Disease relevance of CD29

• 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 [1].

High impact information on CD29

• Expression analysis showed that porcine CD29 is expressed in all lymphoid tissues tested and, in lower amounts, in nonlymphoid tissues [2].
• Pig CD29 deduced amino acid sequence displays extensive conservation compared with CD29 sequences from other species and a common structural feature with all the other CD29 molecules analyzed in mammals, including the 12 potential N-glycosilation sites [2].
• METHODS: The porcine CD29 cDNA has been isolated from a cDNA library and its structure determined [2].
• Binding of anti-Gal(alpha)1-3Gal antibodies to endothelial cell surfaces significantly diminished labeling of fibronectin and the integrin beta1 subunit by galactose oxidase, indicating that these glycoproteins are targets for the antibodies when binding to intact porcine cells [3].
• 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 [1].

Biological context of CD29

• MAb GP4B4 was developed from a mouse immunized with porcine peripheral blood mononuclear cells (PBMC), while MAbs GP1A5, GP1A6, and GP4A1 were produced by immunizing mice with a porcine CD29 recombinant protein (rpCD29) developed in our laboratory, which includes the ligand binding site [4].
• Assignment of the ITGB1 (integrin beta1 subunit) gene to pig chromosome band 10q17 with somatic cell hybrids [5].

Anatomical context of CD29

• 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 [1].
• The phenotypic analysis of the cells recognized by these lectins indicated that PNA(+) lymphocytes showed higher rate of the CD29 antigen (PNA(+)CD29(high)) than ALL(+) (ALL(+)CD29(low)) [6].
• 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 [1].
• Immunohistochemical analyses of these MAbs disclosed a morphological pattern associated with smooth muscle, epithelium, and myeloid cells, as expected in MAbs recognizing CD29 [4].
• Of all the glycoproteins and glycolipids containing Gal(alpha)1-3Gal, two molecules, fibronectin and the integrin beta1 subunit, were most intensely labeled by galactose oxidase, suggesting that these molecules may be preferentially exposed on the apical surface of the endothelium [3].

Analytical, diagnostic and therapeutic context of CD29

• In addition, reverse transcription-polymerase chain reaction (RT-PCR) was performed to determine the expression of CD29 in different tissues [2].
• In addition, the determination of the differences between human and swine CD29 will help to understand the adhesion molecule-ligand interactions and their function across the swine-human barrier in xenotransplantation [2].
• Molecular cloning and characterization of the pig homologue to human CD29, the integrin beta1 subunit [2].
• Localization of porcine CD29 transcripts and protein in pig cells and tissues by RT-PCR and immunohistochemistry [1].

References