2006 Fiscal Year Final Research Report Summary
The role of receptor molecules for IgA in the pathogenic mechanism of IgA nephropathy
| Project/Area Number |
16390242
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Kidney internal medicine
|
|---|
| Research Institution | Niigata University |
|---|
Principal Investigator |
NARITA Ichiei Niigata University, Institute of Medicine and Dentistry, Associate Professor, 医歯学系, 助教授 (20272817)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
SAKATSUME Minoru Niigata University, Medical and Dental Hospital, Lecturer, 医歯学総合病院, 講師 (70334662)
|
|---|
| Project Period (FY) |
2004 – 2006
|
| Keywords | IgA nephropathy / Transferrin receptor / Fcα receptor / genetic polymorphism / Mesangium cell / Receptor |
|---|
| Research Abstract |
The purpose of this study was to elucidate the mechanism of mesangial IgA deposition in IgA nephropathy, especially through investigating the dynamics of receptors for IgA molecules and their metabolisms. Three molecules, pIgR (polymeric immuno-globulin receptor), FcαR, and ASGPR (asyaloglycoprotein receptor), have been known as receptor molecules for IgA. In addition, fourth molecules, TfR (Transferrin receptor), has recently been identified as receptor of IgA. It has been shown that the expression of TfR is upregulated in glomeruli of patients with IgAN, suggesting that TfR plays a role in formation of pathological immune complex in this disease.
In this study, we investigated the possible associations of genetic polymorphisms in these receptor molecules and IgAN. However, we did not find any significant association of FcαR, ASGPR, and TfR polymorphisms and IgAN.
During the last decade, several lines of evidence have been reported indicating that incompleteness of O-glycosylation in the IgAl hinge region may be a plausible cause of the IgAl deposition. O-Glycans are found in many glycoproteins, particularly in secretory glycoproteins. The common core 1 O-glycan structure, Galb-1-3GalNAc-R, is a precursor for many extended mucin-type O-glycan structures on animal cell surfaces and secreted glycoproteins including IgAl. We also have published a review paper about this notion in Kidney International (Narita I, et al. 2007).
|
-
-
-
-
-
-
-
-
-
-
-
[Journal Article] Bezafibrate suppresses rat antiglomerular basement membrane crescentic glomerulonephritis.2005
Author(s)
Saga D, Sakatsume M, Ogawa A, Tsubata Y, Kaneko Y, Kuroda T, Sato F, Ajiro J, Kondo D, Miida T, Narita I, Gejyo F
-
Journal Title
Kidney International 67
Pages: 1821-1829
Description
「研究成果報告書概要(欧文)」より
-
-
-
-
