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Review
. 2017 Jun;39(6):1327-1337.
doi: 10.3892/ijmm.2017.2964. Epub 2017 Apr 21.

Human osteopontin: Potential clinical applications in cancer (Review)

Chengcheng Hao  1 , Yuxin Cui  2 , Sionen Owen  2 , Wenbin Li  3 , Shan Cheng  1 , Wen G Jiang  1
Affiliations
Review

"VSports手机版" Human osteopontin: Potential clinical applications in cancer (Review)

Chengcheng Hao et al. Int J Mol Med. 2017 Jun.

V体育平台登录 - Abstract

Human osteopontin (OPN) is a glycosylated phosphoprotein which is expressed in a variety of tissues in the body. In recent years, accumulating evidence has indicated that the aberrant expression of OPN is closely associated with tumourigensis, progression and most prominently with metastasis in several tumour types. In this review, we present the current knowledge on the expression profiles of OPN and its main splice variants in human cancers, as well as the potential implications in patient outcome VSports手机版. We also discuss its putative clinical application as a cancer biomarker and as a therapeutic target. .

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Figures

Figure 1
Figure 1
Structural features of the three osteopontin (OPN) splice variants. OPN-a is the full-length isoform with 6 translated exons (314 aa), OPN-b lacks exon 5 (300 aa), and OPN-c lacks exon 4 (287 aa). All OPN variants possess functional domains: arginine-glycine-aspartic acid (RGD) domain (159–161), serine-valine-valine-tyrosine-glutamate-leucine-arginine (SVVYGLR) domain (162–168), thrombin cleavage site, calcium binding domain (216–228) and heparin binding domain. Integrin binding occurs at RGD and SVVYGLR sequences, whilst the CD44 variant receptor binding occurs near the C-terminus. Phosphorylation sites are throughout the whole precusor-mRNA (pre-mRNA). Thrombin cleavage and matrix metalloproteinase (MMP) cleavage sites are present in all three splice variants. Compared with the full-length isoform (OPN-a), OPN-b misses certain phosphorylation sites, while OPN-c is unable to undergo transglutaminase cross-linking. To some extent, the structural differences that exist between the three OPN isoforms may contribute to their clinical and functional differences.
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