Download Powerpoint - Blood Journal

Survey
yes no Was this document useful for you?
   Thank you for your participation!

* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project

Document related concepts
no text concepts found
Transcript
Human cathelicidin, hCAP-18, is processed to the
antimicrobial peptide LL-37 by extracellular cleavage with
proteinase 3
by Ole E. Sørensen, Per Follin, Anders H. Johnsen, Jero Calafat, G. Sandra
Tjabringa, Pieter S. Hiemstra, and Niels Borregaard
Blood
Volume 97(12):3951-3959
June 15, 2001
©2001 by American Society of Hematology
Cleavage sites of cathelicidins.Cleavage sites between the cathelin part and the antimicrobial
peptide of the bovine and porcine cathelicidins, cleaved by elastase, compared with the
cleavage site of hCAP-18.
Ole E. Sørensen et al. Blood 2001;97:3951-3959
©2001 by American Society of Hematology
Electron microscopy of neutrophils from skin windows after phagocytosis of latex beads.(A)
Cryosection incubated with anti–hCAP-18 and 10-nm protein A-gold.
Ole E. Sørensen et al. Blood 2001;97:3951-3959
©2001 by American Society of Hematology
Immunoblotting of cell lysates.Neutrophils were TCA-precipitated, and the precipitates were run
on SDS-PAGE and analyzed by immunoblotting with anti–hCAP-18 antibodies.
Ole E. Sørensen et al. Blood 2001;97:3951-3959
©2001 by American Society of Hematology
Immunoblotting of exocytosed material.After stimulation, the neutrophils were pelleted and the
supernatant containing the exocytosed material was analyzed by SDS-PAGE and
immunoblotting with anti–hCAP-18 antibodies.
Ole E. Sørensen et al. Blood 2001;97:3951-3959
©2001 by American Society of Hematology
Immunoblotting of hCAP-18 after incubation with azurophil granule proteins.Purified hCAP-18
was incubated with azurophil granule proteins.
Ole E. Sørensen et al. Blood 2001;97:3951-3959
©2001 by American Society of Hematology
Immunoblotting with monoclonal anti–LL-37 antibody.All samples were run on SDS-PAGE
followed by immunoblotting with monoclonal anti–LL-37 antibody.
Ole E. Sørensen et al. Blood 2001;97:3951-3959
©2001 by American Society of Hematology
Cleavage experiment with exocytosed material.Exocytosed material from ionomycin-stimulated
neutrophils was depleted of endogenous hCAP-18 and subsequently incubated with purified
hCAP-18 with or without protease inhibitors.
Ole E. Sørensen et al. Blood 2001;97:3951-3959
©2001 by American Society of Hematology
Differential inhibition of hCAP-18 cleavage by serine proteases from azurophil granules.Samples
were run on SDS-PAGE followed by immunoblotting with anti–hCAP-18 antibodies.
Ole E. Sørensen et al. Blood 2001;97:3951-3959
©2001 by American Society of Hematology
Cleavage of hCAP-18 by exocytosed material after the immunoprecipitation of individual serine
proteases.Endogenous hCAP-18 fragments were deleted from the exocytosed material.
Ole E. Sørensen et al. Blood 2001;97:3951-3959
©2001 by American Society of Hematology
Susceptibility of lipoprotein-bound hCAP-18 to cleavage by proteinase 3.Lipoprotein-bound
hCAP-18 (lane a) was incubated with proteinase 3 (lane b).
Ole E. Sørensen et al. Blood 2001;97:3951-3959
©2001 by American Society of Hematology