Human Osteoclast Formation from Blood Monocytes, Peritoneal Macrophages, and Bone Marrow Cells

1998 ◽  
Vol 62 (6) ◽  
pp. 527-531 ◽  
Author(s):  
J. M. W. Quinn ◽  
S. Neale ◽  
Y. Fujikawa ◽  
J. O. D. McGee
Keyword(s):  
Bone Marrow ◽  
Bone Marrow Cells ◽  
Peritoneal Macrophages ◽  
Osteoclast Formation ◽  
Blood Monocytes ◽  
Human Osteoclast ◽  
Marrow Cells

scholarly journals Observations on the binding and interaction of radioiodinated colony- stimulating factor with murine bone marrow cells in vivo

Blood ◽  
1982 ◽  
Vol 59 (2) ◽  
pp. 408-420 ◽  
Author(s):  
G Pigoli ◽  
A Waheed ◽  
RK Shadduck
Keyword(s):  
Bone Marrow ◽  
Bone Marrow Cells ◽  
Marrow Cell ◽  
Cell Interaction ◽  
Peritoneal Macrophages ◽  
Colony Stimulating Factor ◽  
Murine Bone Marrow ◽  
Stimulating Factor ◽  
Marrow Cells

Abstract Radioiodinated L-cell-derived colony-stimulating factor (CSF) was used to characterize the binding reaction to murine bone marrow cells. The major increment in cell-associated radioactivity occurred over 24 hr incubation at 37 degrees C, but virtually no binding was observed at 4 degrees C. The reaction was saturable with approximately 1 ng/ml of purified CSF. Unlabeled CSF prevented the binding, whereas a number of other hormones and proteins did not compete for CSF uptake. Further specificity studies showed virtually no binding to human bone marrow, which is unresponsive to this form of murine CSF. Minimal CSF uptake was noted with murine peritoneal macrophages, but virtually no binding was detected with thymic, lymph node, liver, or kidney cells. The marrow cell interaction with tracer appeared to require a new protein synthesis, as the binding was prevented by cycloheximide or puromycin. Preincubation of marrow cells in medium devoid of CSF increased the degree of binding after 1 hr exposure to the tracer. This suggests that CSF binding sites may be occupied or perhaps decreased in response to ambient levels of CSF in vivo. Approximately 70% of the bound radioactivity was detected in the cytoplasm at 24 hr. This material was partially degraded as judged by a decrease in molecular weight from approximately 62,000 to 2 peaks of approximately 32,000 and approximately 49,000, but 72% of the binding activity was retained. After plateau binding was achieved, greater than 80% of the radioactivity released into the medium was degraded into biologically inactive peptides with molecular weights less than 10,000. These findings suggest that the interaction of CSF with marrow cells is characterized by binding with subsequent internalization and metabolic degradation into portions of the molecule that are devoid of biologic activity.

scholarly journals Jun Dimerization Protein 2 (JDP2), a Member of the AP-1 Family of Transcription Factor, Mediates Osteoclast Differentiation Induced by RANKL

2003 ◽  
Vol 197 (8) ◽  
pp. 1029-1035 ◽  
Author(s):  
Reimi Kawaida ◽  
Toshiaki Ohtsuka ◽  
Junichi Okutsu ◽  
Tohru Takahashi ◽  
Yuho Kadono ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Bone Marrow Cells ◽  
Osteoclast Differentiation ◽  
Osteoclast Formation ◽  
Raw264.7 Cells ◽  
Tartrate Resistant Acid Phosphatase ◽  
Gene Promoters ◽  
Primary Bone ◽  
Primary Bone Marrow ◽  
Marrow Cells

Osteoclasts are multinucleated cells that resorb bones, and are derived from hematopoietic cells of the monocyte/macrophage lineage. The receptor activator of NF-κB ligand (RANKL, also called ODF/TRANCE/OPGL) stimulates both osteoclast differentiation from osteoclast progenitors and activation of mature osteoclasts. To identify genes responsible for osteoclast differentiation, we used a molecular indexing technique. Here, we report a clone of one of these genes whose transcription is induced by soluble RANKL (sRANKL) in both the RAW264.7 cells of the mouse macrophage cell line and the mouse primary bone marrow cells. The predicted protein was found to be a mouse homologue of Jun dimerization protein 2 (JDP2), a member of the AP-1 family of transcription factors, containing a basic region-leucine zipper motif. Transient transfection experiments revealed that overexpression of JDP2 leads to activation of both tartrate-resistant acid phosphatase (TRAP) and cathepsin K gene promoters in RAW264.7 cells. Infection of mouse primary bone marrow cells with retroviruses expressing JDP2-facilitated sRANKL-mediated formation of TRAP-positive multinuclear osteoclasts. Importantly, antisense oligonucleotide to JDP2 strongly suppressed sRANKL-induced osteoclast formation of RAW264.7 cells. Our findings suggest that JDP2 may play an important role in the RANK-mediated signal transduction system, especially in osteoclast differentiation.

Reversibility of alendronate-induced contraction in human osteoclast-like cells formed from bone marrow cells in culture

1999 ◽  
Vol 17 (2) ◽  
pp. 98-107 ◽  
Author(s):  
Yasuko Koshihara ◽  
Shunji Kodama ◽  
Hideaki Ishibashi ◽  
Yoshiaki Azuma ◽  
Tomohiro Ohta ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Bone Marrow Cells ◽  
Cells In Culture ◽  
Human Osteoclast ◽  
Marrow Cells

Vitamin D antagonist, TEI-9647, inhibits osteoclast formation induced by 1α,25-dihydroxyvitamin D3 from pagetic bone marrow cells

2004 ◽  
Vol 89-90 ◽  
pp. 331-334 ◽  
Author(s):  
Seiichi Ishizuka ◽  
Noriyoshi Kurihara ◽  
Daishiro Miura ◽  
Kazuya Takenouchi ◽  
Jillian Cornish ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Vitamin D ◽  
Bone Marrow Cells ◽  
Osteoclast Formation ◽  
Dihydroxyvitamin D3 ◽  
Pagetic Bone ◽  
Marrow Cells

Abstract 2: Loss of Rictor in Macrophages Suppresses Their Viability and Reduces Atherosclerosis in LDLR Null Mice

2016 ◽  
Vol 36 (suppl_1) ◽  
Author(s):  
Vladimir R Babaev ◽  
Lei Ding ◽  
Youmin Zhang ◽  
James M May ◽  
MacRae F Linton
Keyword(s):  
Gene Expression ◽  
Bone Marrow ◽  
Blood Cells ◽  
Inflammatory Responses ◽  
Bone Marrow Cells ◽  
White Blood Cells ◽  
Mammalian Target Of Rapamycin ◽  
Peritoneal Macrophages ◽  
Blood Monocytes ◽  
Glucose Plasma

The mammalian target of rapamycin (mTOR) is a conserved serine/threonine kinase that plays a central role in the regulation of cell viability, growth and metabolism. mTOR complex 2 (mTORC2) directly activates phosphorylation of Akt at S 473 , promoting pro-survival signaling. Rictor is an essential component of mTORC2, and genetic loss of Rictor inactivates the complex. To examine whether macrophage mTORC2 signaling has an impact on atherosclerosis, we transplanted male Ldlr null mice with bone marrow isolated from male mice with myeloid-specific Rictor deletion ( Rictor -/- , n=9) and control marrow from Rictor flox-flox mice ( Rictor flox/flox ; n=10). Compared to control mice reconstituted with Rictor flox/flox cells, the recipients of Rictor -/- bone marrow cells exhibited dramatic changes in blood cells including lower levels of white blood cells, B-cells, T-cells and monocytes but had similar levels of neutrophils. After 8 weeks of the Western diet, both groups of recipients had similar levels of body weight, blood glucose, plasma total cholesterol and triglycerides. However, Rictor -/- → Ldlr -/- mice developed smaller atherosclerotic lesions in the proximal and distal aorta (46 and 40% reduction, respectively). These lesions contained less macrophage area and more apoptotic macrophages than lesions of control Rictor flox/flox → Ldlr -/- mice. Importantly, blood monocytes and peritoneal macrophages isolated from Rictor -/- → Ldlr -/- mice were more sensitive to apoptotic stimuli compared to control Rictor flox/flox cells. In response to LPS, Rictor -/- macrophages exhibited the M1 phenotype with high levels of pro-inflammatory gene expression. Both Rictor -/- blood monocytes and macrophages had lower levels of Il10 gene expression than Rictor flox/flox cells. Thus, loss of Rictor and, consequently, mTORC2 in monocyte/macrophages significantly compromises their survival, and this markedly diminishes early atherosclerosis in Ldlr -/- mice. Our results indicate that mTORC2 is a key signaling regulator of macrophage survival and inflammatory responses and promote atherosclerosis.

IL-18 induces apoptosis of adherent bone marrow cells in TNF-α mediated osteoclast formation in synergy with IL-12

2006 ◽  
Vol 107 (1) ◽  
pp. 22-31 ◽  
Author(s):  
Hideki Kitaura ◽  
Mutsuhito Tatamiya ◽  
Noriko Nagata ◽  
Yuji Fujimura ◽  
Toshiko Eguchi ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Bone Marrow Cells ◽  
Osteoclast Formation ◽  
Tnf Α ◽  
Marrow Cells
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