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

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.

journal_name

Cytokine

journal_title

Cytokine

authors

Fu WX,Zhu ML,Gong SY,Li Y,Chen WF

doi

10.1016/j.cyto.2003.12.007

keywords:

subject

Has Abstract

pub_date

2004-04-07 00:00:00

pages

37-43

issue

1

eissn

1043-4666

issn

1096-0023

pii

S1043466604000043

journal_volume

26

pub_type

杂志文章

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