Cited by 540Bone and Dental Protein StudiesBone Metabolism and DiseasesCell Adhesion Molecules Research

The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.

Interactions between the bone matrix proteins osteopontin and bone sialoprotein and the osteoclast integrin alpha v beta 3 potentiate bone resorption

Open access

Ross, F.P., Chappel, J., Alvarez, J.I., Sander, D., Butler, W.T., Farach-Carson, M.C., Mintz, K.A., Robey, P.G., Teitelbaum, S.L., Cheresh, D.A.·1993·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)98430-9

Open this paper in CoChat — free account

Abstract

We have investigated the mechanism by which osteoclasts adhere to and resorb bone. We show that these cells express beta 1 and beta 3 integrins which are involved in attachment to purified bone matrix proteins. Binding to osteopontin and bone sialoprotein is mediated by alpha v beta 3, while a beta 1 integrin is responsible for attachment to fibronectin. Both the rapid attachment by osteoclasts to intact bone particles and their subsequent resorption are blocked by a monoclonal antibody directed to the alpha v beta 3 complex but not by an antibody against beta 1 integrins. Attachment of osteoclasts to bone is also inhibited with soluble osteopontin, Arg-Gly-Asp-containing peptides derived from both osteopontin and bone sialoprotein, or a monospecific polyclonal antibody against osteopontin. We conclude that both osteoclast adherence to bone and subsequent resorption of its matrix are dependent on interactions between the bone matrix proteins osteopontin and/or bone sialoprotein and the integrin alpha v beta 3. Moreover, collagen, which constitutes 90% of its organic matrix, is minimally involved in binding of chicken osteoclasts to bone.

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(18)98430-9

Cites

56 of 56 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

New Perspectives in Cell Adhesion: RGD and Integrins
Ruoslahti, E. I., & Pierschbacher, M. D. (1987) · Science · doi:10.1126/science.2821619 · Cited by 4,875
Integrins: A family of cell surface receptors
Hynes, R. O. (1987) · Cell · doi:10.1016/0092-8674(87)90233-9 · Cited by 4,258
VLA Proteins in the Integrin Family: Structures, Functions, and Their Role on Leukocytes
Hemler, M. E. (1990) · Annual Review of Immunology · doi:10.1146/annurev.iy.08.040190.002053 · Cited by 1,561
Integrins.
Ruoslahti, E. I. (1991) · Journal of Clinical Investigation · doi:10.1172/jci114957 · Cited by 1,391
Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence.
Oldberg, Å., Franzén, A., & Heinegård, D. K. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.23.8819 · Cited by 1,081
Bone and Mineral Research
(1990) · Elsevier eBooks · doi:10.1016/c2009-0-34738-8 · Cited by 1,073
Osteopontin--a possible anchor of osteoclasts to bone.
Reinholt, F. P., Hultenby, K. R., Oldberg, Å., & Heinegård, D. K. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.12.4473 · Cited by 831
The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins.
Lawler, J., & Hynes, R. O. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.5.1635 · Cited by 580
Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor.
Cheresh, D. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.18.6471 · Cited by 569
Self-citation
Structure and biology of cartilage and bone matrix noncollagenous macromolecules
Heinegård, D. K., & Oldberg, Å. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.9.2663581 · Cited by 567

Show all 56 references

Research works printed but not linked: 2

Chambers, 1986, Bone Miner., 1, 127
Goldman, 1979, Natl. Cancer Inst., 63, 1009

Sorted by citations

Items 201–300 of 540

The cellular and molecular basis of prostate cancer
Foster, Cornford, Forsyth, Djamgoz, & Ke (1999) · British Journal of Urology · doi:10.1046/j.1464-410x.1999.00954.x · Cited by 60
Gene expression analyses of primary melanomas reveal CTHRC1 as an important player in melanoma progression
Eriksson, J., Joncour, V. L., Nummela, P., Jahkola, T., Virolainen, S., Laakkonen, P. M., Saksela, O., & Hölttä, E. (2016) · Oncotarget · doi:10.18632/oncotarget.7604 · Cited by 59
Osteoclasts secrete osteopontin into resorption lacunae during bone resorption
Luukkonen, J., Hilli, M., Nakamura, M., Ritamo, I., Valmu, L., Kauppinen, K., Tuukkanen, J., & Lehenkari, P. P. (2019) · Histochemistry and Cell Biology · doi:10.1007/s00418-019-01770-y · Cited by 58
Trabecular bone turnover, bone marrow cell development, and gene expression of bone matrix proteins after low calcium feeding in rats
Seto, H., Aoki, K., Kasugai, S., & Ohya, K. (1999) · Bone · doi:10.1016/s8756-3282(99)00229-x · Cited by 58
Granulocyte Macrophage-Colony Stimulating Factor Reciprocally Regulates αv-Associated Integrins on Murine Osteoclast Precursors
Inoue, M., Namba, N., Chappel, J. C., Teitelbaum, S. L., & Ross, F. P. (1998) · Molecular Endocrinology · doi:10.1210/mend.12.12.0213 · Cited by 58
Self-citation
Integrins: Structure, Function, and Biological Properties
Cheresh, D. A. (1993) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60204-0 · Cited by 58
Self-citation
C-terminal Modification of Osteopontin Inhibits Interaction with the αVβ3-Integrin
Christensen, B., Kläning, E., Nielsen, M. S., Andersen, M. H., & Sørensen, E. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277996 · Cited by 57
Interleukin-4 Induces Expression of the Integrin αvβ3 via Transactivation of the β3 Gene
Kitazawa, S., Ross, F. P., McHugh, K. P., & Teitelbaum, S. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.8.4115 · Cited by 57
Self-citation
The Regulatory Role of Matrix Proteins in Mineralization of Bone
Boskey, A. L., & Robey, P. G. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415853-5.00011-x · Cited by 59
Self-citation
In Vitro and In Vivo Characteristics of Stem Cells Derived from the Periodontal Ligament of Human Deciduous and Permanent Teeth
Song, J. S., Kim, S., Kim, S.-H., Choi, H.-J., Son, H.-K., Jung, H.-S., Kim, C., & Lee, J. H. (2012) · Tissue Engineering Part A · doi:10.1089/ten.tea.2011.0318 · Cited by 56
Altered osteoclast development and function in osteopontin deficient mice
Franzén, A., Hultenby, K. R., Reinholt, F. P., Önnerfjord, P., & Heinegård, D. K. (2007) · Journal of Orthopaedic Research® · doi:10.1002/jor.20544 · Cited by 56
Osteoblast-released Matrix Vesicles, Regulation of Activity and Composition by Sulfated and Non-sulfated Glycosaminoglycans
Schmidt, J. R., Kliemt, S., Preißler, C., Moeller, S. J., von Bergen�, M., Hempel, U., & Kalkhof, S. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.049718 · Cited by 57
Regulation of Collagenase-3 and Osteocalcin Gene Expression by Collagen and Osteopontin in Differentiating MC3T3-E1 Cells
DʼAlonzo, R. C., Kowalski, A. J., Denhardt, D. T., Nickols, G. A., & Partridge, N. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202604200 · Cited by 56
Tumour progression and angiogenesis in bone metastasis from breast cancer: new approaches to an old problem
van der Pluijm, G., Löwik, C. W. G. M., & Papapoulos, S. E. (2000) · Cancer Treatment Reviews · doi:10.1053/ctrv.1999.0143 · Cited by 56
A Mechanism for Modulation of Cellular Responses to VEGF
Byzova, T. V., Goldman, C. K., Pampori, N. A., Thomas, K. A., Bett, A. J., Shattil, S. J., & Plow, E. F. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00076-6 · Cited by 55
Serum bone sialoprotein as a marker of tumour burden and neoplastic bone involvement and as a prognostic factor in multiple myeloma
Woitge, H. W., Pecherstorfer, M., Horn, E., A-V, K., Diel, I., Bayer, P., Ludwig, H., Ziegler, R., & Seibel, M. J. (2001) · British Journal of Cancer · doi:10.1054/bjoc.2000.1614 · Cited by 54
Evidence That the Integrin β3 and β5 Subunits Contain a Metal Ion-dependent Adhesion Site-like Motif but Lack an I Domain
Lin, E. C. K., Ratnikov, B. I., Tsai, P. M., Gonzalez, E. R., McDonald, S. M., Pelletier, A. J., & Smith, J. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14236 · Cited by 54
Osteopontin Signals through Calcium and Nuclear Factor of Activated T Cells (NFAT) in Osteoclasts
Tanabe, N., Wheal, B. D., Kwon, J., Chen, H. H., Shugg, R. P. P., Sims, S. M., Goldberg, H. A., & Dixon, S. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.295048 · Cited by 53
Vascular calcification and its relation to bone calcification: Possible underlying mechanisms
Mody, N., Tintut, Y., Radcliff, K. E., & Demer, L. L. (2003) · Journal of Nuclear Cardiology · doi:10.1067/mnc.2003.0012 · Cited by 53
Bone matrix proteins in osteogenesis and remodelling in the neonatal rat mandible as studied by immunolocalization of osteopontin, bone sialoprotein, α2HS-glycoprotein and alkaline phosphatase
Pinero, G. J., Farach‐Carson, M. C., Devoll, R. E., Aubin, J. E., Brunn, J. C., & Butler, W. T. (1995) · Archives of Oral Biology · doi:10.1016/0003-9969(94)00144-z · Cited by 53
Self-citation
Encapsulation of simvastatin in PLGA microspheres loaded into hydrogel loaded BCP porous spongy scaffold as a controlled drug delivery system for bone tissue regeneration
Nath, S. D., Linh, N. T. B., Sadiasa, A., & Lee, B. (2013) · Journal of Biomaterials Applications · doi:10.1177/0885328213499272 · Cited by 52
Bone sialoprotein deficiency impairs osteoclastogenesis and mineral resorption in vitro
Boudiffa, M., Wade‐Gueye, N. M., Guignandon, A., Vanden‐Bossche, A., Sabido, O., Aubin, J. E., Jurdic, P., Vico, L., Lafage‐Proust, M., & Malaval, L. (2010) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.245 · Cited by 52
Dendritic-cell-derived osteoclasts: a new game changer in bone-resorption-associated diseases
Lapérine, O., Blin‐Wakkach, C., Guicheux, J., Beck-Cormier, S., & Lesclous, P. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.04.022 · Cited by 54
NO-dependent osteoclast motility: reliance on cGMP-dependent protein kinase I and VASP
Yaroslavskiy, B. B., Zhang, Y., Kalla, S. E., Palacios, V. G., Sharrow, A. C., Li, Y., Zaidi, M., Wu, C., & Blair, H. C. (2005) · Journal of Cell Science · doi:10.1242/jcs.02655 · Cited by 52
Diastereoselective Synthesis of New ψ[(E)-CHCMe]- and ψ[(Z)-CHCMe]-type Alkene Dipeptide Isosteres by Organocopper Reagents and Application to Conformationally Restricted Cyclic RGD Peptidomimetics
Oishi, S., Kamano, T., Niida, A., Odagaki, Y., Hamanaka, N., Yamamoto, M., Ajito, K., Tamamura, H., Otaka, A., & Fujii, N. (2002) · The Journal of Organic Chemistry · doi:10.1021/jo025923m · Cited by 52
Peptidomimetic antagonists of alphavbeta3 inhibit bone resorption by inhibiting osteoclast bone resorptive activity, not osteoclast adhesion to bone
Carron, C. P., Meyer, D. M., Engleman, V. W., RICO, J. G., Ruminski, P. G., Ornberg, R., Westlin, W., & Nickols, G. A. (2000) · Journal of Endocrinology · doi:10.1677/joe.0.1650587 · Cited by 52
The “love–hate” relationship between osteoclasts and bone matrix
Rucci, N., & Teti, A. M. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.02.009 · Cited by 52
Restricted and coordinated expression of β3-integrin and bone sialoprotein during cultured osteoblast differentiation
Schneider, G. B., Whitson, S. W., & Cooper, L. F. (1999) · Bone · doi:10.1016/s8756-3282(99)00007-1 · Cited by 50
Calcium sensing and cell signaling processes in the local regulation of osteoclastic bone resorption
Zaidi, M., Moonga, B. S., & Huang, C. L.-H. (2004) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1017/s1464793103006262 · Cited by 49
Nonpeptide αvβ3 antagonists. Part 2: constrained glycyl amides derived from the RGD tripeptide
Meißner, R., Perkins, J. J., Duong, L. T., Hartman, G. D., Hoffman, W. F., Huff, J. R., Ihle, N. C., Leu, C., Nagy, R. M., Naylor-Olsen, A. M., et al. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(01)00687-4 · Cited by 50
The role of the integrin vitronectin receptor, ?v?3 in melanoma metastasis
Nip, J., & Brodt, P. (1995) · Cancer and Metastasis Reviews · doi:10.1007/bf00690295 · Cited by 50
Basic Principles and Clinical Applications of Biochemical Markers of Bone Metabolism
Seibel, M. J., & Woitge, H. W. (1999) · Journal of Clinical Densitometry · doi:10.1385/jcd:2:3:299 · Cited by 50
The bovine Lactoferrin-Osteopontin complex increases proliferation of human intestinal epithelial cells by activating the PI3K/Akt signaling pathway
Liu, L., Jiang, R., Liu, J., & Lönnerdal, B. L. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.125919 · Cited by 52
Histomorphometric Evidence for Echistatin Inhibition of Bone Resorption in Mice with Secondary Hyperparathyroidism
Masarachia, P. J., Yamamoto, M., Leu, C., Rodan, G. A., & Duong, L. T. (1998) · Endocrinology · doi:10.1210/endo.139.3.5828 · Cited by 49
The role of vascular cell integrins αvß3 and αvß5 in angiogenesis
Varner, J. A. (1997) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-0348-9006-9_15 · Cited by 49
New targeted probes for radioimaging of angiogenesis
Stollman, T. H., Ruers, T. J. M., Oyen, W. J. G., & Boerman, O. C. (2009) · Methods · doi:10.1016/j.ymeth.2009.03.006 · Cited by 48
Downregulation of lizard immuno-genes in the regenerating tail and myogenes in the scarring limb suggests that tail regeneration occurs in an immuno-privileged organ
Vitulo, N., Valle, L. D., Skobo, T., Valle, G., & Alibardi, L. (2017) · PROTOPLASMA · doi:10.1007/s00709-017-1107-y · Cited by 48
Predominant integrin ligands expressed by osteoblasts show preferential regulation in response to both cell adhesion and mechanical perturbation
Carvalho, R. S., Bumann, A., Schaffer, J. L., & Gerstenfeld, L. C. (2002) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10031 · Cited by 48
Calcium signals in prostate cancer cells: specific activation by bone-matrix proteins
Lecrone, V., Li, W., Devoll, R. E., Logothetis, C. J., & Farach‐Carson, M. C. (2000) · Cell Calcium · doi:10.1054/ceca.1999.0083 · Cited by 48
Self-citation
The critical role of osteopontin (OPN) in fibrotic diseases
Tang, Z., Xia, Z., Wang, X., & Liu, Y. (2023) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2023.08.007 · Cited by 47
Osteopontin in Skeletal Tissue Homeostasis: An Emerging Picture of the Autocrine/Paracrine Functions of the Extracellular Matrix
Gerstenfeld, L. C. (1999) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.1999.14.6.850 · Cited by 47
The role of osteoprogenitors in vascular calcification
Jakoby, M., & Semenkovich, C. F. (2000) · Current Opinion in Nephrology & Hypertension · doi:10.1097/00041552-200001000-00003 · Cited by 47
Osteopontin expression in ovarian carcinomas and tumors of low malignant potential (LMP)
TINIAKOS, D. G., Yu, H., & Liapis, H. (1998) · Human Pathology · doi:10.1016/s0046-8177(98)90253-2 · Cited by 46
Development and Characterization of a Human In Vitro Resorption Assay: Demonstration of Utility Using Novel Antiresorptive Agents
James, I. E., Lark, M. W., Zembryki, D. L., Lee-Rykaczewski, E., Hwang, S. M., Tomaszek, T. A., Belfiore, P., & Gowen, M. (1999) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.1999.14.9.1562 · Cited by 46
Bone extracts immunomodulate and enhance the regenerative performance of dicalcium phosphates bioceramics
Mansour, A., Nada, L. A., Al‐Waeli, H., Mezour, M. A., Abdallah, M., Kinsella, J. M., Kort-Mascort, J., Henderson, J. E., Ramírez-GarcíaLuna, J. L., Tran, S. D., et al. (2019) · Acta Biomaterialia · doi:10.1016/j.actbio.2019.03.012 · Cited by 45
Expression and Regulation of RAB3 Proteins in Osteoclasts and Their Precursors
Abu‐Amer, Y., Teitelbaum, S. L., Chappel, J. C., Schlesinger, P. H., & Ross, F. P. (1999) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.1999.14.11.1855 · Cited by 45
Self-citation
Mitigation of Ectopic Calcification in Osteopontin-Deficient Mice by Exogenous Osteopontin
Ohri, R., Tung, E. L., Rajachar, R. M., & Giachelli, C. M. (2005) · Calcified Tissue International · doi:10.1007/s00223-004-0071-7 · Cited by 45
Parallels between arterial and cartilage calcification
Rutsch, F., & Terkeltaub, R. A. (2003) · Current Opinion in Rheumatology · doi:10.1097/00002281-200305000-00019 · Cited by 45
Colony Stimulating Factor-1–Induced Osteoclast Spreading Depends on Substrate and Requires the Vitronectin Receptor and the c-src Proto-Oncogene
Teti, A. M., Taranta, A., Migliaccio, S., Degiorgi, A., Santandrea, E., Villanova, I., Faraggiana, T., Chellaiah, M., & Hruska, K. A. (1998) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.1998.13.1.50 · Cited by 43
Continued sustained insulin-releasing PLGA nanoparticles modified 3D-Printed PCL composite scaffolds for osteochondral repair
Wei, P., Xu, Y., Zhang, H., & Wang, L. (2021) · Chemical Engineering Journal · doi:10.1016/j.cej.2021.130051 · Cited by 44
Absence of ERRα in Female Mice Confers Resistance to Bone Loss Induced by Age or Estrogen-Deficiency
Teyssier, C., Gallet, M., Rabier, B., Monfoulet, L., Dine, J., Macari, C., Espallergues, J., Horard, B., Giguère, V., Cohen-Solal, M. E., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007942 · Cited by 44
Altered Expression of Bone Sialoproteins in Vitamin D–Deficient rBSP2.7Luc Transgenic Mice
Chen, J. D., Jin, H., Ranly, D. M., Sodek, J., & Boyan, B. D. (1999) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.1999.14.2.221 · Cited by 44
Bovine Oviduct Epithelial Cells Dedifferentiate Partly in Culture, While Maintaining their Ability to Improve Early Embryo Development Rate and Quality
Schmaltz-Panneau, B., Locatelli, Y., Uzbekova, S., Perreau, C., & Mermillod, P. (2015) · Reproduction in Domestic Animals · doi:10.1111/rda.12556 · Cited by 43
Biological role of site-specific O-glycosylation in cell adhesion activity and phosphorylation of osteopontin
Oyama, M., Kariya, Y., Kariya, Y., Matsumoto, K., Kanno, M., Yamaguchi, Y., & Hashimoto, Y. (2018) · Biochemical Journal · doi:10.1042/bcj20170205 · Cited by 43
Sp1/Sp3 and PU.1 Differentially Regulate β5Integrin Gene Expression in Macrophages and Osteoblasts
Feng, X., Teitelbaum, S. L., Quiroz, M. E., Cheng, S., Lai, C.-F., Avioli, L. V., & Ross, F. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8331 · Cited by 44
Self-citation
Attachment of Human Periodontal Ligament Cells to Enamel Matrix‐Derived Protein Is Mediated Via Interaction Between BSP‐Like Molecules and Integrin αvβ3
Suzuki, N., Ohyama, M., Maeno, M., Ito, K., & Otsuka, K. (2001) · Journal of Periodontology · doi:10.1902/jop.2001.72.11.1520 · Cited by 42
Extensive Clear Zone and Defective Ruffled Border Formation in Osteoclasts of Osteopetrotic (ia/ia) Rats: Implications for Secretory Function
Reinholt, F. P., Hultenby, K. R., Heinegård, D. K., Marks, S. C., Norgård, M., & Anderson, G. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4585 · Cited by 42
The anatomy of bone sialoprotein immunoreactive sites in bone as revealed by combined ultrastructural histochemistry and immunohistochemistry
Riminucci, M., Silvestrini, G., BONUCCI, E., Fisher, L. W., Robey, P. G., & Bianco, P. (1995) · Calcified Tissue International · doi:10.1007/bf00298883 · Cited by 42
Self-citation
Mechanisms of bone resorption
Everts, V. E., Jansen, I. D. C., & de Vries, T. J. (2022) · Bone · doi:10.1016/j.bone.2022.116499 · Cited by 46
Journal of Bone and Mineral Research
Teitelbaum, S. L. (1993) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.5650081318 · Cited by 41
Self-citation
Blockade of osteoclast‐mediated bone resorption through occupancy of the integrin receptor: A potential approach to the therapy of osteoporosis
Dresner–Pollak, R., & Rosenblatt, M. (1994) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240560308 · Cited by 41
Biphasic alloplastic graft used to preserve the dimension of the edentulous ridge: an experimental study in the dog
Lindhe, J., Araújo, M. G., Bufler, M., & Liljenberg, B. (2012) · Clinical Oral Implants Research · doi:10.1111/j.1600-0501.2012.02527.x · Cited by 40
Identification of osteopontin (OPN) mRNA and protein in the rat testis and epididymis, and on sperm
Siiteri, J. E., Ensrud, K. M., Moore, A., & Hamilton, D. W. (1995) · Molecular Reproduction and Development · doi:10.1002/mrd.1080400104 · Cited by 40
Tumor Necrosis Factor α Regulatesα vβ5 Integrin Expression by Osteoclast Precursors in Vitro and in Vivo1
Inoue, M., Ross, F. P., Erdmann, J. M., Abu‐Amer, Y., Shi, W., & Teitelbaum, S. L. (2000) · Endocrinology · doi:10.1210/endo.141.1.7285 · Cited by 40
Self-citation
Differential Expression of Osteopontin, PC4, and CEC5, a Novel mRNA Species, duringin VitroAngiogenesis
Pröls, F., Loser, B., & Marx, M. (1998) · Experimental Cell Research · doi:10.1006/excr.1997.3882 · Cited by 40
Ultrastructural localization of osteopontin in the kidney
Madsen, K., Zhang, L., Shamat, A. R. A., Siegfried, S., & H, J. (1997) · Journal of the American Society of Nephrology · doi:10.1681/asn.v871043 · Cited by 39
Root resorption: The possible role of extracellular matrix proteins
Lee, A. F., Schneider, G. B., Finkelstein, M. W., & Southard, T. E. (2004) · American Journal of Orthodontics and Dentofacial Orthopedics · doi:10.1016/j.ajodo.2004.02.009 · Cited by 38
Osteopontin Expression in Prostate Cancer and Benign Prostatic Hyperplasia
Tozawa, K., Yamada, Y., Kawai, N., Okamura, T., Ueda, K., & Kohri, K. (1999) · Urologia Internationalis · doi:10.1159/000030381 · Cited by 38
CD44 Antibodies Inhibit Osteoclast Formation
Kania, J., Kehat-Stadler, T., & Kupfer, S. R. (1997) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.1997.12.8.1155 · Cited by 38
Expression of Adhesion Molecules during Tooth Resorption in Feline Teeth: A Model System for Aggressive Osteoclastic Activity
Shigeyama, Y., Grove, T. K., Strayhorn, C. L., & Somerman, M. J. (1996) · Journal of Dental Research · doi:10.1177/00220345960750090601 · Cited by 38
Targeted overexpression of BSP in osteoclasts promotes bone metastasis of breast cancer cells
Tu, Q., Zhang, J., Fix, A., Brewer, E., Li, Y., Zhang, Z., & Chen, J. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21576 · Cited by 37
Apoptosis and Bcl-2 oncoprotein expression in the human fetal central nervous system
Chan, W., & Yew, D. T. W. (1998) · The Anatomical Record · doi:10.1002/(sici)1097-0185(199810)252:2 · Cited by 58
The Biochemistry of Bone
Gokhale, J. A., Boskey, A. L., & Robey, P. G. (2001) · Elsevier eBooks · doi:10.1016/b978-012470862-4/50005-2 · Cited by 37
Self-citation
Insulin-like growth factor binding proteins in femoral and vertebral bone marrow stromal cells: Expression and regulation by thyroid hormone and dexamethasone
Milne, M. L., Quail, J. M., Rosen, C. J., & Baran, D. T. (2001) · Journal of Cellular Biochemistry · doi:10.1002/1097-4644(20010501)81:2 · Cited by 43
Self-citation
Response of cementoblast-like cells to mechanical tensile or compressive stress at physiological levels in vitro
Huang, L., Meng, Y., Ren, A., Han, X., Bai, D., & Bao, L. (2008) · Molecular Biology Reports · doi:10.1007/s11033-008-9376-3 · Cited by 35
New Alternatively Spliced Form of Galectin-3, a Member of the β-Galactoside-binding Animal Lectin Family, Contains a Predicted Transmembrane-spanning Domain and a Leucine Zipper Motif
Gorski, J. P., Liu, F., Artigues, A., Castagna, L. F., & Osdoby, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109578200 · Cited by 35
The Molecular Biology of Bone Resorption Due to Chronic Otitis Media
Chole, R. A. (1997) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1997.tb51882.x · Cited by 34
Synthesis of (−)-Calicoferol B
Taber, D. F., Jiang, Q. L., Chen, B., Zhang, W., & Campbell, C. L. (2002) · The Journal of Organic Chemistry · doi:10.1021/jo020103v · Cited by 35
Morphological examination of bone synthesis via direct administration of basic fibroblast growth factor into rat bone marrow
Amizuka, N., Yamada, M., Watanabe, J., Hoshi, K., Fukushi-Irie, M., Oda, K., Ikehara, Y., & Ozawa, H. (1998) · Microscopy Research and Technique · doi:10.1002/(sici)1097-0029(19980515)41:4 · Cited by 35
Regulation of RANKL-induced osteoclastic differentiation by vascular cells
Tintut, Y., Abedin, M. Z., CHO, J., Choe, A., Lim, J. H., & Demer, L. L. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.03.019 · Cited by 34
Secreted factors from metastatic prostate cancer cells stimulate mesenchymal stem cell transition to a pro‐tumourigenic ‘activated’ state that enhances prostate cancer cell migration
Ridge, S. M., Bhattacharyya, D. D., Dervan, E., Naicker, S. D., Burke, A. J., Murphy, M. J., O’Leary, K., Greene, J. P., Ryan, A. E., Sullivan, F. J., et al. (2017) · International Journal of Cancer · doi:10.1002/ijc.31226 · Cited by 35
Increased osteopontin plasma levels in multiple sclerosis patients correlate with bone-specific markers
Vogt, M., ten Kate, J. T., Drent, R., Polman, C., & Hupperts, R. (2010) · Multiple Sclerosis · doi:10.1177/1352458509359723 · Cited by 33
Synergistic effect of Indian hedgehog and bone morphogenetic protein-2 gene transfer to increase the osteogenic potential of human mesenchymal stem cells
Reichert, J. C., Schmalzl, J., Prager, P., Gilbert, F., Quent, V. M. C., Steinert, A. F., Rudert, M., & Nöth, U. A. (2013) · Stem Cell Research & Therapy · doi:10.1186/scrt316 · Cited by 33
Short- and Long-Term Effects of Ibandronate Treatment on Bone Turnover in Paget Disease of Bone
Woitge, H. W., Oberwittler, H., Heichel, S., Grauer, A., Ziegler, R., & Seibel, M. J. (2000) · Clinical Chemistry · doi:10.1093/clinchem/46.5.684 · Cited by 33
Adhesion Receptors in Health and Disease
Rojas, A. I., & Ahmed, A. R. (1999) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/10454411990100030601 · Cited by 33
Expression of rat bone sialoprotein promoter in transgenic mice
Chen, J., Thomas, H. F., Jin, H., Jiang, H., & Sodek, J. (1996) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.5650110513 · Cited by 33
A Novel 3D Osteoblast and Osteocyte Model Revealing Changes in Mineralization and Pro-osteoclastogenic Paracrine Signaling During Estrogen Deficiency
Naqvi, S. M., Pérez, J. A. P., Kumar, V., Verbruggen, A. S. K., & McNamara, L. M. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00601 · Cited by 35
Recognition of cryptic sites in human and mouse laminins by rat osteoclasts is mediated by β3 and β1 integrins
Horton, M. A., Spragg, J. H., Bodary, S. C., & Helfrich, M. H. (1994) · Bone · doi:10.1016/8756-3282(94)90312-3 · Cited by 32
Expression of bone sialoprotein mRNA during bone formation and resorption induced by colchicine in rat tibial bone marrow cavity
Arai, N., Ohya, K., Kasugai, S., Shimokawa, H., Ohida, S., Ogura, H., & Amagasa, T. (1995) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.5650100811 · Cited by 32
In Vitro Differentiation of CD14 Cells From Osteopetrotic Subjects: Contrasting Phenotypes With TCIRG1, CLCN7, and Attachment Defects
Blair, H. C., Borysenko, C. W., VILLA, A. M., Schlesinger, P. H., Kalla, S. E., Yaroslavskiy, B. B., Palacios, V. G., Oakley, J. I., & Orchard, P. J. (2004) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.040403 · Cited by 32
Overview of mechanisms and novel therapies on rheumatoid arthritis from a cellular perspective
Han, P., Liu, X., He, J., Luyang, H., & Li, J. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1461756 · Cited by 38
FGF upregulates osteopontin in epiphyseal growth plate chondrocytes: Implications for endochondral ossification
Weizmann, S., Tong, A., Reich, A., Genina, O., Yayon, A., & Ornan, E. M. (2005) · Matrix Biology · doi:10.1016/j.matbio.2005.07.003 · Cited by 31
Effects of impaired functional domains of osteopontin on renal crystal formation: Analyses of OPN transgenic and OPN knockout mice
Hamamoto, S., Nomura, S., Yasui, T., Okada, A., Hirose, M., Shimizu, H., Itoh, Y., Tozawa, K., & Kohri, K. (2009) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.090520 · Cited by 31
Cloning, Sequence Analysis, and Chromosomal Localization of the Novel Human Integrin α11 Subunit (ITGA11)
Lehnert, K., Ni, J., Leung, E. Y., Gough, S. M., Weaver, A., Yao, W.-P., Liu, D. X., Wang, S.-X., Morris, C. M., & Krissansen, G. W. (1999) · Genomics · doi:10.1006/geno.1999.5909 · Cited by 31
Protein kinases of cultured osteoblasts: Selectivity for the extracellular matrix proteins of bone and their catalytic competence for osteopontin
Salih, E., Ashkar, S., Gerstenfeld, L. C., & Glimcher, M. J. (1996) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.5650111013 · Cited by 31
Differential regulation of osteoadherin (OSAD) by TGF-β1 and BMP-2
Rehn, A. P., Chalk, A. M., & Wendel, M. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.133 · Cited by 31
Mammalian cell death proteases: A family of highly conserved aspartate specific cysteine proteases
Alnemri, E. S. (1997) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(199701)64:1 · Cited by 307
Regulation of Bone Sialoprotein and Osteopontin mRNA Expression by Dexamethasone and 1,25-dihydroxyvitamin D3in Rat Bone Organ Cultures
Chen, J., Thomas, H. F., & Sodek, J. (1996) · Connective Tissue Research · doi:10.3109/03008209609028892 · Cited by 31
Fas stimulation induces RB dephosphorylation and proteolysis that is blocked by inhibitors of the ICE protease family
Dou, Q. P., An, B., Antoku, K., & Johnson, D. E. (1997) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19970315)64:4 · Cited by 46
Proteins involved in regulating bone invasion in skull base meningiomas
Salehi, F., Jalali, S., Alkins, R. D., Lee, J.-I., Lwu, S., Burrell, K. E., Gentili, F., Croul, S. E., & Zadeh, G. M. (2012) · Acta Neurochirurgica · doi:10.1007/s00701-012-1577-9 · Cited by 30

Authors: Ross, F. P., Chappel, J., Alvarez, J. I., Sander, D., Butler, W. T., Farach-Carson, M. C., Mintz, K. A., Robey, P. G., Teitelbaum, S. L., & Cheresh, D. A.
Affiliations: National Institutes of Health (US)
Scripps Research Institute (US)
ORCID: Butler, W.T.
Robey, P.G.
Teitelbaum, S.L.
Cheresh, D.A.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1993-05
Volume: 268
Issue: 13
Pages: 9901-9907
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)98430-9
OpenAlex: W1511542029
Cited by: 537
References: 56
Citations by year: 2026: 6 · 2025: 3 · 2024: 8 · 2023: 6 · 2022: 9 · 2021: 8 · 2020: 7 · 2019: 10 · 2018: 12 · 2017: 8 · 2016: 11 · 2015: 8 · 2014: 9 · 2013: 15 · 2012: 11
FWCI: 28.07
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 10043 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ar039273-12)
National Cancer Institute (CA-50286, CA-47526)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR39273)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Keywords: osteoclasts, osteopontin, bone sialoprotein, alpha v beta 3 integrin, beta1 integrin, bone resorption, bone matrix proteins, fibronectin, RGD peptide, collagen
MeSH terms: Amino Acid Sequence, Animals, Bone Matrix, Bone Resorption, Cell Adhesion, Humans, Kinetics, Models, Biological, Molecular Sequence Data, Oligopeptides, Osteoclasts, Sialoglycoproteins, Integrins, Rats, Osteopontin, Integrin-Binding Sialoprotein

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

Interactions between the bone matrix proteins osteopontin and bone sialoprotein and the osteoclast integrin alpha v beta 3 potentiate bone resorption

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks