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In vivo evidence of the role of α 4 β 1 ‐VCAM‐1 interaction in sarcoma, but not in carcinoma extravasation
Author(s) -
Paavonen Timo,
Tiisala Sinikka,
Majuri MarjaLeena,
Böhling Tom,
Renkonen Risto
Publication year - 1994
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910580225
Subject(s) - extravasation , sarcoma , cell adhesion molecule , endothelium , pathology , selectin , endothelial stem cell , biology , in vivo , cell adhesion , immunoglobulin superfamily , cancer research , metastasis , leukocyte extravasation , vcam 1 , in vitro , immunology , cell , cancer , medicine , icam 1 , endocrinology , biochemistry , genetics , microbiology and biotechnology
Tumor‐cell invasion can occur via either lymphatics or blood vessels. When in the blood circulation, tumor cells have to adhere to endothelium lining the blood vessels before they can extravasate. Several families of adhesion molecules have been recognized: selectins and their oligosaccharide‐containing ligands and integrins and their counter‐receptors belonging to the immunoglobulin superfamily. Besides their essential role in leukocyte extravasation, these adhesion molecules have been proposed by in vitro experiments to be involved in tumor‐cell invasion by facilitating the adhesion of malignant cells to endothelium leading to extravasation and metastasis. We have previously shown that, in vitro , several sarcoma cell lines adhere strongly to cultured endothelial cells via α 4 β 1 ‐VCAM‐1 interaction. Here we show that sarcoma cells, especially in the metastatic lesions, were strongly α 4 β 1 positive but did not express α 4 β 7 , which is another receptor for VCAM‐1. Furthermore, we demonstrate that the capillary endothelium within metastatic sarcoma lesions reacted strongly with anti‐VCAM‐1 antibody and very often the α 4 β 1 ‐expressing sarcoma cells were localized in the close vicinity of VCAM‐1‐expressing vessels. As control material we analyzed carcinoma specimens, but could not detect any α 4 ‐integrin expression on malignant cells even though the endothelial cells were often VCAM‐1 positive. These results suggest that carcinomas do not use α 4 β 1 ‐VCAM‐1 in extravasation and, taken together, provide circumstantial evidence that in vitro findings of α 4 β 1 ‐VCAM‐1‐dependent sarcoma cell adhesion to endothelium can be extended to in vivo situations.