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5 results on '"Disheng Qin"'

1. Abstracts of Poster Presentations

Author

Amjad Javed, Sarah L. Dallas, Mitsuhiro Enjo, Jeffrey A. Winkles, Bernd Grohe, Colette A. Inkson, David W. Rowe, Tatiana Foroud, Jim Simmer, Hitesh Kapadia, Chi P. Lee, Frédéric Lézot, Chunxi Ge, Bill Daly, Ryuichi Fujisawa, Jason O’Young, Izabela Maciejewska, Ana Carolina Acevedo, Hua Wu, Yanming Bi, L. Lausten, L.F. Bonewald, Matthew R. Allen, Patricia A. Veno, Hongshan Zhao, Laurie K. McCauley, Dominique Hotton, Mina Mina, Soraya E. Gutierrez, Wu Li, Faiza Afzal, Johanne LeBihan, Dana Olton, Hailan Feng, Elizabeth Lowder, L.M. Paula, Nabil G. Seidah, Gabriele Mues, Larry W. Fisher, Masato Tamura, Tao Peng, Z. Schwartz, J. Katz, Marjorie Weaver, Jolene Bohensky, Dong Yan, William T. Butler, Ling Ye, Sara Jeffrey, Ejvis Lamani, Jinhua Li, Daming Fan, Kurtulus Golcuk, Eric T. Everett, Carolyn W. Gibson, Muhanad Aïoub, M. Johnson, Peter S. N. Rowe, Ming Zhong, Lynda F. Bonewald, J.R. Néfussi, Gérard Goubin, Noritaka Isogai, A.C. Acevedo, Yong Li, Harvey A. Goldberg, Janet Moradian-Oldak, Yan Li, Vickram Srinivas, M.T. Hincke, C. Barragan-Adjemian, Thuan Le, Bat Ami Gotliv, Yuka Shinmura, Xiaoxia Zhang, Martin Montecino, Yixia Xie, Xiaowei Su, Paul H. Krebsbach, Sharon Segvich, Michèle Garabédian, Joseph M. Wallace, Frederick H. Silver, Li Zhu, Chaoying Cui, Mohammad Q. Hassan, Laurence Pibouin, Sharanjot Saini, Jian Q. Feng, Mila Spevak, Ivo Kalajzic, Sergei A. Kuznetsov, M.D. McKee, Chunlin Qin, Renny T. Franceschi, Esben S. Sørensen, Sylvie Babajko, Laurent Ameye, Barbara Rodgers, Di Jiang, Mireille Bonnefoix, Yixin Wu, Michel Goldberg, Janet L. Stein, Bingzhen Huang, Coralee E. Tye, Robin Jacquet, Mikko Karttunen, Michael D. Morris, Rachel L. Lorenz, Karl J. Jepsen, Pamela DenBesten, J. Timothy Wright, Zhi-An Yuan, Yoshinori Shinohara, Chad M. Novince, Jane B. Lian, Rajamani Lakshminarayanan, Wilbur Tong, Jingfeng Wu, W. Kim Seow, Hyon Jong Kim, John D. Bartlett, Lixiang Liu, Céline Gaucher, Sharon B. Midura, Zvi Schwartz, Sara Chirico, Alastair James Sloan, Nehal Al Tarhuni, Shuo Chen, Hernan Roca, Petros Papagerakis, Adele L. Boskey, Ellen P. Henderson, Darrell H. Carney, Donghyun Lee, Irving M. Shapiro, Tchilalo Boukpessi, David H. Kohn, Graeme K. Hunter, Dominique Septier, Yoshitaka Wada, Amit Vasanji, Juan Dong, Urban Lindgren, Hayden William Courtland, Jan C.-C. Hu, Guozhi Xiao, Mark Stephen Litaker, Brent B. Ward, Nan E. Hatch, James P. Simmer, Marian F. Young, Stéphane Petit, Chang Du, B.D. Boyan, Fleur Meary, Ashok B. Kulkarni, M. MacDougall, Arthur Veis, Gabrielle Mues, Kaleem Zaidi, Mitsuaki Ono, Zhi Sun, E. Angeles Martinez-Mier, Subhashis Biswas, Isabelle Fernandes, Thomas C. Hart, Jong-Sup Bae, Cynthia Suggs, Mildred C. Embree, Shelley E. Brown, Jonathan A. R. Gordon, Jerry Q. Feng, Nadder D. Sahar, Prashant N. Kumta, William J. Landis, Jitesh Pratap, Melissa Aragon, Rachel J. Waddington, J. Dong, Udo Becker, Kotaro Tanimoto, Andre J. van Wijnen, Rena N. D'Souza, Ronald J. Midura, Yongbo Lu, Jan Hu, Anamaria Balic, Jeffrey P. Gorski, Charles Sfeir, Ying Wang, Yao Sun, Frédéric Jehan, Darrin Simmons, Mary MacDougall, Bill Daley, Disheng Qin, Yuanyuan Hu, Masaki J. Honda, Hanson Fong, L.J.S. Santos, P. Suzanne Hart, Gary S. Stein, Tina M. Kilts, Catherine Chaussain-Miller, Y.-C. Chien, Lars-Arne Haldosén, D.B. Ang, Barbara D. Boyan, Muriel Molla, Sarah Jane Youde, Thorsten Kirsch, Ariane Berdal, Jennifer Rosser, Morimichi Mizuno, Yuwei Fan, Kathy K.H. Svoboda, Nichole T. Huffman, James T. Ryaby, Carl-Magnus Bäckesjö, and Cielo Barragan-Adjemian

Subjects
Pharmacology, Histology, Pharmaceutical Science, Pharmacology (medical), Pharmacy, General Medicine, Anatomy, Toxicology
Published
2008
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2. Distinct Compartmentalization of Dentin Matrix Protein 1 Fragments in Mineralized Tissues and Cells

Author

Yao Sun, Jerry Q. Feng, Gabrielle Mues, Bingzhen Huang, Disheng Qin, Chunlin Qin, Kathy K.H. Svoboda, Lynda F. Bonewald, Izabela Maciejewska, and William T. Butler

Subjects
Paper, Mineralized tissues, Histology, Osteocytes, Bone and Bones, Rats, Sprague-Dawley, Extracellular matrix, Mice, Calcification, Physiologic, stomatognathic system, medicine, Dentin, Animals, Humans, Cellular compartment, Extracellular Matrix Proteins, biology, Chemistry, Cartilage, Anatomy, Phosphoproteins, Immunohistochemistry, Peptide Fragments, DMP1, Cell Compartmentation, Rats, Cell biology, medicine.anatomical_structure, Proteoglycan, Organ Specificity, biology.protein, Dentinogenesis, Tooth
Abstract

Dentin matrix protein 1 (DMP1) has been shown to be critical for the formation of dentin and bone. However, the precise pathway by which DMP1 participates in dentinogenesis and osteogenesis remains to be clarified. DMP1 is present in the extracellular matrix of dentin and bone as processed NH2- and COOH-terminal fragments. The NH2-terminal fragment occurs as a proteoglycan, whereas the COOH-terminal fragment is highly phosphorylated. The differences in biochemical properties suggest that these fragments may have different tissue and cell distribution in association with distinct functions. In this study, we analyzed the distribution of the NH2- and COOH-terminal fragments of DMP1 in tooth, bone, osteocytes as well as MC3T3-E1 and HEK-293 cells. Immunohistochemical analyses were performed using antibodies specific to the NH2- or COOH-terminal region of DMP1. Clear differences in the distribution of these fragments were observed. In the teeth and bone, the NH2-terminal fragment was primarily located in the nonmineralized predentin and cartilage of the growth plate, while the COOH-terminal fragment accumulated in the mineralized zones. In osteocytes, the NH2-terminal fragment appeared more abundant along cell membrane and processes of osteocytes, while the COOH-terminal fragment was often found in the nuclei. This pattern of distribution in cellular compartments was further confirmed by analyses on MC3T3-E1 and HEK-293 cells transfected with a construct containing DMP1 cDNA. In these cell lines, the COOH-terminal fragment accumulated in cell nuclei, while the NH2-terminal fragment was in the cytosol. The different distribution of DMP1 fragments indicates that these DMP1 variants must perform distinct functions.

Published
2008
Full Text
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3. Identification of full-length dentin matrix protein 1 in dentin and bone

Author

Yongbo Lu, Lynda F. Bonewald, Bingzhen Huang, Chunlin Qin, Disheng Qin, Yao Sun, Izabela Maciejewska, Jian Q. Feng, Tao Peng, and William T. Butler

Subjects
Endocrinology, Diabetes and Metabolism, Bone Matrix, Fluorescent Antibody Technique, Immunofluorescence, Kidney, Transfection, Article, Extracellular matrix, Mice, Endocrinology, stomatognathic system, Dentin, medicine, Animals, Humans, Orthopedics and Sports Medicine, Peptide sequence, Dental Pulp, Extracellular Matrix Proteins, Viral matrix protein, Osteoblasts, medicine.diagnostic_test, Chemistry, Anatomy, 3T3 Cells, Phosphoproteins, DMP1, Peptide Fragments, Recombinant Proteins, Cell biology, Extracellular Matrix, Rats, stomatognathic diseases, Odontoblast, medicine.anatomical_structure, Protein Processing, Post-Translational
Abstract

Dentin matrix protein 1 (DMP1) has been identified in the extracellular matrix (ECM) of dentin and bone as the processed NH(2)-terminal and COOH-terminal fragment. However, the full-length form of DMP1 has not been identified in these tissues. The focus of this investigation was to search for the intact full-length DMP1 in dentin and bone. We used two types of anti-DMP1 antibodies to identify DMP1: one type specifically recognizes the NH(2)-terminal region and the other type is only reactive to the COOH-terminal region of the DMP1 amino acid sequence. An approximately 105-kDa protein, extracted from the ECM of rat dentin and bone, was recognized by both types of antibodies; and the migration rate of this protein was identical to the recombinant mouse full-length DMP1 made in eukaryotic cells. We concluded that this approximately 105-kDa protein is the full-length form of DMP1, which is considerably less abundant than its processed fragments in the ECM of dentin and bone. We also detected the full-length form of DMP1 and its processed fragments in the extract of dental pulp/odontoblast complex dissected from rat teeth. In addition, immunofluorescence analysis showed that in MC3T3-E1 cells the NH(2)-terminal and COOH-terminal fragments of DMP1 are distributed differently. Our findings indicate that the majority of DMP1 must be cleaved within the cells that synthesize it and that minor amounts of uncleaved DMP1 molecules are secreted into the ECM of dentin and bone.

Published
2008

4. Distinct Compartmentalization of Dentin Matrix Protein 1 Fragments in Mineralized Tissues and Cells.

Author

Maciejewska, Izabela, Disheng Qin, Bingzhen Huang, Yao Sun, Mues, Gabrielle, Svoboda, Kathy, Bonewald, Lynda, Butler, William T., Feng, Jerry Q., and Chunlin Qin

Subjects
*NUTRITION & oral health, *BONE growth, *TISSUES, *DENTAL pulp, *CELL nuclei, *DENTAL matrices, *EXTRACELLULAR matrix proteins
Abstract

Dentin matrix protein 1 (DMP1) has been shown to be critical for the formation of dentin and bone. However, the precise pathway by which DMP1 participates in dentinogenesis and osteogenesis remains to be clarified. DMP1 is present in the extracellular matrix of dentin and bone as processed NH2- and COOH-terminal fragments. The NH2-terminal fragment occurs as a proteoglycan, whereas the COOH-terminal fragment is highly phosphorylated. The differences in biochemical properties suggest that these fragments may have different tissue and cell distribution in association with distinct functions. In this study, we analyzed the distribution of the NH2- and COOH-terminal fragments of DMP1 in tooth, bone, osteocytes as well as MC3T3-E1 and HEK-293 cells. Immunohistochemical analyses were performed using antibodies specific to the NH2- or COOH-terminal region of DMP1. Clear differences in the distribution of these fragments were observed. In the teeth and bone, the NH2-terminal fragment was primarily located in the nonmineralized predentin and cartilage of the growth plate, while the COOH-terminal fragment accumulated in the mineralized zones. In osteocytes, the NH2-terminal fragment appeared more abundant along cell membrane and processes of osteocytes, while the COOH-terminal fragment was often found in the nuclei. This pattern of distribution in cellular compartments was further confirmed by analyses on MC3T3-E1 and HEK-293 cells transfected with a construct containing DMP1 cDNA. In these cell lines, the COOH-terminal fragment accumulated in cell nuclei, while the NH2-terminal fragment was in the cytosol. The different distribution of DMP1 fragments indicates that these DMP1 variants must perform distinct functions. Copyright © 2008 S. Karger AG, Basel [ABSTRACT FROM AUTHOR]

Published
2008
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5. Identification of full-length dentin matrix protein 1 in dentin and bone.

Author

Bingzhen Huang, Maciejewska, Izabela, Yao Sun, Tao Peng, Disheng Qin, Yongbo Lu, Bonewald, Lynda, Butler, William, Jian Feng, Chunlin Qin, Huang, Bingzhen, Sun, Yao, Peng, Tao, Qin, Disheng, Lu, Yongbo, Butler, William T, Feng, Jian, and Qin, Chunlin

Subjects
DENTIN, BONES, PROTEINS, EXTRACELLULAR matrix, IMMUNOGLOBULINS, PROTEIN analysis, OSTEOBLAST metabolism, ANIMALS, CELLS, DENTAL pulp, EXTRACELLULAR space, FLUORESCENT antibody technique, GENETIC techniques, KIDNEYS, MICE, PEPTIDES, PHOSPHOPROTEINS, RATS, RECOMBINANT proteins, OSTEOBLASTS
Abstract

Dentin matrix protein 1 (DMP1) has been identified in the extracellular matrix (ECM) of dentin and bone as the processed NH(2)-terminal and COOH-terminal fragment. However, the full-length form of DMP1 has not been identified in these tissues. The focus of this investigation was to search for the intact full-length DMP1 in dentin and bone. We used two types of anti-DMP1 antibodies to identify DMP1: one type specifically recognizes the NH(2)-terminal region and the other type is only reactive to the COOH-terminal region of the DMP1 amino acid sequence. An approximately 105-kDa protein, extracted from the ECM of rat dentin and bone, was recognized by both types of antibodies; and the migration rate of this protein was identical to the recombinant mouse full-length DMP1 made in eukaryotic cells. We concluded that this approximately 105-kDa protein is the full-length form of DMP1, which is considerably less abundant than its processed fragments in the ECM of dentin and bone. We also detected the full-length form of DMP1 and its processed fragments in the extract of dental pulp/odontoblast complex dissected from rat teeth. In addition, immunofluorescence analysis showed that in MC3T3-E1 cells the NH(2)-terminal and COOH-terminal fragments of DMP1 are distributed differently. Our findings indicate that the majority of DMP1 must be cleaved within the cells that synthesize it and that minor amounts of uncleaved DMP1 molecules are secreted into the ECM of dentin and bone. [ABSTRACT FROM AUTHOR]

Published
2008
Full Text
View/download PDF

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