Tumour-expressed CD43 (sialophorin) mediates tumour-mesothelial cell adhesion
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Paul Ziprin
, Nawar A. Alkhamesi , Paul F. Ridgway , David H. Peck und Ara W. Darzi
Abstract
Mesothelial cell intercellular adhesion molecule-1 (ICAM-1) has recently been shown to play a role in tumour cell adherence to the peritoneum. However, solid tumours poorly express its most ubiquitous ligand, β2 integrin. The aim of this study was to investigate the role of the β2 integrin subunit and CD43, a known ligand for ICAM-1, in the development of peritoneal metastases. β2 Integrin subunit and CD43 expression was assessed on a number of tumour cell lines. Adhesion of SW1222 and PSN-1 cells to human peritoneal mesothelial cells was investigated using a fluorometric assay incorporating an inhibitory antibody to β2 integrin and CD43. β2 Integrin expression was not inducible on these tumour cell lines, but Western blotting demonstrated CD43 expression in all the cancer cell lines examined and cell surface expression was confirmed by flow cytometry. The anti-CD43 antibody significantly reduced adhesion of PSN-1 and SW1222 cells to HPMC, however β2 integrin inhibition did not reduce tumour cell adhesion. CD43 is expressed by a variety of carcinoma cell lines, and plays a role in tumour cell-peritoneal adhesion probably via interactions with its putative ligand ICAM-1.
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Artikel in diesem Heft
- Molecular genetics of human cervical cancer: role of papillomavirus and the apoptotic cascade
- Regulatory role of membrane-bound peptidases in the progression of gynecologic malignancies
- Functional genomics identifies novel and diverse molecular targets of nutrients in vivo
- Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction
- Functional GATA- and initiator-like-elements exhibit a similar arrangement in the promoters of Caenorhabditis elegans polyamine synthesis enzymes
- Fluid shear stress induces endothelial KLF2 gene expression through a defined promoter region
- Recombinant expression, purification and cross-reactivity of chenopod profilin: rChe a 2 as a good marker for profilin sensitization
- Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding
- Distinctive functional features in prokaryotic and eukaryotic Cu,Zn superoxide dismutases
- Tumour-expressed CD43 (sialophorin) mediates tumour-mesothelial cell adhesion