Fridman R, Lider O, Naparstek Y, Fuks Z, Vlodavsky I, Cohen I R
J Cell Physiol. 1987 Jan;130(1):85-92. doi: 10.1002/jcp.1041300113.
The antigen-mediated induction of heparanase, an endoglycosidase capable of degrading heparan sulfate from the subendothelial extracellular matrix (ECM), was investigated in a rat T lymphocyte cell line reactive against the basic protein (BP) of myelin. We found that nonactivated T lymphocytes could be induced to express heparanase activity following exposure to soluble but not to ECM-bound BP. The induction of heparanase was immunologically specific and independent of the presence of syngeneic or allogeneic antigen presenting cells (APC). However, anti-IA antibodies inhibited heparanase expression. Soluble BP induced secretion of heparanase into the culture medium within minutes, despite inhibition of protein synthesis. Cell lysates of T lymphocytes contained heparanase activity. Thus, T lymphocytes secrete a preformed heparanase following exposure to specific antigen.
在一种对髓鞘碱性蛋白（BP）有反应的大鼠T淋巴细胞系中，研究了抗原介导的乙酰肝素酶（一种能够从内皮下细胞外基质（ECM）降解硫酸乙酰肝素的内切糖苷酶）的诱导作用。我们发现，未活化的T淋巴细胞在暴露于可溶性BP而非ECM结合的BP后，可被诱导表达乙酰肝素酶活性。乙酰肝素酶的诱导具有免疫特异性，且与同基因或异基因抗原呈递细胞（APC）的存在无关。然而，抗IA抗体可抑制乙酰肝素酶的表达。可溶性BP在数分钟内即可诱导乙酰肝素酶分泌到培养基中，尽管蛋白质合成受到抑制。T淋巴细胞的细胞裂解物含有乙酰肝素酶活性。因此，T淋巴细胞在暴露于特定抗原后会分泌预先形成的乙酰肝素酶。
