1989
DOI: 10.1016/0006-291x(89)90837-1
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Multiple forms of SppI (secreted phosphoprotein, osteopontin) synthesized by normal and transformed rat bone cell populations: Regulation by TGF-β

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Cited by 97 publications
(50 citation statements)
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“…Although phosphorylation of OPN and BSP is believed to occur intracellularly, as demonstrated previously in bone cell cultures with $#PO % $− as a substrate [12,15], our previous studies of purinergic receptors in bone cells, including the UMR 106.06 cell line (L. C. Luo, H. Yu and J. Ferrier, unpublished work), have indicated the presence of ectokinase activity. Similarly, ectokinase activity has been demonstrated in neonatal rat calvarial bone cell populations [18], confirming an earlier observation of an extracellular enzyme in bone that could catalyse the transfer of phosphoryl groups from ATP to protein within the bone matrix [50].…”
Section: Discussionsupporting
confidence: 57%
See 1 more Smart Citation
“…Although phosphorylation of OPN and BSP is believed to occur intracellularly, as demonstrated previously in bone cell cultures with $#PO % $− as a substrate [12,15], our previous studies of purinergic receptors in bone cells, including the UMR 106.06 cell line (L. C. Luo, H. Yu and J. Ferrier, unpublished work), have indicated the presence of ectokinase activity. Similarly, ectokinase activity has been demonstrated in neonatal rat calvarial bone cell populations [18], confirming an earlier observation of an extracellular enzyme in bone that could catalyse the transfer of phosphoryl groups from ATP to protein within the bone matrix [50].…”
Section: Discussionsupporting
confidence: 57%
“…In comparison, OPN, which is expressed later than BSP, binds rapidly to pre-existing crystals [12,13] and will inhibit crystal growth, the efficacy of the inhibition being dependent on the presence of phosphate groups [14]. Previous studies using $#PO % $− labelling have shown that phosphorylation of BSP and OPN occurs intracellularly [12,13,15], primarily through a casein kinase II-like enzyme [16].…”
Section: Introductionmentioning
confidence: 99%
“…Breast milk has also been shown to contain highly phosphorylated OPN (37). OPN is usually secreted in both nonphosphorylated and phosphorylated forms (5,16,35,37). In the present study, we did not elucidate which form of OPN was secreted from P. marneffei-stimulated PBMCs, because the ELISA used recognizes both.…”
Section: Fig 4 Failure Of Anti-tnf-␣ and -Il-1rimentioning
confidence: 79%
“…In addition to osteoblasts, preosteoblasts, osteocytes as well as other haemopoietic cells, also synthesise Opn within the BM (Mark et al, 1987a(Mark et al, ,b, 1988Swanson et al, 1989). Opn does not appear to be synthesised by mesenchymal cells or fibroblasts in vivo (Butler, 1989). Opn is thought to be a single protein coded by a single gene (Smith & Denhardt, 1987;Swanson et al, 1989), but through phosphorylation, glycosylation and proteolytic cleavage, various molecular masses of Opn can be detected, ranging from 25 to 75 kDa.…”
Section: Osteopontinmentioning
confidence: 99%
“…Opn is secreted in non-phosphorylated (Kubota et al, 1989;Chambers et al, 1992;Chang & Prince, 1993;Barber et al, 1999) and phosphorylated (Salih et al, 1995(Salih et al, , 1997Sorensen et al, 1994) forms, which contains up to 28 phosphate residues and are differentially induced by cytokines. Phosphorylation appears to be functionally important in determining whether Opn binds to cell surface receptors or the extracellular matrix (Nemir et al, 1989;Ek-Rylander et al, 1994).…”
Section: Osteopontinmentioning
confidence: 99%