Porcine monocyte subsets differ in the expression of CCR2 and in their responsiveness to CCL2

被引：28

作者：

Moreno, Sara ^{[1
]}

Alvarez, Belen ^{[1
]}

Poderoso, Teresa ^{[1
]}

Revilla, Concepcion ^{[1
]}

Ezquerra, Angel ^{[1
]}

Alonso, Fernando ^{[1
]}

Dominguez, Javier ^{[1
]}

机构：

[1] INIA, Dept Biotechnol, Madrid 28040, Spain

来源：

VETERINARY RESEARCH | 2010年 / 41卷 / 05期

关键词：

porcine monocyte; chemokine receptor; chemotaxis; BLOOD MONOCYTES; MONOCLONAL-ANTIBODIES; DENDRITIC CELLS; CHEMOKINE; DIFFERENTIATION; SUBPOPULATIONS; HETEROGENEITY; PROTEIN-1; MIGRATION; CD163;

D O I：

10.1051/vetres/2010048

中图分类号：

S85 [动物医学（兽医学）];

学科分类号：

0906 ;

摘要：

Monocyte subsets have been shown to differ in the pattern of chemokine receptor expression and their migratory properties, both in human and mouse. Previously we have characterized in the swine several monocyte subpopulations, based on the expression of CD163, Tuk4 and SLA-II, which share features with the populations described in human and mouse. Here, we have analysed the expression of different chemokine receptors in the CD163(-)Tuk(4+)SLA-II- and CD163(+)Tuk4(-)SLA-II+ populations of porcine monocytes. CD163(+)Tuk4(-)SLA-II+ monocytes expressed higher CX(3)CR1 but lower CCR2 and CXCR4 mRNA levels than CD163(-)Tuk4(+)SLA-II- monocytes. Moreover, porcine CCL2 binding on Tuk4(+)SLA-II- but not on Tuk4(-)SLA-II+ cells was detected by using a CCL2-green fluorescence protein (pCCL2-GFP) fusion protein. Finally, flow cytometric analyses of monocytes recovered after chemotaxis assays show a clear increase in the proportion of Tuk4(+)SLA-II- cells in the fraction migrating toward CCL2, consistent with the polarized CCR2 expression in this monocyte population. The pattern of expression of these chemokine receptors reinforces the similarities of these porcine subsets with their human and mouse counterparts.

引用

页数：11

共 29 条

[1] A porcine cell surface receptor identified by monoclonal antibodies to SWC3 is a member of the signal regulatory protein family and associates with protein-tyrosine phosphatase SHP-1 [J].