Rat tibial osteoblasts III: Propagation in vitro is accompanied by enhancement of osteoblast phenotype

Manduca, Paola; Palermo, Claudia; Caruso, C.; Brizzolara, Antonella; Sanguineti, C.; Filanti, C.; Zicca, A

doi:10.1016/s8756-3282(97)00037-9

Cited by 16 publications

(20 citation statements)

References 29 publications

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“…Similar to the bone-specific OC gene, BSP mRNA is upregulated in concert with the active deposition of minerals (36,41,43,45,57). However, BSP is temporally expressed earlier than OC during development of the osteoblast phenotype and is downregulated in mature osteocytes (8,23,35,57,60).…”

Section: Discussionmentioning

confidence: 99%

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runt Homology Domain Transcription Factors (Runx, Cbfa, and AML) Mediate Repression of the Bone Sialoprotein Promoter: Evidence for Promoter Context-Dependent Activity of Cbfa Proteins

Javed

Barnes

Jasanya

et al. 2001

Molecular and Cellular Biology

171

100

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Bone sialoprotein (BSP) is a phosphorylated and sulfated 34-kDa protein that represents one of the major noncollagenous, extracellular matrix (ECM) proteins associated with mineralized tissues. In developing rat calvaria, BSP mRNA expression is detected in osteoblasts on day 17 along with type I collagen, osteocalcin (OC), osteonectin, and alkaline phosphatase. BSP expression is also found in hypertrophic chondrocytes (8). BSP, similar to OC, is upregulated during osteoblast differentiation in vitro as the ECM mineralizes. BSP reaches peak levels slightly earlier than OC and is downregulated in mature osteocytes (14,35,36,39,43). The protein is selectively associated with clusters of needle-like crystals of hydroxyapatite. Various in vitro studies suggest that BSP can either promote mineral nucleation or facilitate mineral growth (22). In other studies the functional role of this protein was assessed by stably transfecting murine osteosarcoma cell lines with avian forms of this gene (15). The results demonstrated that the cell lines expressing the highest levels of BSP displayed the greatest accumulation of calcium in the ECM, consistent with BSP binding to hydroxyapatite (5,12).Regulatory elements in the BSP promoter that contribute to its high level of transcription in osteoblasts have not been identified. BSP promoters from several species have been shown to contain a negative vitamin D response element (33), an inverted TATA sequence, a YY1 motif (28), several Sp1 sites, and a homeodomain (engrailed) motif in the proximal promoter (59), but none of these has been demonstrated to mediate tissue-specific expression. The OC promoter, however, has provided examples of several elements that contribute to its osteoblast-specific expression. The OC box I and homeodomain (Msx or Dlx) binding site (20, 21, 56) both restricts and attenuates OC expression in developing osteoblasts. Most significantly, multiple Cbfa (core binding factor ␣) sites in the various OC promoters support cell type-specific expression, and forced expression of Cbfa factors can confer induction of OC promoter-reporter constructs in both osseous and nonosseous cells (1,11,25). Cbfa1 has been shown to be a key regulator of osteogenic differentiation (2, 31, 42) and regulates several osteoblast-related genes. The Gallus BSP promoter has been sequenced (59) and contains multiple Cbfa consensus motifs. Several important observations prompted examination of the functionality of these putative Cbfa sites. Firstly, the Cbfa1 null mutant revealed loss of BSP expression, along with other osteoblast phenotypic markers (31). Secondly, the similarities between BSP and OC with respect to their high expression levels restricted to mineralized tissues in vivo and in vitro suggest that

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Section: Discussionmentioning

confidence: 99%

“…BSP, similar to OC, is upregulated during osteoblast differentiation in vitro as the ECM mineralizes. BSP reaches peak levels slightly earlier than OC and is downregulated in mature osteocytes (14,35,36,39,43). The protein is selectively associated with clusters of needle-like crystals of hydroxyapatite.…”

mentioning

confidence: 99%

runt Homology Domain Transcription Factors (Runx, Cbfa, and AML) Mediate Repression of the Bone Sialoprotein Promoter: Evidence for Promoter Context-Dependent Activity of Cbfa Proteins

Javed

Barnes

Jasanya

et al. 2001

Molecular and Cellular Biology

171

100

View full text Add to dashboard Cite

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“…Moreover, BSP acts as a nucleator for mineralization in bone [80]. Cell growth on collagen gels acts by inducing rapid differentiation of osteoblastic cells [75]. Thus, the enhancement of Col-1 formation in the extracellular matrix could be interpreted as an indicator of the osteoblast differentiation process reported here.…”

Section: Discussionmentioning

confidence: 62%

“…Furthermore, changes in the extracellular matrix trigger the pathways that affect growth and phenotype differentiation [75]. The cells cultivated on various materials examined here showed an enhanced production of OC, BSP and Col-1 with the exception of Ti cp and Cercon.…”

Section: Discussionmentioning

confidence: 81%

Ti-SLActive and TiZr-SLActive Dental Implant Surfaces Promote Fast Osteoblast Differentiation

et al. 2017

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A primary goal in modern surface modification technology of dental implants is to achieve biocompatible surfaces with rapid but controlled healing which also allow health and longevity of implants. In order to realize all, understanding of osseointegration phenomena is crucial. Although Ti-SLA, Ti-SLActive and TiZr-SLActive surfaces have been successfully used in clinical implantology and were shown to notably reduce the primary healing time, available in vitro studies are sparse and do not concern or explore the mechanism(s) involved in human osteoblast behavior on these surfaces. Ti-SLA, Ti-SLActive, TiZr-SLActive, Ti cp, Ticer and Cercon surfaces were used. Osteoblast proliferation, cell cluster formation, morphological changes, induction of autophagy, nitric oxide (NO), reactive oxygen species/reactive nitrogen species (ROS/RNS) formation, osteocalcin (OC), bone sialoprotein (BSP) and collagen type I (Col-1) affected by various surfaces were analyzed. These surfaces induced formation of mature osteoblasts caused by elevated oxidative stress (ROS) followed by overexpression of osteoblast maturation key molecule (NO), with different intensity however. These mature osteoblasts induced upregulation of OC, BSP and Col-1, activating PI3/Akt signalling pathway resulting in autophagy, known as an important process in differentiation of osteoblast cells. Additional distinctive subpopulation identified on Ticer, Ti-SLA (after 5 days), Ti-SLActive and TiZr-SLActive surfaces (after 2 days) were forming cell clusters, essential for bone noduli formation and mineralisation. The results suggest that Ti-and TiZr-SLActive possess advanced properties in comparison with Ticer and Ti-SLA manifested as accelerated osteoblast differentiation. These effects could explain already known fast osseointegration of these surfaces in vivo.

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“…Cultures at 46 -70 cumulative population doublings were utilized for the preparation of conditioned medium in differentiation medium (100 g/ml ascorbic acid and 10 mM ␤-glycerophosphate) (53). MDA MB231, MDA MB435, MCF-7, and ZR75.1 breast cancer cell line (courtesy of Prof. S. Toma, Università di Genova, Italy) and endothelial cells, EA hy926, were cultured in Dulbecco's modified Eagle's medium, 10% FCS.…”

Section: Methodsmentioning

confidence: 99%

Pro-collagen I COOH-terminal Trimer Induces Directional Migration and Metalloproteinases in Breast Cancer Cells

Palmieri¹,

Poggi²,

Ulivi³

et al. 2003

Journal of Biological Chemistry

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Breast and prostatic carcinomas, melanoma, and endothelial cell lines are chemoattracted by medium conditioned by mature osteoblasts. The chemoattractant for endothelial cells was identified with C3, carboxyl-terminal trimer of pro-collagen type I. We report that C3 induces directional migration and proliferation, the expression of tissue inhibitor of metalloproteinases-2, prometalloproteinase-2 and -9, and their activation in MDA MB231 cells, without changing the expression of tissue inhibitor of metalloproteinases-1 and of metalloproteinase-14. Antiserum against metalloproteinase-2 or -9 or -14, tissue inhibitor of metalloproteinases-1, or GM6001 inhibits the C3-induced migration. Urokinase and its receptor are detected and unchanged upon exposure to C3. The antibody against urokinase or addition of plasminogen activator inhibitor inhibits migration. Blocking antibodies to integrins ␣ 2 , ␣ 6 , ␤ 1 , and ␤ 3 inhibit chemotaxis and do not change urokinase and urokinase receptor expression. Blockage of ␣ 2 , ␤ 1 , and ␤ 3 integrins affect differently the induction by C3 of pro-metalloproteinase-2 and -9 and of tissue inhibitor of metalloproteinases-2. Chemotaxis to C3 is also inhibited by genistein, by pertussis toxin, which also inhibits C3-induced pro-metalloproteinase -2 and -9, but not urokinase expression. Wortmannin partially inhibits C3-induced cell migration. Other, but not all, breast carcinoma lines tested responded to C3 with migration and pro-metalloproteinase-2 induction. Presently C3 is the only agent known to induce migration specifically of both endothelial and breast carcinoma cells. The mitogenic and motogenic role of C3 in vitro might prefigure a role in in vivo carcinogenesis and in the establishment of metastasis.Mature osteoblasts conditioned medium (CM), 1 collected when sustained biosynthesis of collagen type I occurs during osteogenesis in vitro from differentiating cultures of rat, rabbit, human osteoblasts, and conditionally transformed human osteoblast-like line HFO, induces directional migration of endothelial and melanoma and breast and prostatic carcinoma cells but not of normal cells or of transformed mesenchymal cells in the classical in vitro double chamber Boyden assay (1-4).The molecule chemoattractant for endothelial cells was purified from rat osteoblast CM, and it identifies by sequence, immunoreactivity, and molecular size with the trimer carboxylterminal of type I pro-collagen, C3 (4). C3 is a by-product of the processing of pro-collagen by pro-collagenase C (or BMP-1), preliminary to the formation of collagen fibrils (5).We investigated whether MDA MB231 breast carcinoma cells, which are stimulated by mature osteoblasts CM to directional migration, are induced by C3 to activate migratory and proliferation responses. It is recognized that the stroma of the tumors plays instructive and active roles toward tumor cells growth and invasiveness and that tumor-associated stromal fibroblasts undergo changes in the biosynthetic phenotype (6), assume the production of factors supp...

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Rat tibial osteoblasts III: Propagation in vitro is accompanied by enhancement of osteoblast phenotype

Cited by 16 publications

References 29 publications

runt Homology Domain Transcription Factors (Runx, Cbfa, and AML) Mediate Repression of the Bone Sialoprotein Promoter: Evidence for Promoter Context-Dependent Activity of Cbfa Proteins

runt Homology Domain Transcription Factors (Runx, Cbfa, and AML) Mediate Repression of the Bone Sialoprotein Promoter: Evidence for Promoter Context-Dependent Activity of Cbfa Proteins

Ti-SLActive and TiZr-SLActive Dental Implant Surfaces Promote Fast Osteoblast Differentiation

Pro-collagen I COOH-terminal Trimer Induces Directional Migration and Metalloproteinases in Breast Cancer Cells

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