Heparin Cofactor II-Proteinase Reaction Products Exhibit Neutrophil Chemoattractant Activity

The physiologic function of the plasma glycoprotein heparin cofactor ll (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...

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Bibliographic Details
Published in:Blood 1989-05, Vol.73 (6), p.1682-1685
Main Authors: Hoffman, Maureane, Pratt, Charlotte W., Brown, Rebecca L., Church, Frank C.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Cathepsin G
Cathepsins - metabolism
Chemotaxis, Leukocyte
Fundamental and applied biological sciences. Psychology
Glycoproteins
Glycoproteins - physiology
Heparin Cofactor II
Humans
In Vitro Techniques
Neutrophils - physiology
Pancreatic Elastase - metabolism
Peptide Fragments - physiology
Proteins
Serine Endopeptidases
Time Factors
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Summary:The physiologic function of the plasma glycoprotein heparin cofactor ll (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 elas-tase (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.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood.V73.6.1682.1682