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Your search keyword '"Hong-Lin Tan"' showing total 5 results
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5 results on '"Hong-Lin Tan"'

1. A bispecific antibody targeting sclerostin and DKK-1 promotes bone mass accrual and fracture repair

Author

Monica Florio, Kannan Gunasekaran, Marina Stolina, Xiaodong Li, Ling Liu, Barbara Tipton, Hossein Salimi-Moosavi, Franklin J. Asuncion, Chaoyang Li, Banghua Sun, Hong Lin Tan, Li Zhang, Chun-Ya Han, Ryan Case, Amy N. Duguay, Mario Grisanti, Jennitte Stevens, James K. Pretorius, Efrain Pacheco, Heidi Jones, Qing Chen, Brian D. Soriano, Jie Wen, Brenda Heron, Frederick W. Jacobsen, Emil Brisan, William G. Richards, Hua Zhu Ke, and Michael S. Ominsky

Subjects
Science
Abstract

Antibodies that block the Wnt inhibitors sclerostin and DKK- 1 enhance bone formation and fracture repair. Here the authors show these monospecific antibodies induce compensatory mechanisms that limit efficacy, and have designed a sclerostin/DKK-1 bispecific antibody that promotes superior fracture repair in rodents and bone formation in primates.

Published
2016
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2. Osteoprotegerin Ligand Modulates Murine Osteoclast Survival in Vitro and in Vivo

Author

Hong Lin Tan, Steven Kaufman, Anthony Polverino, Frederick A. Fletcher, Sheila Scully, Gwyneth Van, Alana Rattan, Todd Juan, Wanrang Qiu, John Lu, Teresa L. Burgess, William J. Boyle, Michael J. Kelley, and David L. Lacey

Subjects
Macrophage colony-stimulating factor, musculoskeletal diseases, Male, medicine.medical_specialty, Time Factors, Cell Survival, medicine.medical_treatment, Injections, Subcutaneous, bcl-X Protein, Osteoclasts, Receptors, Cytoplasmic and Nuclear, Caspase 3, Apoptosis, Biology, Receptors, Tumor Necrosis Factor, Pathology and Forensic Medicine, Mice, Osteoprotegerin, Osteoclast, Internal medicine, medicine, Animals, RNA, Messenger, Cells, Cultured, Glycoproteins, Mice, Inbred C3H, Membrane Glycoproteins, Receptor Activator of Nuclear Factor-kappa B, Macrophage Colony-Stimulating Factor, RANK Ligand, NF-kappa B, Cell biology, Endocrinology, Cytokine, medicine.anatomical_structure, Gene Expression Regulation, Proto-Oncogene Proteins c-bcl-2, Cell culture, Carrier Proteins, Regular Articles
Abstract

Osteoprotegerin ligand (OPGL) targets osteoclast precursors and osteoclasts to enhance differentiation and activation, however, little is known about OPGL effects on osteoclast survival. In vitro, the combination of OPGL + colony-stimulating factor-1 (CSF-1) is required for optimal osteoclast survival. Ultrastructurally, apoptotic changes were observed in detached cells and culture lysates exhibited elevated caspase 3 activity, particularly in cultures lacking CSF-1. DEVD-FMK (caspase 3 inhibitor) partially protected cells when combined with OPGL, but not when used alone or in combination with CSF-1. CSF-1 maintained NF-kappaB activation and increased the expression of bcl-2 and bcl-X(L) mRNA, but had no effect on JNK activation. In contrast, OPGL enhanced both NF-kappaB and JNK kinase activation and increased the expression of c-src, but not bcl-2 and bcl-X(L) mRNA. These data suggest that aspects of both OPGL's and CSF-1's signaling/survival pathways are required for optimal osteoclast survival. In mice, a single dose of OPG, the OPGL decoy receptor, led to a90% loss of osteoclasts because of apoptosis within 48 hours of exposure without impacting osteoclast precursor cells. Therefore, OPGL is essential, but not sufficient, for osteoclast survival and endogenous CSF-1 levels are insufficient to maintain osteoclast viability in the absence of OPGL.

Published
2000

3. Denosumab, a Fully Human Monoclonal Antibody to RANKL, Inhibits Bone Resorption and Increases BMD in Knock-In Mice That Express Chimeric (Murine/Human) RANKL.

Author

Kostenuik, Paul J., Nguyen, Hung Q., McCabe, James, Warmington, Kelly S., Kurahara, Carol, Ning Sun, Ching Chen, Li, Luke, Cattley, Russ C., Van, Gwyneth, Scully, Shelia, Elliott, Robin, Grisanti, Mario, Morony, Sean, Hong Lin Tan, Asuncion, Frank, Xiaodong Li, Ominsky, Michael S., Stolina, Marina, and Dwyer, Denise

Abstract

This article discusses how denosumab, a fully human monoclonal antibody to RANKL, inhibits bone resorption and increases bone mass density in knock-in mice that express chimeric RANKL. Denosumab treatment reduces bone resorption and inhibits osteoclastogenesis by inhibiting human RANKL. The treated mice were forced to form a chimeric form of RANKL which maintained bone resorption. Histomorphometry showed that denosumab reduces osteoclast numbers and increases bone volume.

Published
2009
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4. OPGL is a key regulator of osteoclastogenesis, lymphocyte development and lymph-node organogenesis.

Author

Kong, Young-Yun, Yoshida, Hiroki, Sarosi, Ildiko, Hong-Lin Tan, Timms, Emma, Capparelli, Casey, Morony, Sean, Oliveira-dos-Santos, Antonio J., Van, Gwyneth, Itie, Annick, Khoo, Wilson, Wakeham, Andrew, Dunstan, Colin R., Lacey, David L., Mak, Tak W., Boyle, William J., and Penninger, Josef M.

Subjects
TUMOR necrosis factors, OSTEOCLASTS, T cells, OSTEOPETROSIS, LYMPH nodes
Abstract

Presents research on the tumor-necrosis-factor-family molecule osteoprotegerin ligand, or OPGL. Identification of OPGL as a potential osteoclast differentiation factor and regulator of interaction between T cells and dendritic cells in vitro; Severity of osteopetrosis and a defect in tooth eruption of mice; Lack of osteoclasts as a result of an inability of osteoblasts to support osteoclastogenesis; Implication of OPGL as a regulator of lymph-node organogenesis and lymphocyte development.

Published
1999
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5. Osteoprotegerin: A Novel Secreted Protein Involved in the Regulation of Bone Density

Author

Hung Q. Nguyen, P Derby, Anne Colombero, Michael J. Kelley, N. Bucay, Dave Hill, L Renshaw-Gegg, William J. Boyle, Grant Shimamoto, W Pattison, S Sander, Colin R. Dunstan, R Lüthy, Patricia Shehan Campbell, David L. Lacey, William S. Simonet, John K. Sullivan, T.M Hughes, Geraldine Trail, Ming-Shi Chang, Margaret L. DeRose, S Wooden, Gwyneth Van, L Bennett, John E. Tarpley, Richard Lee, Robin Elliott, E. Davy, Tom Boone, and Hong-Lin Tan

Subjects
Male, musculoskeletal diseases, medicine.medical_specialty, Ovariectomy, Recombinant Fusion Proteins, Osteoimmunology, Cellular differentiation, Molecular Sequence Data, Osteoclasts, Receptors, Cytoplasmic and Nuclear, Mice, Transgenic, Biology, Receptors, Tumor Necrosis Factor, General Biochemistry, Genetics and Molecular Biology, Bone resorption, Osteoclast maturation, Mice, Osteoprotegerin, Bone Density, Osteoclast, Cricetinae, Internal medicine, medicine, Animals, Humans, Amino Acid Sequence, RNA, Messenger, Bone Resorption, Cells, Cultured, Glycoproteins, Sequence Homology, Amino Acid, Biochemistry, Genetics and Molecular Biology(all), Gene Expression Regulation, Developmental, Cell Differentiation, RANK Ligand, Rats, Inbred F344, Rats, Endocrinology, medicine.anatomical_structure, Liver, Organ Specificity, RANKL, Osteopetrosis, biology.protein, Female
Abstract

A novel secreted glycoprotein that regulates bone resorption has been identified. The protein, termed Osteoprotegerin (OPG), is a novel member of the TNF receptor superfamily. In vivo, hepatic expression of OPG in transgenic mice results in a profound yet nonlethal osteopetrosis, coincident with a decrease in later stages of osteoclast differentiation. These same effects are observed upon administration of recombinant OPG into normal mice. In vitro, osteoclast differentiation from precursor cells is blocked in a dose-dependent manner by recombinant OPG. Furthermore, OPG blocks ovariectomy-associated bone loss in rats. These data show that OPG can act as a soluble factor in the regulation of bone mass and imply a utility for OPG in the treatment of osteoporosis associated with increased osteoclast activity.

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