Heparin cofactor II-proteinase reaction products exhibit neutrophil chemoattractant activity.
The physiologic function of the plasma glycoprotein heparin cofactor II (HCII) is not well understood. An in vivo role for thrombin (IIa) inhibition by HCII in the presence of certain glycosaminoglycans (dermatan sulfate and heparin) can be proposed. Many proteins, such as complement components, can be proteolyzed to generate secondary bioactive molecules. HCII is a substrate for the human neutrophil (PMN) proteinases cathepsin G (CG) and elastase (LE). We found that degradation of HCII by CG or LE generated products with potent PMN chemotactic activity, which did not stimulate the PMN oxidative burst. Our results suggest that HCII may be a physiologic regulator of the acute inflammatory response.
Hoffman
M
M
Department of Pathology, University of North Carolina School of Medicine, Chapel Hill 27599-7035.
Pratt
C W
CW
Brown
R L
RL
Church
F C
FC
D056649:Cathepsin G; D002403:Cathepsins / Q000378:metabolism; D002634:Chemotaxis, Leukocyte; D006023:Glycoproteins / Q000502:physiology*; D015844:Heparin Cofactor II; D006801:Humans; D066298:In Vitro Techniques; D009504:Neutrophils / Q000502:physiology*; D010196:Pancreatic Elastase / Q000378:metabolism; D010446:Peptide Fragments / Q000502:physiology; D012697:Serine Endopeptidases; D013997:Time Factors
D006023:Glycoproteins; D010446:Peptide Fragments; D015844:Heparin Cofactor II; D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase