Abstract:
:We have previously characterized the expression of the alpha nu beta 5 and alpha nu beta 6 integrins as major receptors for the human colonic adenocarcinoma cell line (HT29-D4), on vitronectin and fibronectin, respectively [Lehmann et al. (1994): Cancer Res 54:2102-2107]. In the present work we investigated the glycosylation role of these integrins in their adhesive functions. To this end, we used glycohydrolases to show that cell surface integrins were N-glycosylated and sialylated, and that only the alpha v subunit carried some immature oligosaccharide side chains. To alter the glycosylation state of the cell surface alpha v beta 5 and alpha v beta 6 integrins, we used two oligosaccharide-processing inhibitors: 1-deoxymannojirimycin (dMNJ) and tunicamycin (TM). Following treatment of HT29-D4 cells with dMNJ, cell surface alpha v beta 5 and alpha v beta 6 carried only high-mannose-type sugar chains, while TM-treated cells expressed de-N-glycosylated integrins. Neither alpha/beta heterodimers assembly nor cell surface expression were impaired in the presence of the drugs. Finally, we established that adhesion of dMNJ- or TM-treated cells was altered on both vitronectin and fibronectin substrata, whereas the adhesion of these cells on laminin or collagen type I was virtually unchanged.
journal_name
J Cell Biochemjournal_title
Journal of cellular biochemistryauthors
Lehmann M,El Battari A,Abadie B,Martin JM,Marvaldi Jdoi
10.1002/(sici)1097-4644(19960501)61:2<266::aid-jcbsubject
Has Abstractpub_date
1996-05-01 00:00:00pages
266-77issue
2eissn
0730-2312issn
1097-4644pii
10.1002/(SICI)1097-4644(19960501)61:2<266::AID-JCBjournal_volume
61pub_type
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