Inhibition of degranulation of human polymorphonuclear leukocytes by complement factor D.
A degranulation inhibiting protein could be isolated from human plasma ultrafiltrate by a three-step purification method including ion-exchange chromatography, gelfiltration and affinity-chromatography. The protein was identified as complement factor D by means of sequence analysis. Its degranulation inhibiting activity was determined with regard to its effect on the FNLPNTL-induced lactoferrin secretion of human polymorphonuclear leukocytes. Complement factor D caused a dose-dependent decrease of the FNLPNTL-stimulated lactoferrin degranulation down to 34% of stimulated controls.
Balke
N
N
Department of Biochemistry, Faculty of Chemistry, University of Bielefeld, Germany.
Holtkamp
U
U
Hörl
W H
WH
Tschesche
H
H
D000595:Amino Acid Sequence; D015550:Cell Degranulation / Q000502:physiology*; D011416:Complement Factor D / Q000302:isolation & purification / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000502:physiology*; D014462:Ultrafiltration
C493488:CFD protein, human; D011416:Complement Factor D