Bone morphogenetic protein (BMP)-2 enhances the expression of type II collagen and aggrecan in chondrocytes embedded in alginate beads

Gründer, Tatiana; Gaissmaier, Christoph; Fritz, Jürgen; Stoop, Reinout; Hortschansky, Peter; Mollenhauer, Jürgen; Aicher, Wilhelm K.

doi:10.1016/j.joca.2004.04.001

Cited by 178 publications

(122 citation statements)

References 28 publications

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“…The concentrations of recombinant human sema3A used in the present study were selected according to these previous studies. Type II collagen produced by cells is incorporated into the extracellular matrix (11,12). However, in the present study, type II collagen was not detected in cells and matrix, nevertheless type II collagen was digested by pepsin and elastase for solubilizing collagen.…”

Section: Discussioncontrasting

confidence: 68%

“…The cells and extracellular matrices were also assayed for concentrations of type II collagen using an enzyme immunoassay kit (Type II Collagen Detection kit; Chondrex, Inc., Redmond, WA, USA) as previously described (11,12). In accordance with the manufacturer's protocol, the cells and extracellular matrices were solubilized by pepsin digestion (at 4˚C for 24 h) and elastase digestion (at 4˚C for 24 h) prior to with the assay.…”

Section: Methodsmentioning

confidence: 99%

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PLXNA2 identified as a candidate gene by genome-wide association analysis for mandibular prognathism in human chondrocytes

et al. 2018

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Abstract. In a previous genome-wide association study, plexin A2 (PLXNA2) was suggested as one of the candidate genes for mandibular prognathism. PLXNA2 encodes plexin A2, a member of the plexin-A family of semaphorin co-receptors. Semaphorin 3A (sema3A) exerts an osteoprotective effect. However, to the best of our knowledge, there have been no previous studies examining the role of sema3A or plexin A2 on human chondrocytes. The objectives of the present study were to examine the function of sema3A and its receptor, plexin A2, in human chondrocytes. Normal human chondrocytes were cultured in media with either a high (100 ng/ml) or a low (1 ng/ml) concentration of sema3A, or without sema3A as a control. Cells and extracellular matrices were assayed for concentrations of protein and parathyroid hormone-related peptide receptor 1 (PTH-R1) using a bicinchoninic acid assay and an enzyme immunoassay, respectively. At culture day 7, the high and low concentrations of exogenous sema3A significantly increased the protein content compared with the control (P=0.0008 and 0.00002, respectively). At culture day 14, a high concentration of exogenous sema3A significantly increased the protein content and decreased the concentration of PTH-R1 compared with the control (P=0.002). The present study revealed novel results that exogenous sema3A suppresses the expression of PTH-R1 in human proliferative chondrocytes and suggested that sema3A may affect human chondrocytes via its receptor, plexin A2.

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Section: Discussioncontrasting

confidence: 68%

Section: Methodsmentioning

confidence: 99%

PLXNA2 identified as a candidate gene by genome-wide association analysis for mandibular prognathism in human chondrocytes

et al. 2018

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“…In osteoarthritis cartilage, the expression of BMP-2 is significantly increased (12, 15), possibly through the induction by the proinflammatory cytokines (12). Because the protein has potent anabolic actions on chondrocytes (62,63), it is possible that the induced BMP-2 counteracts the progression of the disease by enhancing the chondrocyte metabolism. In fact, the result of this study indicated a possibility that BMP-2, after induction by TNF-␣, could compensate the reduced chondrocyte metabolism caused by the cytokine (Fig.…”

Section: Discussionmentioning

confidence: 99%

Pro-inflammatory Cytokine Tumor Necrosis Factor-α Induces Bone Morphogenetic Protein-2 in Chondrocytes via mRNA Stabilization and Transcriptional Up-regulation

Fukui

Ikeda

Ohnuki

et al. 2006

Journal of Biological Chemistry

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In articular chondrocytes, the inflammatory cytokine tumor necrosis factor-␣ (TNF-␣) induces the expression of bone morphogenetic protein-2 (BMP-2), a growth factor known to be involved in the induction of cartilage and bone. A study was performed to clarify the mechanism(s) underlying the induction of BMP-2 in chondrogenic ATDC5 cells and primary cultured adult human articular chondrocytes. In ATDC5 cells, the endogenous BMP-2 expression was consistently low throughout the process of chondrogenic differentiation, and TNF-␣ induced BMP-2 expression only after the cells acquired the chondrogenic phenotype. The results of nuclear run-off assay and cycloheximide treatment consistently indicated that ATDC5 cells acquire the capacity to synthesize BMP-2 mRNA in the nuclei during the differentiation process. In an attempt to explain the discrepancy between the active nuclear mRNA synthesis and the observed low expression level in differentiated ATDC5 cells, the stability of BMP-2 mRNA was evaluated, and the cells were found to regulate the expression of BMP-2 at the post-transcriptional level. Human chondrocytes were confirmed to have a similar post-transcriptional regulation. The result of 3-rapid amplification of cDNA end revealed that both human and mouse BMP-2 mRNAs contain multiple pentameric AUUUA motifs in a conserved manner in the 3-untranslated regions, and transient transfection experiments demonstrated that TNF-␣ increases the stability of BMP-2 mRNA through the pentameric motifs. Further experiments revealed that TNF-␣ modulates mRNA stability via p38 signal transduction pathway, whereas the cytokine also augmented the expression of BMP-2 through transcriptional up-regulation via the transcriptional factor NF-B.

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“…Nevertheless, addition of fusion tags was in context of BMPs employed mostly for protein purification (histag [91], maltose binding protein [92]), or detection and enrichment purposes [93,94], and only in a few cases designed to enable a more permanent immobilization on scaffolds. Insertion of any kind of tag within the mature part of thr BMP sequence is strongly restricted to the N-terminus, which is caused by the buried architecture of its C-terminal end.…”

Section: Delivery Of Bmp-2 Utilizing Affinity Interactionsmentioning

confidence: 99%

How to use BMP-2 for clinical applications? A review on pros and cons of existing delivery strategies

Mumcuoglu¹,

Siverino²,

Tabisz³

et al. 2017

J Transl Sci

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Bone morphogenetic protein (BMP)-2 enhances the expression of type II collagen and aggrecan in chondrocytes embedded in alginate beads

Abstract: We conclude that chondrocytes during expansion for ACT may benefit from BMP-2 activation only when seeded in an appropriate 3D culture system.

Cited by 178 publications

References 28 publications

PLXNA2 identified as a candidate gene by genome-wide association analysis for mandibular prognathism in human chondrocytes

PLXNA2 identified as a candidate gene by genome-wide association analysis for mandibular prognathism in human chondrocytes

Pro-inflammatory Cytokine Tumor Necrosis Factor-α Induces Bone Morphogenetic Protein-2 in Chondrocytes via mRNA Stabilization and Transcriptional Up-regulation

How to use BMP-2 for clinical applications? A review on pros and cons of existing delivery strategies

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