Burgess W H, Dionne C A, Kaplow J, Mudd R, Friesel R, Zilberstein A, Schlessinger J, Jaye M
American Red Cross, Rockville, Maryland 20855.
Mol Cell Biol. 1990 Sep;10(9):4770-7. doi: 10.1128/mcb.10.9.4770-4777.1990.
Heparin-binding growth factors (HBGFs) bind to high-affinity cell surface receptors which possess intrinsic tyrosine kinase activity. A Mr 150,000 protein phosphorylated on tyrosine in response to class 1 HBGF (HBGF-1) was purified and partially sequenced. On the basis of this sequence, cDNA clones were isolated from a human endothelial cell library and identified as encoding phospholipase C-gamma. Phosphorylation of phospholipase C-gamma in intact cells treated with HBGF-1 was directly demonstrated by using antiphospholipase C-gamma antibodies. Thus, HBGF-1 joins epidermal growth factor and platelet-derived growth factor, whose receptor activation leads to tyrosine phosphorylation and probable activation of phospholipase C-gamma.
肝素结合生长因子（HBGFs）与具有内在酪氨酸激酶活性的高亲和力细胞表面受体结合。一种分子量为150,000的蛋白质，在对1类HBGF（HBGF-1）作出反应时发生酪氨酸磷酸化，已被纯化并进行了部分测序。根据该序列，从人内皮细胞文库中分离出cDNA克隆，并鉴定为编码磷脂酶C-γ。通过使用抗磷脂酶C-γ抗体直接证明了用HBGF-1处理的完整细胞中磷脂酶C-γ的磷酸化。因此，HBGF-1加入了表皮生长因子和血小板衍生生长因子的行列，它们的受体激活会导致酪氨酸磷酸化以及磷脂酶C-γ的可能激活。
