, was completely inhibited by levamisole and converted by neuraminidase to a species with a more basic pI than that of neuraminidase-digested tissue-nonspecific form.
19	1700741	We investigated by enzyme electrophoresis after prolonged neuraminidase treatment the activity of "intestinal variant" (alpha 2-globulin mobility) alkaline phosphatase (EC 3.1.3.1; ALP) in the plasma of 189 patients selected for disorders (diabetes mellitus, liver cirrhosis, and chronic renal failure) with a known high frequency of increased plasma intestinal (beta-globulin mobility) ALP activity.
20	1727740	Furthermore, liver binding data were not due to cross-reaction of 125I-labeled insulin to the insulinlike growth factor I receptor, and treatment of liver membranes with neuraminidase did not alter the inhibitory effect of the IgGa fraction from patient I-2 on 125I-labeled insulin binding to liver.
21	1727740	Binding inhibition experiments performed with cells transfected with and overexpressing the -12 (human insulin receptor [HIR]-A) or the +12 (HIR-B) variant of HIR revealed that the IgGa fraction from patient I-2 inhibited 125I-labeled insulin binding to the HIR-A receptor but not to the HIR-B receptor.
22	2232255	Serum very low molecular weight growth factor like-activity (S-VLMGA, molecular weight less than 3,000) and serum and urinary epidermal growth factor (S-, U-EGF) were investigated in 180 patients of non-insulin-dependent diabetes mellitus (NIDDM) by bioassay using skin fibroblast cells (CCD-27 SK) and enzyme- and radio-immunoassay, respectively.
23	2232255	S-VLMGA was slightly elevated in NIDDM patients with retinopathy (RET) and/or neuropathy (NEU), but slightly decreased in those with nephropathy (NEP) compared with patients without complications, though the differences were not significant (without complications: 122 +/- 9, with RET and/or NEU and without NEP: 145 +/- 15, all with NEP: 110 +/- 8% of increased growth activity, mean +/- SE).
24	2232255	However the changes in S-EGF were small and the decrease of U-EGF in patients with NEP was remarkable (U-EGF of without complications: 22.7 +/- 2.5, with RET and/or NEU and without NEP: 24.5 +/- 4.2, all with NEP: 17.6 +/- 3.2 ng/mg creatinine, mean +/- SE).
25	2232255	Serum very low molecular weight growth factor like-activity (S-VLMGA, molecular weight less than 3,000) and serum and urinary epidermal growth factor (S-, U-EGF) were investigated in 180 patients of non-insulin-dependent diabetes mellitus (NIDDM) by bioassay using skin fibroblast cells (CCD-27 SK) and enzyme- and radio-immunoassay, respectively.
26	2232255	S-VLMGA was slightly elevated in NIDDM patients with retinopathy (RET) and/or neuropathy (NEU), but slightly decreased in those with nephropathy (NEP) compared with patients without complications, though the differences were not significant (without complications: 122 +/- 9, with RET and/or NEU and without NEP: 145 +/- 15, all with NEP: 110 +/- 8% of increased growth activity, mean +/- SE).
27	2232255	However the changes in S-EGF were small and the decrease of U-EGF in patients with NEP was remarkable (U-EGF of without complications: 22.7 +/- 2.5, with RET and/or NEU and without NEP: 24.5 +/- 4.2, all with NEP: 17.6 +/- 3.2 ng/mg creatinine, mean +/- SE).
28	2656166	Human pancreatic tissues were treated with periodate (A), borohydride (B), neuraminidase (C), methanol (D), chloroform-methanol (E), or protease (F) to modify the antigens, and stained by an immunofluorescent method using ICA-positive sera from five Japanese insulin-dependent diabetes mellitus (IDDM) patients.
29	2666202	Neuraminidase treatment of isolated rat adipocytes and differential regulation of basal and insulin-stimulated glucose transport.
30	2666202	The role of membrane carbohydrate in the function of insulin receptors and glucose transporters was investigated with neuraminidase to release sialic acid from isolated rat adipocytes.
31	2666202	The enzyme action on glucose transport was not due to a nonspecific membrane perturbation because neuraminidase caused only a nonsignificant decrease in the uptake of the amino acid analog alpha-(methylamino)isobutyric acid and had no effect on basal or insulin-stimulated protein synthesis.
32	2666202	Insulin binding was slightly increased in neuraminidase-treated cells, yet the shapes of the dose-response curves for insulin stimulation of glucose transport were similar (EC50 = 0.087 +/- 0.010 and 0.082 +/- 0.008 nM for control and treated cells, respectively).
33	2666202	Neuraminidase treatment of isolated rat adipocytes and differential regulation of basal and insulin-stimulated glucose transport.
34	2666202	The role of membrane carbohydrate in the function of insulin receptors and glucose transporters was investigated with neuraminidase to release sialic acid from isolated rat adipocytes.
35	2666202	The enzyme action on glucose transport was not due to a nonspecific membrane perturbation because neuraminidase caused only a nonsignificant decrease in the uptake of the amino acid analog alpha-(methylamino)isobutyric acid and had no effect on basal or insulin-stimulated protein synthesis.
36	2666202	Insulin binding was slightly increased in neuraminidase-treated cells, yet the shapes of the dose-response curves for insulin stimulation of glucose transport were similar (EC50 = 0.087 +/- 0.010 and 0.082 +/- 0.008 nM for control and treated cells, respectively).
37	2666202	Neuraminidase treatment of isolated rat adipocytes and differential regulation of basal and insulin-stimulated glucose transport.
38	2666202	The role of membrane carbohydrate in the function of insulin receptors and glucose transporters was investigated with neuraminidase to release sialic acid from isolated rat adipocytes.
39	2666202	The enzyme action on glucose transport was not due to a nonspecific membrane perturbation because neuraminidase caused only a nonsignificant decrease in the uptake of the amino acid analog alpha-(methylamino)isobutyric acid and had no effect on basal or insulin-stimulated protein synthesis.
40	2666202	Insulin binding was slightly increased in neuraminidase-treated cells, yet the shapes of the dose-response curves for insulin stimulation of glucose transport were similar (EC50 = 0.087 +/- 0.010 and 0.082 +/- 0.008 nM for control and treated cells, respectively).
41	2666202	Neuraminidase treatment of isolated rat adipocytes and differential regulation of basal and insulin-stimulated glucose transport.
42	2666202	The role of membrane carbohydrate in the function of insulin receptors and glucose transporters was investigated with neuraminidase to release sialic acid from isolated rat adipocytes.
43	2666202	The enzyme action on glucose transport was not due to a nonspecific membrane perturbation because neuraminidase caused only a nonsignificant decrease in the uptake of the amino acid analog alpha-(methylamino)isobutyric acid and had no effect on basal or insulin-stimulated protein synthesis.
44	2666202	Insulin binding was slightly increased in neuraminidase-treated cells, yet the shapes of the dose-response curves for insulin stimulation of glucose transport were similar (EC50 = 0.087 +/- 0.010 and 0.082 +/- 0.008 nM for control and treated cells, respectively).
45	3070044	Five mutated genes on chromosome 20 have a relation to disease: a mutation in the adenosine deaminase gene results in a deficiency of the enzyme and severe combined immune deficiency; mutations in the gene for the growth hormone releasing factor result in some forms of dwarfism; mutations in the closely linked genes for the hormones arginine vasopressin and oxytocin and their neurophysins are probably responsible for some diabetes insipidus; and mutations in the gene that regulates both alpha-neuraminidase and beta-galactosidase activities determine galactosialidosis.
46	3070044	Two genes that code for tyrosine kinases are on the chromosome, SRC1 the proto-oncogene and a gene (HCK) coding for haemopoietic kinase (an src-like kinase), but no direct relation to cancer has been shown for either of these kinases.
47	3070044	Twenty-four additional loci are assigned to the chromosome: five genes that code for binding proteins, one for a light chain of ferritin, genes for three enzymes (inosine triphosphatase, s-adenosylhomocysteine hydrolase, and sterol delta 24-reductase), one for each of a secretory protein and an opiate neuropeptide, a cell surface antigen, two fragile sites, and 10 DNA sequences (one satellite and nine unique) that detect RFLPs.
48	3130265	Adhesion of bacteria (without additions: 100 bacteria per cell) was reduced dose-dependently by THP, half maximal inhibition occurring with 250 micrograms THP ml-1.
49	3130265	Maximal inhibition (-84% at 1000 micrograms ml-1) exceeded inhibition by alpha-methyl-mannoside (36% at 50 mM), was specific (not reproduced by other glycoproteins, e.g. ovalbumin, mucin or thyroglobulin) and reversible (abolished by washing THP off HUK cells).
50	3130265	Anti-adherence property of THP was not abolished by neuraminidase treatment.
51	3407769	Adipocytes treated with neuraminidase show markedly reduced responsiveness to insulin without any alteration in insulin binding.
52	3407769	Primary cultures of hepatocytes from normal rats treated with neuraminidase demonstrated a dose-dependent decrease in insulin-stimulated lipogenesis.
53	3407769	At a concentration of neuraminidase that decreases insulin action by 50%, 23% of total cellular sialic acid content was released.
54	3407769	Neuraminidase-releasable sialic acid was significantly decreased in hepatocytes from diabetic rats and this was associated with significant insulin resistance.
55	3407769	Adipocytes treated with neuraminidase show markedly reduced responsiveness to insulin without any alteration in insulin binding.
56	3407769	Primary cultures of hepatocytes from normal rats treated with neuraminidase demonstrated a dose-dependent decrease in insulin-stimulated lipogenesis.
57	3407769	At a concentration of neuraminidase that decreases insulin action by 50%, 23% of total cellular sialic acid content was released.
58	3407769	Neuraminidase-releasable sialic acid was significantly decreased in hepatocytes from diabetic rats and this was associated with significant insulin resistance.
59	3407769	Adipocytes treated with neuraminidase show markedly reduced responsiveness to insulin without any alteration in insulin binding.
60	3407769	Primary cultures of hepatocytes from normal rats treated with neuraminidase demonstrated a dose-dependent decrease in insulin-stimulated lipogenesis.
61	3407769	At a concentration of neuraminidase that decreases insulin action by 50%, 23% of total cellular sialic acid content was released.
62	3407769	Neuraminidase-releasable sialic acid was significantly decreased in hepatocytes from diabetic rats and this was associated with significant insulin resistance.
63	3407769	Adipocytes treated with neuraminidase show markedly reduced responsiveness to insulin without any alteration in insulin binding.
64	3407769	Primary cultures of hepatocytes from normal rats treated with neuraminidase demonstrated a dose-dependent decrease in insulin-stimulated lipogenesis.
65	3407769	At a concentration of neuraminidase that decreases insulin action by 50%, 23% of total cellular sialic acid content was released.
66	3407769	Neuraminidase-releasable sialic acid was significantly decreased in hepatocytes from diabetic rats and this was associated with significant insulin resistance.
67	4461551	Proceedings: Neuraminidase activity of the pancreas and insulin secretion.
68	7689963	Rat PC12 pheochromocytoma cells synthesize insulin-like growth factor-binding protein-6.
69	7689963	Insulin-like growth factor-I (IGF-I) and IGF-II are mitogenic for PC12 cells under serum-starved conditions.
70	7689963	It recently was reported that PC12 cells produced an IGFBP that had a marked preferential binding affinity for IGF-II over IGF-I.
71	7689963	Rat IGFBP-6, like human IGFBP-6, is O-glycosylated; incubation with neuraminidase, fucosidase, and O-glycanase reduced its apparent molecular mass to 21 kilodaltons.
72	7689963	Competitive binding studies of rat and human IGFBP-6 with [125I]IGF-II and unlabeled IGF-II or IGF-I demonstrated that both IGFBPs bound IGF-II with similar affinities (Ka, 1.5-1.8 x 10(11) M-1) and bound IGF-I with approximately 25- to 35-fold lower affinity than IGF-II.
73	7947701	In the present study, we investigated the nature and the importance of glycosylation of two mammalian bombesin receptors, the neuromedin B receptor (NMB-R) and the gastrin-releasing peptide receptor (GRP-R), using chemical cross-linking and enzymatic deglycosylation. [125I]-(D-Tyr0)NMB cross-linked to native NMB-R on rat C-6 glioblastoma cells or rat NMB-R transfected into BALB 3T3 cells revealed a single broad band, M(r) = 63,000, on both cell types that was not altered by DTT.
74	7947701	NMB inhibited cross-linking specifically and saturably with an IC50 of 4.8 and 6.1 nM for C-6 and NMB-R transfected cells, respectively, and there was a close correlation between its ability to inhibit binding and its ability to inhibit cross-linking.
75	7947701	A single broad band of M(r) = 82,000 was cross-linked with [125I]GRP on mouse GRP-R transfected BALB 3T3 cells.
76	7947701	Peptide-N4-(N-acetyl-beta- glucosaminyl)asparagine amidase F (PNGase F) digestion increased the mobility of the original band in C-6, NMB-R, and GRP-R transfected cell membranes.
77	7947701	Neuraminidase digestion slightly increased the mobility of the original band in NMB-R transfected cell membranes; however, it had no effect on GRP-R transfected cell membranes.
78	7947701	Endo-alpha-N-acetylglucosaminidase (O-glycanase) digestion subsequent to neuraminidase treatment showed no additional effect on either receptor.
79	7947701	Treatment of unlabeled membranes with PNGase F followed by affinity labeling resulted in fully deglycosylated NMB-R or 75% deglycosylated GRP-R.
80	7947701	Deglycosylation of the NMB-R did not alter its affinity for NMB or alter G-protein coupling; however, 75% deglycosylation of the GRP-R both decreased its affinity for GRP and altered its ability to couple to G-proteins.
81	7947701	In the present study, we investigated the nature and the importance of glycosylation of two mammalian bombesin receptors, the neuromedin B receptor (NMB-R) and the gastrin-releasing peptide receptor (GRP-R), using chemical cross-linking and enzymatic deglycosylation. [125I]-(D-Tyr0)NMB cross-linked to native NMB-R on rat C-6 glioblastoma cells or rat NMB-R transfected into BALB 3T3 cells revealed a single broad band, M(r) = 63,000, on both cell types that was not altered by DTT.
82	7947701	NMB inhibited cross-linking specifically and saturably with an IC50 of 4.8 and 6.1 nM for C-6 and NMB-R transfected cells, respectively, and there was a close correlation between its ability to inhibit binding and its ability to inhibit cross-linking.
83	7947701	A single broad band of M(r) = 82,000 was cross-linked with [125I]GRP on mouse GRP-R transfected BALB 3T3 cells.
84	7947701	Peptide-N4-(N-acetyl-beta- glucosaminyl)asparagine amidase F (PNGase F) digestion increased the mobility of the original band in C-6, NMB-R, and GRP-R transfected cell membranes.
85	7947701	Neuraminidase digestion slightly increased the mobility of the original band in NMB-R transfected cell membranes; however, it had no effect on GRP-R transfected cell membranes.
86	7947701	Endo-alpha-N-acetylglucosaminidase (O-glycanase) digestion subsequent to neuraminidase treatment showed no additional effect on either receptor.
87	7947701	Treatment of unlabeled membranes with PNGase F followed by affinity labeling resulted in fully deglycosylated NMB-R or 75% deglycosylated GRP-R.
88	7947701	Deglycosylation of the NMB-R did not alter its affinity for NMB or alter G-protein coupling; however, 75% deglycosylation of the GRP-R both decreased its affinity for GRP and altered its ability to couple to G-proteins.
89	8046546	This paper is a study to identify the clinical significance of high-molecular-mass alkaline phosphatase (ALP:E:C..3.1.3.1.), ALP-lipoprotein-X complex (LP-X) and intestinal variant ALP.
90	8046546	We used cellulose acetate and agarose gels and techniques including wheat germ lectin, cetavlon-diethyl ether, thermostatability, neuraminidase and L-phenylalanine to improve the electrophoretic separation of the alkaline phosphatase isoenzymes.
91	8046546	Intestinal variant ALP is most likely composed of intestinal ALP attached to a cellular membrane-binding domain, or may be an artifact produced by neuraminidase incubation.
92	8046546	This paper is a study to identify the clinical significance of high-molecular-mass alkaline phosphatase (ALP:E:C..3.1.3.1.), ALP-lipoprotein-X complex (LP-X) and intestinal variant ALP.
93	8046546	We used cellulose acetate and agarose gels and techniques including wheat germ lectin, cetavlon-diethyl ether, thermostatability, neuraminidase and L-phenylalanine to improve the electrophoretic separation of the alkaline phosphatase isoenzymes.
94	8046546	Intestinal variant ALP is most likely composed of intestinal ALP attached to a cellular membrane-binding domain, or may be an artifact produced by neuraminidase incubation.
95	10353622	In contrast, in BREC, AGEs increased beta-D galactosidase, alpha-L fucosidase and neuraminidase activities (+37%, +56%, 36% respectively) whereas galactosyltransferase, fucosyltransferase and sialyltransferase activities were decreased (-11%, -24% and -23% respectively).
96	10353622	In the retina from diabetic rats, beta-D galactosidase, alpha-L fucosidase and neuraminidase activities increased (+70%, +57%, +78% respectively) whereas fucosyl and sialyltransferase decreased (-7% and -15% respectively).
97	10353622	In contrast, in BREC, AGEs increased beta-D galactosidase, alpha-L fucosidase and neuraminidase activities (+37%, +56%, 36% respectively) whereas galactosyltransferase, fucosyltransferase and sialyltransferase activities were decreased (-11%, -24% and -23% respectively).
98	10353622	In the retina from diabetic rats, beta-D galactosidase, alpha-L fucosidase and neuraminidase activities increased (+70%, +57%, +78% respectively) whereas fucosyl and sialyltransferase decreased (-7% and -15% respectively).
99	11606310	We found tryptase to be an inefficient activator of wild-type rat-PAR(2) (wt-rPAR(2)) and therefore decided to explore the factors that may influence tryptase activation of PAR(2). 2.
100	11606310	However, in the presence of either human-PAR(2) or wt-r PAR(2) expressing cells, tryptase could only activate PAR(2) by releasing SLIGRL from the P20 peptide, suggesting that PAR(2) expressed on the cells was protected from tryptase activation. 3.
101	11606310	Three approaches were employed to test the hypothesis that PAR(2) receptor glycosylation restricts tryptase activation.
102	11606310	(a) pretreatment of wt-rPAR(2) expressing cells or human embryonic kidney cells (HEK293) with vibrio cholerae neuraminidase to remove oligosaccharide sialic acid, unmasked tryptase-mediated PAR(2) activation.
103	11606310	(b) Inhibiting receptor glycosylation in HEK293 cells with tunicamycin enabled tryptase-mediated PAR(2) activation.
104	11606310	Immunocytochemistry using antisera that specifically recognized the N-terminal precleavage sequence of PAR(2) demonstrated that tryptase released the precleavage domain from PAR(2)T25(-) but not from wt-rPAR(2). 5.
105	11606310	Our results indicate that glycosylation of PAR(2) and heparin-inhibition of PAR(2) activation by tryptase could provide novel mechanisms for regulating receptor activation by tryptase and possibly other proteases.
106	19450982	Recent advances in the sialidase biology have clarified the role of human sialidases (NEU 1 to NEU4) in the development of various disease states such as cancer, diabetes and arteriosclerosis.
107	23520133	Positive regulation of insulin signaling by neuraminidase 1.
108	23520133	We now report that mammalian neuraminidase 1 (Neu1), in addition to its catabolic function in lysosomes, is transported to the cell surface where it is involved in the regulation of insulin signaling.
109	23520133	Insulin binding to its receptor rapidly induces interaction of the receptor with Neu1, which hydrolyzes sialic acid residues in the glycan chains of the receptor and, consequently, induces its activation.
110	23520133	Cells from sialidosis patients with a genetic deficiency of Neu1 show impairment of insulin-induced phosphorylation of downstream protein kinase AKT, and treatment of these cells with purified Neu1 restores signaling.
111	23520133	Genetically modified mice with ∼10% of the normal Neu1 activity exposed to a high-fat diet develop hyperglycemia and insulin resistance twice as fast as their wild-type counterparts.
112	23520133	Positive regulation of insulin signaling by neuraminidase 1.
113	23520133	We now report that mammalian neuraminidase 1 (Neu1), in addition to its catabolic function in lysosomes, is transported to the cell surface where it is involved in the regulation of insulin signaling.
114	23520133	Insulin binding to its receptor rapidly induces interaction of the receptor with Neu1, which hydrolyzes sialic acid residues in the glycan chains of the receptor and, consequently, induces its activation.
115	23520133	Cells from sialidosis patients with a genetic deficiency of Neu1 show impairment of insulin-induced phosphorylation of downstream protein kinase AKT, and treatment of these cells with purified Neu1 restores signaling.
116	23520133	Genetically modified mice with ∼10% of the normal Neu1 activity exposed to a high-fat diet develop hyperglycemia and insulin resistance twice as fast as their wild-type counterparts.
117	23520133	Positive regulation of insulin signaling by neuraminidase 1.
118	23520133	We now report that mammalian neuraminidase 1 (Neu1), in addition to its catabolic function in lysosomes, is transported to the cell surface where it is involved in the regulation of insulin signaling.
119	23520133	Insulin binding to its receptor rapidly induces interaction of the receptor with Neu1, which hydrolyzes sialic acid residues in the glycan chains of the receptor and, consequently, induces its activation.
120	23520133	Cells from sialidosis patients with a genetic deficiency of Neu1 show impairment of insulin-induced phosphorylation of downstream protein kinase AKT, and treatment of these cells with purified Neu1 restores signaling.
121	23520133	Genetically modified mice with ∼10% of the normal Neu1 activity exposed to a high-fat diet develop hyperglycemia and insulin resistance twice as fast as their wild-type counterparts.
122	23520133	Positive regulation of insulin signaling by neuraminidase 1.
123	23520133	We now report that mammalian neuraminidase 1 (Neu1), in addition to its catabolic function in lysosomes, is transported to the cell surface where it is involved in the regulation of insulin signaling.
124	23520133	Insulin binding to its receptor rapidly induces interaction of the receptor with Neu1, which hydrolyzes sialic acid residues in the glycan chains of the receptor and, consequently, induces its activation.
125	23520133	Cells from sialidosis patients with a genetic deficiency of Neu1 show impairment of insulin-induced phosphorylation of downstream protein kinase AKT, and treatment of these cells with purified Neu1 restores signaling.
126	23520133	Genetically modified mice with ∼10% of the normal Neu1 activity exposed to a high-fat diet develop hyperglycemia and insulin resistance twice as fast as their wild-type counterparts.
127	23520133	Positive regulation of insulin signaling by neuraminidase 1.
128	23520133	We now report that mammalian neuraminidase 1 (Neu1), in addition to its catabolic function in lysosomes, is transported to the cell surface where it is involved in the regulation of insulin signaling.
129	23520133	Insulin binding to its receptor rapidly induces interaction of the receptor with Neu1, which hydrolyzes sialic acid residues in the glycan chains of the receptor and, consequently, induces its activation.
130	23520133	Cells from sialidosis patients with a genetic deficiency of Neu1 show impairment of insulin-induced phosphorylation of downstream protein kinase AKT, and treatment of these cells with purified Neu1 restores signaling.
131	23520133	Genetically modified mice with ∼10% of the normal Neu1 activity exposed to a high-fat diet develop hyperglycemia and insulin resistance twice as fast as their wild-type counterparts.
132	23727924	Mammalian sialidases (NEU1, NEU2, NEU3 and NEU4) that remove sialic acids from glycoconjugates have been implicated in diverse cellular functions.
133	23919962	Elastin-derived peptides are new regulators of insulin resistance development in mice.
134	23919962	In the current study, we show that elastin-derived peptides (EDPs) may be involved in the development of insulin resistance (IRES) in mice.
135	23919962	Based on in vivo, in vitro, and in silico approaches, we propose that this IRES is due to interaction between the insulin receptor (IR) and the neuraminidase-1 subunit of the elastin receptor complex triggered by EDPs.