Keratinocyte urokinase-type plasminogen activator is secreted as a single chain precursor.

Published

Journal Article

Urokinase-type plasminogen activator (uPA) is produced and secreted by cultured human keratinocytes as a single chain precursor. UPA in keratinocyte conditioned medium is not susceptible to inhibition with diisopropylfluorophosphate (DFP), and it has an apparent molecular weight of 55 kD under both reducing and nonreducing conditions. Cleavage of keratinocyte uPA by plasmin results in the formation of a 96 kD complex comprised of activated uPA and PA inhibitor 2. PA extracted from normal human epidermis is only partially inhibited by DFP, suggesting that precursor uPA is also present in vivo. The synthesis of uPA as a precursor with reduced enzymatic activity as well as decreased affinity for inhibitors is likely to be a mechanism by which normal epidermis regulates plasminogen activation in vivo.

Full Text

Duke Authors

Cited Authors

  • Hashimoto, K; Prystowsky, JH; Baird, J; Lazarus, GS; Jensen, PJ

Published Date

  • June 1988

Published In

Volume / Issue

  • 90 / 6

Start / End Page

  • 823 - 828

PubMed ID

  • 2967334

Pubmed Central ID

  • 2967334

International Standard Serial Number (ISSN)

  • 0022-202X

Language

  • eng

Conference Location

  • United States