| Project/Area Number |
62470147
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
物質生物化学
|
|---|
| Research Institution | Nagoya University |
|---|
Principal Investigator |
SUZUKI Sakaru Nagoya Univ., Faculty of Science, Professor, 理学部, 教授 (50022504)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
羽淵 弘子 (羽渕 弘子) 名古屋大学, 理学部, 助手 (70109263)
TSUJI Masahiro Nagoya Univ., Faculty of Science, Assistant, 理学部, 助手 (80022739)
NAKANISHI Yasuo (HABUCHI Hiroko) Nagoya Univ., Faculty of Science, Assistant Professor, 理学部, 助教授 (40022636)
|
|---|
| Project Period (FY) |
1987 – 1988
|
| Project Status |
Completed (Fiscal Year 1988)
|
| Budget Amount *help |
¥6,500,000 (Direct Cost: ¥6,500,000)
Fiscal Year 1988: ¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 1987: ¥3,400,000 (Direct Cost: ¥3,400,000)
|
|---|
| Keywords | chondroitin sulfate proteoglycan / monoclonal antibody / fibronectin / cell-substratum adhesion / 細胞ー基質接着 / 人工プロテオグリカン / コンドロイチン硫酸プロテオグリカンM型 / ヘパラン硫酸プロテオグリカン / 短肢症 / 基底膜 / EHSー腫瘍 |
|---|
| Research Abstract |
1. We have previously demonstrated that chick embryo fibroblasts synthesize and secrete a large chondroitin sulfate proteoglycan (PG-M) that binds to fibronectin. We now report that chick embryo fibroblasts, BHK cells, and many other cell lines failed to adhere to fibronectin-coated substrates when PG-M was added to the medium. PG-M was also shown to inhibit the adhesion of fibroblastic cells to collagen-, or vitronection-coated substrates as well as adhesion of epithelial cells to fibronectin-coated substrates.
2. Treatment of the proteoglycan with either proteolytic enzymes or chondroitinase abolished its inhibitory effects on the fibronectin-mediated BHK cell adhesion.
3. Adhesion of the cells to laminin or GRGDS-derivatized serum albumin (RGD-containing molecules with no capacity to bind PG-M) was also inhibited by PG-M. These results indicate that the intact proteoglycan from, but not core proteinor chondroitin sulfate-free forms, is responsible for the activity, and that direct binding between PG-M and fibronectin, if any, is not a cause of the inhibition by PG-M.
4. When the immobilization of added PG-M to available plastic surfaces of fibronectin- (or GRGDS-serum albumin-) coated dishes was blocked by pretreating the dishes with serum albumin, the inhibitory effect of PG-M was abolished, suggesting that only the immobilized fraction of PG-M can act as a cell adhesion inhibitor. In immobilized form, both cartilage chondroitin sulfate proteoglycan (PG-H) and chondroitin sulfate-derivatized serum albumin also inhibited cell adhesion. In contrast, heparan sulfate proteoglycan form LD and heparan sulfate-derivatized serum albumin had far lower inhibitory activities, indicating that the active site for the interaction between cells and PG-M is on the chondroitin sulfate chain.
|
