Thiocyanate-Based Toxicity of Eosinophil Peroxidase

Slungaard, Arne

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Heart, Lung, and Blood Institute (NHLBI)
• Type: Research Project (R01)
• Project #: 5R01HL048915-03
• Application #: 2225016
• Study Section: Hematology Subcommittee 2 (HEM)
• Project Start: 1994-02-01
• Project End: 1998-01-31
• Budget Start: 1996-02-01
• Budget End: 1997-01-31
• Support Year: 3
• Fiscal Year: 1996

Institution

• Name: University of Minnesota Twin Cities
• Department: Internal Medicine/Medicine
• Type: Schools of Medicine
• DUNS #: 168559177
• City: Minneapolis
• State: MN
• Country: United States
• Zip Code: 55455

Publications

Arlandson, M; Decker, T; Roongta, V A et al. (2001) Eosinophil peroxidase oxidation of thiocyanate. Characterization of major reaction products and a potential sulfhydryl-targeted cytotoxicity system. J Biol Chem 276:215-24

Mitra, S N; Slungaard, A; Hazen, S L (2000) Role of eosinophil peroxidase in the origins of protein oxidation in asthma. Redox Rep 5:215-24

Xu, D; Yoder, M; Sutton, J et al. (1998) Forced expression of Genesis, a winged helix transcriptional repressor isolated from embryonic stem cells, blocks granulocytic differentiation of 32D myeloid cells. Leukemia 12:207-12

Brottman, G M; Regelmann, W E; Slungaard, A et al. (1996) Effect of eosinophil peroxidase on airway epithelial permeability in the guinea pig. Pediatr Pulmonol 21:159-66

Sutton, J; Costa, R; Klug, M et al. (1996) Genesis, a winged helix transcriptional repressor with expression restricted to embryonic stem cells. J Biol Chem 271:23126-33

Slungaard, A; Key, N S (1994) Platelet factor 4 stimulates thrombomodulin protein C-activating cofactor activity. A structure-function analysis. J Biol Chem 269:25549-56