Molecular cloning and characterization of a novel rat CXC chemokine, rPBP, the homologue of human and mouse PBP

Wen Xian Fu, Meng Lei Zhu, Shun You Gong, Yan Li, Wei Feng Chen*

*Corresponding author for this work

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

We have previously cloned the mouse platelet basic protein (mPBP), a homologue of human PBP, from mouse thymic stromal cells. Using EST alignment and RT-PCR, the rat homologue of human and mouse PBP was cloned from lung and named as rPBP. The complete open reading frame and part of the 3′- and 5′-non-coding regions were obtained through rapid amplification of cDNA ends. The rPBP cDNA encodes a protein of 111 amino acids containing a signal peptide of 37 amino acids at the N-terminus, with the mature protein of 74 amino acids. The rPBP is a new member of ELR+CXC chemokines. The mature protein of rPBP shares 69% and 45% homology with mouse and human PBP, respectively. In situ hybridization assay revealed rPBP to be predominantly localized in the pulmonary vascular endothelial cells. The eukaryotic expression vector pCDNA3-rPBP was constructed and transiently transfected into COS-7 cells. In the in vitro chemotaxis assay, the polymorphonuclear leukocytes (PMNs) were chemoattracted to the supernatants from transfected COS-7 cells in a dose-dependent manner. The implication of rPBP found in rat lung is that this chemokine may have the function to recruit PMNs to fight against pulmonary infection.

Original languageEnglish (US)
Pages (from-to)37-43
Number of pages7
JournalCytokine
Volume26
Issue number1
DOIs
StatePublished - Apr 7 2004

Keywords

  • Chemokine
  • Chemotaxis
  • EST assembly
  • PBP

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Biochemistry
  • Hematology
  • Molecular Biology

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