The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Identity of Osteoclastogenesis Inhibitory Factor (OCIF) and Osteoprotegerin (OPG): A Mechanism by which OPG/OCIF Inhibits Osteoclastogenesis in Vitro1
Abstract
The morphogenesis and remodeling of bone depends on the integrated activity of osteoblasts that form bone and osteoclasts that resorb bone. We previously reported the isolation of a new cytokine termed osteoclastogenesis inhibitory factor, OCIF, which specifically inhibits osteoclast development. Here we report the cloning of a complementary DNA of human OCIF. OCIF is identical to osteoprotegerin (OPG), a soluble member of the tumor-necrosis factor receptor family that inhibits osteoclastogenesis. Recombinant human OPG/OCIF specifically acts on bone tissues and increases bone mineral density and bone volume associated with a decrease of active osteoclast number in normal rats. Osteoblasts or bone marrow-derived stromal cells support osteoclastogenesis through cell-to-cell interactions. A single class of high affinity binding sites for OPG/OCIF appears on a mouse stromal cell line, ST2, in response to 1,25-dihydroxyvitamin D3. An anti-OPG/OCIF antibody that blocks the binding abolishes the biological activity of OPG/OCIF. When the sites are blocked with OPG/OCIF, ST2 cells fail to support osteoclastogenesis. These results suggest that the sites are involved in cell-to-cell signaling between stromal cells and osteoclast progenitors and that OPG/OCIF inhibits osteoclastogenesis by interrupting the signaling through the sites.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“OPG is an atypical member of the TNF receptor family in that it is a secreted protein with no transmembrane domain and no direct signaling properties (4,6).”
From Receptor Activator of Nuclear Factor κB Ligand and Osteoprotegerin Regulation of Bone Remodeling in Health and Disease (2008) · cites this paper as [6]
Citations
Cites
Osteoprotegerin: a novel secreted protein involved in the regulation of bone density.
Simonet, W. S., Lacey, D. L., Dunstan, C. R., Kelley, M., Chang, M.-S., Lüthy, R., Nguyen, H. Q., Wooden, S., Bennett, L., Boone, T., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80209-3 · Cited by 5,130
The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis
Itoh, N., Yonehara, S., Ishii, A., Yonehara, M., Mizushima, S.-I., Sameshima, M., Hase, A., Seto, Y., & Nagata, S. (1991) · Cell · doi:10.1016/0092-8674(91)90614-5 · Cited by 2,736
The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death
Smith, C. A., Farrah, T., & Goodwin, R. G. (1994) · Cell · doi:10.1016/0092-8674(94)90372-7 · Cited by 1,909
Yoshida, H., Hayashi, S.-I., Kunisada, T., Ogawa, M., Nishikawa, S., Okamura, H., Sudo, T., Shultz, L. D., & Nishikawa, S.-I. (1990) · Nature · doi:10.1038/345442a0 · Cited by 1,789
Increased Osteoclast Development After Estrogen Loss: Mediation by Interleukin-6
Jilka, R. L., Hangoc, G., Girasole, G., Passeri, G., Williams, D. C., Abrams, J. S., Boyce, B. F., Broxmeyer, H. E., & Manolagas, S. C. (1992) · Science · doi:10.1126/science.1621100 · Cited by 1,440
Takebe, Y., Seiki, M., Fujisawa, J., Hoy, P., Yokota, K., Arai, K., Yoshida, M., & Arai, N. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.1.466-472.1988 · Cited by 1,330
A novel domain within the 55 kd TNF receptor signals cell death
Tartaglia, L. A., Ayres, T. M., Wong, G. H., & Goeddel, D. V. (1993) · Cell · doi:10.1016/0092-8674(93)90464-2 · Cited by 1,290
Protection from Fas-Mediated Apoptosis by a Soluble Form of the Fas Molecule
Cheng, J., Zhou, T., Liu, C., Shapiro, J. P., Brauer, M. J., Kiefer, M. C., Barr, P. J., & Mountz, J. D. (1994) · Science · doi:10.1126/science.7510905 · Cited by 1,108
Modulation of Osteoclast Differentiation
Suda, T., Takahashi, N., & Martin, T. J. (1992) · Endocrine Reviews · doi:10.1210/edrv-13-1-66 · Cited by 1,004
OSTEOBLASTIC CELLS ARE INVOLVED IN OSTEOCLAST FORMATION
Takahashi, N., Akatsu, T., Udagawa, N., Sasaki, T., Yamaguchi, A., Moseley, J. M., Martin, T. J., & Suda, T. (1988) · Endocrinology · doi:10.1210/endo-123-5-2600 · Cited by 934
Cited by
Sorted by citations
Osteoclast differentiation and activation
Boyle, W. J., Simonet, W. S., & Lacey, D. L. (2003) · Nature · doi:10.1038/nature01658 · Cited by 6,670
Yasuda, H., Shima, N., Nakagawa, N., Yamaguchi, K., Kinosaki, M., Mochizuki, S.-I., Tomoyasu, A., Yano, K., Goto, M., Murakami, A., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3597 · Cited by 4,224
Self-citationSuda, T., Takahashi, N., Udagawa, N., Jimi, E., Gillespie, M. T., & Martin, T. J. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.3.0367 · Cited by 2,345
Mechanisms involved in the side effects of glucocorticoids
SCHACKE, H. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00297-8 · Cited by 1,847
Functions of RANKL/RANK/OPG in bone modeling and remodeling
Boyce, B. F., & Xing, L. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.03.018 · Cited by 1,844
Metadata
- Authors
- Yasuda, H., Shima, N., Nakagawa, N., Mochizuki, S.-I., Yano, K., Fujise, N., Sato, Y., Goto, M., Yamaguchi, K., Kuriyama, M., Kanno, T., Murakami, A., Tsuda, E., Morinaga, T., & Higashio, K.
- Affiliations
- Megmilk Snow Brand (Japan) (JP)
- Corresponding author
- Higashio, Kanji
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 1998-03
- Volume
- 139
- Issue
- 3
- Pages
- 1329-1337
- ISSN
- 0013-7227 (ISSN-L)
- 1945-7170
- OpenAlex
- W2167886526
- Cited by
- 1,201
- References
- 33
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 21 · 2023: 15 · 2022: 21 · 2021: 21 · 2020: 29 · 2019: 36 · 2018: 22 · 2017: 38 · 2016: 22 · 2015: 28 · 2014: 36 · 2013: 54 · 2012: 35
- FWCI
- 24.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
- Health Sciences › Medicine › Orthopedics and Sports Medicine › Bone health and osteoporosis research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
- Keywords
- osteoprotegerin, osteoclastogenesis inhibition, TNF receptor superfamily, bone remodeling, bone mineral density, stromal cells, osteoblasts, cell-to-cell signaling, 1,25-dihydroxyvitamin D3, bone resorption, gene cloning
- MeSH terms
- Amino Acid Sequence, Animals, Cells, Cultured, Cloning, Molecular, Glycoproteins, Humans, Male, Molecular Sequence Data, Osteoclasts, Recombinant Proteins, Bone Density, Bone Remodeling, Rats, Sprague-Dawley, Receptors, Tumor Necrosis Factor, Receptors, Cytoplasmic and Nuclear, Mice, Rats, Osteoprotegerin
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review