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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications Vol. 256; no. 3; pp. 642 - 645
Main Authors: Nakagawa, Hideo, Takano, Katsuhiko, Kuzumaki, Hidekazu
Format: Journal Article
Language:English
Published: United States Elsevier Inc 24-03-1999
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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.
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ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1999.0393