| Project/Area Number |
14571034
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Kidney internal medicine
|
|---|
| Research Institution | Kitasato University |
|---|
Principal Investigator |
IWASE Hitoo Kitasato University, School of Medicine, Associate Professor, 医学部, 助教授 (60050663)
|
|---|
| Project Period (FY) |
2002 – 2003
|
| Project Status |
Completed (Fiscal Year 2003)
|
| Budget Amount *help |
¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 2003: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 2002: ¥1,500,000 (Direct Cost: ¥1,500,000)
|
|---|
| Keywords | IgA nephropathy / porcine gastric mucus / hypoglycosylated IgA1-HPLC / IgA1-binding protein / mucin-type sugar chain / mesangial channel / IgA1 hinge / kappa / lambda ratio / 分子間相互作用解析装置 / IgA1-BP / 胃粘膜 / 等電点電気泳動 / 扁桃 / Thomsen-Friedenreich抗原 |
|---|
| Research Abstract |
This research was carried out as a part of the study on IgA nephropathy. Obtained results were summarized as follows;
(1) IgA1-BP could be separated from serum by hypoglycosylated HPLC column. Reproduction of the separation of IgA1-BP was confirmed by this column.
(2) IgA1-BP was composed from IgA, IgG, IgM and C3. Among IgG subclasses, IgA1-BP was abundant in IgG1 and IgG3 subclass. About 87 % of IgA in IgA1-BP composed from IgA1 subclass. The IgA in IgA1-BP was abundant in medium-size IgA, jacalin-high-affinity IgA and IgA with lambda-type light chain. These natures were similar to those of the deposited IgA in IgA nephropathy patient.
(3) The tonsillar IgA was different from serum IgA in those IEF profiles. Since the IgA1 could accept sialic acid by (O)sialyltransferase, tonsillar IgA1 should be hypoglycosylated IgA1. IgA content in tonsillar tissue was significantly higher in IgA nephropathy patient.
(4) Detection of the antibody activity by synthetic glycopeptide probes indicated the gender difference in its activity.
(5) IgA1-BP was separated from pepsin digest of porcine gastric mucin. Analysis of the IgA1-BP by gel filtration, dialysis, electrophoresis and HPLC indicated the IgA1-BP prepared from mucus was a low-molecular-weight material below 5 kd. The IgA1-BP was fractionated into many peaks having the absorbance at 280 nm by ODS column. Due to the contamination peptide or its random degradation by pepsin digestion, sequence analysis of amino acid of these peaks did not show a constant amino acid sequence enough to determine the originated protein.
|
