PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25281698-3 2015 In patients with IgAN, alpha2,6-sialylated GalNAc is a frequent form of the galactose-deficient O-glycans. N-acetylgalactosaminuronic acid 43-49 IGAN1 Homo sapiens 17-21 18046671-9 2007 Compared with controls, serum IgA1 from IgAN patients showed significantly greater binding to the 2 lectins, jacalin (p<0.01) and Helix aspersa (HA, p<0.001), which are specific for O-linked Gal-beta1,3-GalNAc and GalNAc, respectively. N-acetylgalactosaminuronic acid 209-215 IGAN1 Homo sapiens 40-44 24918438-1 2014 Patients with IgA nephropathy (IgAN) have elevated circulating levels of IgA1 with some O-glycans consisting of galactose (Gal)-deficient N-acetylgalactosamine (GalNAc) with or without N-acetylneuraminic acid (NeuAc). N-acetylgalactosaminuronic acid 161-167 IGAN1 Homo sapiens 31-35 24918438-4 2014 As IgA1-producing cells from IgAN patients have an increased activity of alpha2,6-sialyltransferase (ST6GalNAc), we hypothesize that such activity may promote premature sialylation of GalNAc and, thus, production of Gd-IgA1, as sialylation of GalNAc prevents subsequent Gal attachment. N-acetylgalactosaminuronic acid 104-110 IGAN1 Homo sapiens 29-33 24918438-4 2014 As IgA1-producing cells from IgAN patients have an increased activity of alpha2,6-sialyltransferase (ST6GalNAc), we hypothesize that such activity may promote premature sialylation of GalNAc and, thus, production of Gd-IgA1, as sialylation of GalNAc prevents subsequent Gal attachment. N-acetylgalactosaminuronic acid 184-190 IGAN1 Homo sapiens 29-33 23398317-6 2013 A significant increase in N-acetylgalactosamine (GalNAc) in terminal position (p = 0.02) observed in some of the IgAN patients, became more pronounced when sialic acid was removed from IgA1, indicating enhanced expression of alpha-2,6-sialyltransferase in patients compared with controls (p < 0.0001). N-acetylgalactosaminuronic acid 49-55 IGAN1 Homo sapiens 113-117 23398317-8 2013 IgAN patients with both IgA1 and IgA2 glomerular deposits (21.7%) had increased GalNAc in terminal position (p = 0.003). N-acetylgalactosaminuronic acid 80-86 IGAN1 Homo sapiens 0-4 23098908-3 2012 In the present study, the molar ratios of GalNAc or Gal to HP were analyzed for serum IgA from IgAN patients. N-acetylgalactosaminuronic acid 42-48 IGAN1 Homo sapiens 95-99 24918438-7 2014 Sialylation of Gal-deficient asialo-IgA1 (Ale) myeloma protein by an ST6GalNAc enzyme generated sialylated IgA1 that mimics the Gal-deficient IgA1 glycoforms in patients with IgAN, characterized by alpha2,6-sialylated Gal-deficient GalNAc. N-acetylgalactosaminuronic acid 72-78 IGAN1 Homo sapiens 175-179 24131475-2 2014 N-acetylgalactosamine (GalNAc) exposure plays a pivotal role in the pathogenesis of IgAN. N-acetylgalactosaminuronic acid 23-29 IGAN1 Homo sapiens 84-88 24131475-3 2014 The aim of the current study is to investigate whether GalNAc exposure of serum IgA1 was associated with clinical and pathological manifestation of IgAN. N-acetylgalactosaminuronic acid 55-61 IGAN1 Homo sapiens 148-152 23098908-4 2012 The GalNAc/HP ratio was increased in the patients who achieved remission after a combination therapy of tonsillectomy and intravenous corticosteroid, suggesting any non-innate factors to affect the IgA O-glycosylation in IgAN that is thought to be inherently determined. N-acetylgalactosaminuronic acid 4-10 IGAN1 Homo sapiens 221-225 15954905-14 2005 The exposure of GalNAc of serum IgA1 from patients with focal proliferative and sclerosing IgAN was significantly higher than that of controls (P= 0.017), but had no statistical difference with that of patients with mild mesangial proliferative IgAN. N-acetylgalactosaminuronic acid 16-22 IGAN1 Homo sapiens 91-95 17495450-7 2007 IgG from IgAN patients exhibited strong reactivity with HR-GalNAc-BSA, but not with HR-BSA. N-acetylgalactosaminuronic acid 59-65 IGAN1 Homo sapiens 9-13 17050773-8 2006 Both in patients with IgAN and in control subjects, IgA binding to the GalNAc-specific lectin Helix Aspersa and to mannose-binding lectin was much stronger for pIgA than for mIgA. N-acetylgalactosaminuronic acid 71-77 IGAN1 Homo sapiens 22-26 15954905-14 2005 The exposure of GalNAc of serum IgA1 from patients with focal proliferative and sclerosing IgAN was significantly higher than that of controls (P= 0.017), but had no statistical difference with that of patients with mild mesangial proliferative IgAN. N-acetylgalactosaminuronic acid 16-22 IGAN1 Homo sapiens 245-249 11518779-8 2001 Patients with IgAN displayed increased levels of IgA glycoforms exposing sialic acid in alpha2,6 linkage with N-acetylgalactosamine (Neu5Acalpha2,6GalNAc) (P < 0.02) and GalNAc (P < 0.05), indicating truncation of O-linked glycans of IgA1. N-acetylgalactosaminuronic acid 147-153 IGAN1 Homo sapiens 14-18 15086888-1 2004 Immunoglobulin A nephropathy (IgAN) patients exhibit circulating IgA1 with reduced galactose (Gal) and/or sialic acid (Neu5Ac) and increased exposure of N-acetylgalactosamine (GalNAc). N-acetylgalactosaminuronic acid 176-182 IGAN1 Homo sapiens 30-34 11518779-13 2001 In conclusion, a significant modulation of several human MC functions exerted by serum IgA with increased exposure of GalNAc, Neu5Acalpha2,6GalNAc, and mannose residues isolated from IgAN patients is reported for the first time. N-acetylgalactosaminuronic acid 118-124 IGAN1 Homo sapiens 183-187 10777713-5 2000 The results obtained clearly showed a decrease of GalNAc, Gal, and sialic acid in IgAN compared with non-IgAN and normal controls, and those strongly suggested the possibility that the decreased galactosylation and sialylation of the IgA1 hinge result in its glomerular deposition in IgAN. N-acetylgalactosaminuronic acid 50-56 IGAN1 Homo sapiens 82-86 11115067-7 2000 Serum IgA glycoforms isolated from IgAN patients with high exposure of internal sugars, GalNAc, Neu5Ac2,6GalNAc, and Man enhanced alphav expression on cultured MCs more than healthy controls. N-acetylgalactosaminuronic acid 88-94 IGAN1 Homo sapiens 35-39 10446944-7 1999 In some patients with IgAN, FACE analysis demonstrated a significant increase in the percentage of IgA1 O-glycan chains consisting of single N-acetyl galactosamine (GalNAc) units rather than the more usual galactosylated and sialylated forms. N-acetylgalactosaminuronic acid 165-171 IGAN1 Homo sapiens 22-26 10446944-10 1999 This is the first study in which all of the predicted O-glycan forms of IgA1 have been analyzed simultaneously, and demonstrates that in IgAN, the IgA1 Oglycan chains are truncated, with increased terminal GalNAc. N-acetylgalactosaminuronic acid 206-212 IGAN1 Homo sapiens 137-141 10393701-1 1999 Circulating immune complexes (CICs) isolated from sera of patients with IgA nephropathy (IgAN) consist of undergalactosylated, mostly polymeric, and J chain-containing IgA1 and IgG antibodies specific for N-acetylgalactosamine (GalNAc) residues in O-linked glycans of the hinge region of IgA1 heavy chains. N-acetylgalactosaminuronic acid 228-234 IGAN1 Homo sapiens 89-93 9555659-9 1998 These results suggested the presence of a defect in the Gal and/or GalNAc residues in the IgA1 hinge glycopeptides in IgAN. N-acetylgalactosaminuronic acid 67-73 IGAN1 Homo sapiens 118-122 30553446-9 2019 The numbers of GalNAc and Gal and the Gal/GalNAc ratio in the HR of the IgAN recipients had significantly lower comparing to the IgAD and non-IgAD healthy donors. N-acetylgalactosaminuronic acid 15-21 IGAN1 Homo sapiens 72-76 30553446-9 2019 The numbers of GalNAc and Gal and the Gal/GalNAc ratio in the HR of the IgAN recipients had significantly lower comparing to the IgAD and non-IgAD healthy donors. N-acetylgalactosaminuronic acid 42-48 IGAN1 Homo sapiens 72-76 30553446-10 2019 The decreased Gal/GalNAc ratio in IgAN recipients means the increased ratio of galactose-deficient IgA1. N-acetylgalactosaminuronic acid 18-24 IGAN1 Homo sapiens 34-38 30553446-12 2019 Overall, decreased GalNAc and Gal contents in HR could play a material pathogenic role in IgAN. N-acetylgalactosaminuronic acid 19-25 IGAN1 Homo sapiens 90-94 30570353-1 2018 Galactose-deficient IgA1 (Gd-IgA1) that exposes GalNAc or sialylated GalNAc has been shown to be associated with disease activity of IgA nephropathy (IgAN). N-acetylgalactosaminuronic acid 48-54 IGAN1 Homo sapiens 133-148 30570353-1 2018 Galactose-deficient IgA1 (Gd-IgA1) that exposes GalNAc or sialylated GalNAc has been shown to be associated with disease activity of IgA nephropathy (IgAN). N-acetylgalactosaminuronic acid 48-54 IGAN1 Homo sapiens 150-154 30570353-1 2018 Galactose-deficient IgA1 (Gd-IgA1) that exposes GalNAc or sialylated GalNAc has been shown to be associated with disease activity of IgA nephropathy (IgAN). N-acetylgalactosaminuronic acid 69-75 IGAN1 Homo sapiens 133-148 30570353-1 2018 Galactose-deficient IgA1 (Gd-IgA1) that exposes GalNAc or sialylated GalNAc has been shown to be associated with disease activity of IgA nephropathy (IgAN). N-acetylgalactosaminuronic acid 69-75 IGAN1 Homo sapiens 150-154