Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk.

@article{Lin1999PurificationAC,
  title={Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk.},
  author={Chu Yuan Lin and Jonas Anders and Marc C. Johnson and Robert B. Dickson},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 26},
  pages={18237-42}
}
Matriptase, a trypsin-like serine protease with two potential regulatory modules (low density lipoprotein receptor and complement C1r/s domains), was initially purified from T-47D breast cancer cells. Given its plasma membrane localization, extracellular matrix-degrading activity, and expression by breast cancer cells, this protease may be involved in multiple aspects of breast tumor progression, including cancer invasion. In breast cancer cells, matriptase was detected mainly as an uncomplexed… CONTINUE READING
Highly Influential
This paper has highly influenced 13 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS