Abstract:
:Osteopontin is a secreted glycoprotein with adhesive and migratory functions. Cellular interactions with osteopontin are mediated through integrin receptors which recognize the RGD domain. Recently, CD44, a non-integrin, multifunctional adhesion molecule was identified as an osteopontin receptor. CD44 is a ubiquitous surface molecule that exists as a number of different isoforms, generated by alternative splicing. To analyze which forms of CD44 mediate binding to osteopontin, we used the standard form of CD44 as CD44-human immunoglobulin fusion proteins and several splice variants in enzyme-linked immunosorbant assays. Multiple preparations of osteopontin were used including native osteopontin derived from smooth muscle cells, human urinary osteopontin, full-length recombinant osteopontin, and two recombinant osteopontin fragments expected to be formed following thrombin cleavage. Our data show that although the CD44-hlg fusion proteins could interact with hyaluronic acid as expected, there was no interaction between CD44H, CD44E, CD44v3,v8-v10, or CD44v3 with osteopontin. These studies suggest that CD44-osteopontin interactions may not be common in vivo and may be limited to a specific CD44 isoform(s), and/or a particular modified form of osteopontin.
journal_name
J Cell Biochemjournal_title
Journal of cellular biochemistryauthors
Smith LL,Greenfield BW,Aruffo A,Giachelli CMdoi
10.1002/(sici)1097-4644(19990401)73:1<20::aid-jcb3subject
Has Abstractpub_date
1999-04-01 00:00:00pages
20-30issue
1eissn
0730-2312issn
1097-4644pii
10.1002/(SICI)1097-4644(19990401)73:1<20::AID-JCB3journal_volume
73pub_type
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