Internalization and degradation of heparin binding growth factor-I by endothelial cells.
Internalization and degradation of heparin binding growth factor-I by endothelial cells.
复制标题
内皮细胞对肝素结合生长因子-I 的内化和降解。
DOI:
10.1016/s0006-291x(88)80459-5
复制
发表时间:
1988
影响因子:
3.1
通讯作者:
Maciag,T
中科院分区:
文献类型:
--
作者:
Friesel,R;Maciag,T
The fate of125I-labeled heparin binding growth factor I (125I-HBGF-I) after binding to its cell surface receptor has been studied using murine lung capillary endothelial cells (LEII). Binding of125I-HBGF-I to its receptor at 4°C shows pH dependence with optimal binding at pH 6.5–7.5. The majority (∼80%) of125I-HBGF-I bound to cells at 4°C can be removed by washing with low pH medium, but rapidly becomes acid resistant upon shifting cells to 37°C, with 50% of the125I-HBGF-I becoming acid resistant after 20 minutes. Electrophoretic analysis of internalized125I-HBGF-I shows that degradation begins approximately 2 hours after internalization with the appearance of two major labeled fragments of Mr15,000 and Mr10,000. Degradation of internalized125I-HBGF-I is inhibited by the lysosomotropic agent chloroquine. These data suggest that cell-associated125I-HBGF-I is rapidly internalized and directed to a lysosomal cellular compartment where it is slowly degraded.