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Localization of porcine CD29 transcripts and protein in pig cells and tissues by RT-PCR and immunohistochemistry

Authors :
Angela Moreno
Yolanda Millán
Ángeles Jiménez-Marín
Juana Martín de la Mulas
L. Morera
D. Llanes
M. Barbancho
Juan J. Garrido
Source :
Veterinary Immunology and Immunopathology. 104:281-288
Publication Year :
2005
Publisher :
Elsevier BV, 2005.

Abstract

Integrins are heterodimeric cell adhesion proteins with major roles in a variety of biological processes ranging from cell migration to tissue organization, immune and non-immune defense mechanisms and oncogenic transformation. Members of the beta(1) integrin subfamily are composed of a beta(1) subunit (CD29) non-covalently associated with different alpha subunits to constitute a group of transmembrane glycoproteins that participate in many physiologically important events. Here, we have studied the CD29 expression in porcine tissues and cells at two different levels: expression of the CD29 mRNA by RT-PCR and localization of the protein by immunohistochemistry. CD29 transcripts were detected in a variety of tissues and cells: platelets, PBMC, granulocytes, alveolar macrophages, smooth muscle, intestine, lung, liver, spleen, lymph node, skin, testis, heart, kidney and bone marrow. Our results suggest that CD29 gene transcription occurs in all organs examined, although with different intensities. The precise localization of CD29 protein in paraffin-embedded tissues was detected by using a specific polyclonal antibody indicating that its expression is limited to smooth muscle, epithelium cells, endothelium of blood vessels and myeloid cells and is no detectable in cells of the lymphoid lineage. The distribution of the CD29 in normal tissues provide insight into the physiological function of the porcine beta(1) integrins and should be of importance in understanding the role of this integrin family in pathological processes.

Details

ISSN :
01652427
Volume :
104
Database :
OpenAIRE
Journal :
Veterinary Immunology and Immunopathology
Accession number :
edsair.doi.dedup.....8f52e97097ccced747ac495929e83e21
Full Text :
https://doi.org/10.1016/j.vetimm.2004.12.009