{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T11:03:55Z","timestamp":1790852635369,"version":"4.1.0"},"reference-count":31,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2006,7,17]],"date-time":"2006-07-17T00:00:00Z","timestamp":1153094400000},"content-version":"vor","delay-in-days":4996,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Intl Journal of Cancer"],"published-print":{"date-parts":[[1992,11,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The expression of the VLA\u2010integrins \u03b1<jats:sub>2<\/jats:sub>, \u03b1<jats:sub>3<\/jats:sub>, v<jats:sub>5<\/jats:sub> and \u03b1<jats:sub>6<\/jats:sub> was studied immunohistochemically in tissue samples from ductal pancreatic cancer, chronic pancreatitis, normal pancreas and in 8 cell lines of ductal human pancreatic cancer. Furthermore, adhesion assays on purified extracellular matrix (ECM)\u2010compounds were used to define the function of \u03b1<jats:sub>2<\/jats:sub>, \u03b1<jats:sub>3<\/jats:sub>, \u03b1<jats:sub>5<\/jats:sub> and \u03b1<jats:sub>6<\/jats:sub>in pancreatic cancer cells. Immunohistochemically, VLA \u03b1<jats:sub>2<\/jats:sub> and VLA \u03b1<jats:sub>6<\/jats:sub> were moderately to strongly expressed on the basal surface of ductal and acinar cells in normal pancreatic tissue, while centro\u2010acinar cells predominantly expressed VLA \u03b1<jats:sub>3<\/jats:sub> and VLA \u03b1<jats:sub>5<\/jats:sub>. Pancreatic carcinoma showed intense staining for VLA \u03b1<jats:sub>2<\/jats:sub> and VLA \u03b1<jats:sub>6<\/jats:sub> with a diffuse distribution on the cell surface. The redistribution of VLA \u03b1<jats:sub>2<\/jats:sub> and VLA \u03b1<jats:sub>6<\/jats:sub> may reflect a loss of spatial arrangement of tumor cells and their ability to interact randomly with extracellular matrix structures during invasion and metastasis. Expression of VLA \u03b1<jats:sub>3<\/jats:sub> and VLA \u03b1<jats:sub>5<\/jats:sub> in pancreatic carcinoma was heterogeneous, ranging from moderate to weak, and was lost in about 50% of the cells. Two pancreatic carcinoma cell lines (PC 3, PC 44) were further investigated in adhesion assays. Monoclonal antibodies (MAbs) against \u03b1<jats:sub>2<\/jats:sub> (Gl 9, 10\u2010G\u201011) were able to inhibit tumor\u2010cell adhesion to collagen IV (59%\u201072%) in both cell lines. A MAb against \u03b1<jats:sub>6<\/jats:sub> (GoH<jats:sub>3<\/jats:sub>) inhibited tumor\u2010cell adhesion to laminin (52%\u201086%) in both cell lines. These results suggest that \u03b1<jats:sub>2<\/jats:sub> is a collagen\u2010binding site and \u03b1<jats:sub>6<\/jats:sub> a laminin\u2010binding site in pancreatic cancer cells. The anti\u2010\u03b1<jats:sub>5<\/jats:sub>\u2010MAb SAM I inhibited adhesion of PC3 to fibronectin (76%), being without effect in PC44. Adhesion of both cell lines to fibronectin was almost completely inhibited by RGDS (85%\u201088%). Thus, \u03b1<jats:sub>5<\/jats:sub>is a functionally important fibronectin binding site in some pancreatic carcinoma cells, suggesting further RGD\u2010dependent fibronectin binding sites in other pancreatic carcinoma cells. \u00a9 1992 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/ijc.2910520526","type":"journal-article","created":{"date-parts":[[2007,2,19]],"date-time":"2007-02-19T22:48:04Z","timestamp":1171925284000},"page":"827-833","source":"Crossref","is-referenced-by-count":64,"title":["Expression and function of VLA\u2010\u03b1<sub>2<\/sub>, \u2010\u03b1<sub>3<\/sub>, \u2010\u03b1<sub>5<\/sub> and \u2010\u03b1<sub>6<\/sub>\u2010integrin receptors in pancreatic carcinoma"],"prefix":"10.1002","volume":"52","author":[{"given":"R. J.","family":"Weinel","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.","family":"Rosendahl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K.","family":"Neumann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B.","family":"Chaloupka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D.","family":"Erb","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M.","family":"Rothmund","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S.","family":"Santoso","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,7,17]]},"reference":[{"key":"e_1_2_1_2_1","first-page":"17","article-title":"Establishment and characterization of continuous tumor cell lines from human pancreatic carcinomain vitro","volume":"25","author":"Bulow M.","year":"1982","journal-title":"Digestion"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.2011740"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.111.6.2795"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1177\/32.2.6198355"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.86.24.9906"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.112.1.169"},{"key":"e_1_2_1_8_1","doi-asserted-by":"crossref","unstructured":"Elsasser H. 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