A 16-kDa Fragment of Collagen Type XIV Is a Novel Neutrophil Chemotactic Factor Purified from Rat Granulation Tissue
A neutrophil chemotactic factor has been purified from the homogenate of rat granulation tissues. The purified chemoattractant was a basic protein with heparin-binding site and gave a single band corresponding to a molecular mass of 16 kDa on SDS–PAGE under reducing conditions. The chemoattractant w...
Saved in:
Published in: | Biochemical and biophysical research communications Vol. 256; no. 3; pp. 642 - 645 |
---|---|
Main Authors: | , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
Elsevier Inc
24-03-1999
|
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | A neutrophil chemotactic factor has been purified from the homogenate of rat granulation tissues. The purified chemoattractant was a basic protein with heparin-binding site and gave a single band corresponding to a molecular mass of 16 kDa on SDS–PAGE under reducing conditions. The chemoattractant was treated with lysylendopeptidase and the resulting peptides were isolated by reversed-phase HPLC. Amino acid sequences of the peptides were almost identical with the sequence of N-terminal fibronectin type III domain of human collagen type XIV, suggesting that the purified chemoattractant consists mainly of N-terminal fibronectin type III domain and the adjacent heparin-binding site of rat collagen type XIV. The 16-kDa fragment of collagen type XIV dose dependently attracted rat neutrophils and transiently increased the intracellular free Ca2+concentration of neutrophils. The results suggest that the novel chemoattractant plays a role in neutrophil recruitment in rat inflammation. |
---|---|
Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1006/bbrc.1999.0393 |