Isolation, characterization, and cDNA cloning of a vampire bat salivary plasminogen activator.


Journal Article

Vampire bat saliva contains a plasminogen activator that presumably assists these hematophagous animals during feeding. Here, we report that the vampire bat salivary plasminogen activator, Bat-PA, is homologous to tissue-type plasminogen activator (t-PA) but contains neither a kringle 2 domain nor a plasmin-sensitive processing site. Three Bat-PA species corresponding to full-length, finger-, and finger- epidermal growth factor homology domain- forms of t-PA have been isolated. Bat-PA(H), the full-length form, was purified and its activity has been characterized. Bat-PA(H) and t-PA are of similar efficacy when monitored for their abilities to catalyze plasminogen activation in the presence of a fibrin cofactor. Interestingly, Bat-PA activity toward plasminogen is stimulated 45,000-fold in the presence of fibrin I; the corresponding value for t-PA is only 205-fold. Bat-PA(H) is the only Bat-PA species which binds tightly to fibrin, although each of the three species exhibit remarkable stimulation by a fibrin cofactor.

Full Text

Duke Authors

Cited Authors

  • Gardell, SJ; Duong, LT; Diehl, RE; York, JD; Hare, TR; Register, RB; Jacobs, JW; Dixon, RA; Friedman, PA

Published Date

  • October 25, 1989

Published In

Volume / Issue

  • 264 / 30

Start / End Page

  • 17947 - 17952

PubMed ID

  • 2509450

Pubmed Central ID

  • 2509450

International Standard Serial Number (ISSN)

  • 0021-9258


  • eng

Conference Location

  • United States