Studies on biological activities, their molecular mechanisms, and structure-function relationships of lectins from marine algae
| Project/Area Number |
15380143
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Fisheries chemistry
|
|---|
| Research Institution | Hiroshima University |
|---|
Principal Investigator |
HORI Kanji Hiroshima University, Graduate School of Biosphere Science, Professor, 大学院生物圏科学研究科, 教授 (50116662)
|
|---|
| Project Period (FY) |
2003 – 2005
|
| Project Status |
Completed (Fiscal Year 2005)
|
| Budget Amount *help |
¥15,000,000 (Direct Cost: ¥15,000,000)
Fiscal Year 2005: ¥4,000,000 (Direct Cost: ¥4,000,000)
Fiscal Year 2004: ¥4,100,000 (Direct Cost: ¥4,100,000)
Fiscal Year 2003: ¥6,900,000 (Direct Cost: ¥6,900,000)
|
|---|
| Keywords | Algae / lectins / sugar recognition / molecular structures / cancer / Anti-HIV / Biological activities / receptor / 抗HIV活性 / 糖鎖結合特異性 / cDNAクローニング / ニワトリ抗体 / 癌細胞 / 糖鎖 / 簡易精製法 / 腫瘍細胞 / 活性発現機構 / cDNA / 構造解析 |
|---|
| Research Abstract |
The studies were performed aimed at clarifying biological activities, their molecular mechanisms, and structure-function relationships of marine algal lectins, especially those that belong to a high-mannose N-glycan specific lectin family or a multifunctional low-molecular weight polypeptidic lectin family.
With respect to a high-mannose N-glycan specific lectin family, first, the detailed carbohydrate-binding specificity and the primary structure of a red alga, Eucheuma serra lectin (ESA-2) were elucidated. Next, it was found that orally administration of ESA-2 suppressed the formation of colon aberrant crypt foci in mice received 1,2-dimethylhydrazine, due to the lower production of active oxygen in the colonic tissues. Relating to this, a receptor for ESA-2 on the cultured cells (HT-29) derived from human colonic cancer was identified using a newly established method for isolation of cell membrane receptors. In addition, the primary structure and the detailed carbohydrate-binding specificity of a cyanobacterium, Oscillatoria agardhii lectin (OAA), that belongs to this family, was elucidated. Furthermore, it was demonstrated that some lectins belonging to this family are very useful as affinity ligands for one-step purification of chicken monoclonal antibody that is usable for diagnosis of bovine spongiform encephalopathy (BSE).
With respect to a multifunctional low-molecular weight polypeptidic lectin family, it was found that the lectin (hypnin A) from the red alga, Hypnea japonica is strictly specific for core α1-6 fucose in N-glycans, and would be useful as a reagent to detect cancer marker(s) as well as to prepare medicinal antibodies lacking the core α1-6 fucose that have effective antibody-dependent cellular cytotoxicity (ADCC)
|
Report
(4 results)
Research Products
(9 results)
