120-kD surface glycoprotein of Pneumocystis carinii is a ligand for surfactant protein A.

@article{Zimmerman1992120kDSG,
  title={120-kD surface glycoprotein of Pneumocystis carinii is a ligand for surfactant protein A.},
  author={Paul Zimmerman and Dennis R. Voelker and Francis X McCormack and John R. Paulsrud and Ii William J. Martin},
  journal={The Journal of clinical investigation},
  year={1992},
  volume={89 1},
  pages={
          143-9
        }
}
Pneumocystis carinii is the most common cause of life-threatening pneumonia in immunocompromised patients. In the current study, surfactant protein A (SP-A), the major nonserum protein constituent of pulmonary surfactant, is demonstrated to bind P. carinii in a specific and saturable manner. SP-A is surface bound and does not appear to be internalized or degraded by the P. carinii organism. Furthermore, SP-A binding to P. carinii is time- and calcium-dependent and is competitively inhibited by… CONTINUE READING

Figures and Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 53 CITATIONS, ESTIMATED 43% COVERAGE

Nitrated SP-A does not enhance adherence of Pneumocystis carinii to alveolar macrophages.

  • American journal of physiology. Lung cellular and molecular physiology
  • 1998
VIEW 5 EXCERPTS
CITES BACKGROUND & RESULTS

Inhibition of surfactant activity by Pneumocystis carinii organisms and components in vitro.

  • American journal of physiology. Lung cellular and molecular physiology
  • 2005
VIEW 4 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

FILTER CITATIONS BY YEAR

1993
2018

CITATION STATISTICS

  • 3 Highly Influenced Citations