NELL-1 promotes cell adhesion and differentiation via integrinβ1

NELL‐1 (Nel‐like molecule‐1) is a secreted osteogenic growth factor first identified in human craniosynostosis (CS) patients. NELL‐1 protein has been observed to promote bone and cartilage differentiation and to suppress adipogenesis in both in vitro and in vivo models. Despite these findings, the c...

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Published in:	Journal of cellular biochemistry Vol. 113; no. 12; pp. 3620 - 3628
Main Authors:	Shen, Jia, James, Aaron W., Chung, Jonguk, Lee, Kiho, Zhang, James B., Ho, Stephanie, Lee, Kevin S., Kim, Toyong M., Niimi, Tomoaki, Kuroda, Shun'ichi, Ting, Kang, Soo, Chia
Format:	Journal Article
Language:	English
Published:	Hoboken Wiley Subscription Services, Inc., A Wiley Company 01-12-2012
Subjects:	3T3 Cells Amino Acid Sequence Animals Blotting, Western CELL ADHERENCE Cell Adhesion Cell Differentiation Cell Proliferation FAK Focal Adhesions Humans Immunohistochemistry Integrin beta1 - genetics Integrin beta1 - metabolism INTEGRINβ1 Lactic Acid - metabolism Mice Molecular Sequence Data NELL-1 Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Osteogenesis OSTEOGENIC DIFFERENTIATION Polyglycolic Acid - metabolism Protein Binding Protein Interaction Mapping RNA, Small Interfering Sequence Alignment ST2
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Abstract	NELL‐1 (Nel‐like molecule‐1) is a secreted osteogenic growth factor first identified in human craniosynostosis (CS) patients. NELL‐1 protein has been observed to promote bone and cartilage differentiation and to suppress adipogenesis in both in vitro and in vivo models. Despite these findings, the cell surface receptors of NELL‐1 have remained unknown. In this study, we observed for the first time that NELL‐1 promotes cell adherence in multiple cell lines, including ST2, C3H10T1/2, M2‐10B4, ATDC5, and MC3T3 cells. Additionally, we found that NELL‐1 binds to extracellular Integrinβ1 and induces cell focal adhesion. By utilizing siRNA methods, we determined that NELL‐1 cell surface binding and enhanced cell attachment were dependent on Integrinβ1 expression. Finally, we observed that pre‐coating of culture dishes or PLGA (polylactic‐co‐glycolic acid) scaffold with NELL‐1 resulted in a significant increase in both cell attachment and osteogenic differentiation. Our results identify for the first time a cell surface target of NELL‐1, Integrinβ1, and elucidate new functions of NELL‐1 in promoting cell adherence and osteogenic differentiation. J. Cell. Biochem. 113: 3620–3628, 2012. © 2012 Wiley Periodicals, Inc.
AbstractList	NELL-1 (Nel-like molecule-1) is a secreted osteogenic growth factor first identified in human craniosynostosis (CS) patients. NELL-1 protein has been observed to promote bone and cartilage differentiation and to suppress adipogenesis in both in vitro and in vivo models. Despite these findings, the cell surface receptors of NELL-1 have remained unknown. In this study, we observed for the first time that NELL-1 promotes cell adherence in multiple cell lines, including ST2, C3H10T1/2, M2-10B4, ATDC5, and MC3T3 cells. Additionally, we found that NELL-1 binds to extracellular Integrinβ1 and induces cell focal adhesion. By utilizing siRNA methods, we determined that NELL-1 cell surface binding and enhanced cell attachment were dependent on Integrinβ1 expression. Finally, we observed that pre-coating of culture dishes or PLGA (polylactic-co-glycolic acid) scaffold with NELL-1 resulted in a significant increase in both cell attachment and osteogenic differentiation. Our results identify for the first time a cell surface target of NELL-1, Integrinβ1, and elucidate new functions of NELL-1 in promoting cell adherence and osteogenic differentiation. NELL‐1 (Nel‐like molecule‐1) is a secreted osteogenic growth factor first identified in human craniosynostosis (CS) patients. NELL‐1 protein has been observed to promote bone and cartilage differentiation and to suppress adipogenesis in both in vitro and in vivo models. Despite these findings, the cell surface receptors of NELL‐1 have remained unknown. In this study, we observed for the first time that NELL‐1 promotes cell adherence in multiple cell lines, including ST2, C3H10T1/2, M2‐10B4, ATDC5, and MC3T3 cells. Additionally, we found that NELL‐1 binds to extracellular Integrinβ1 and induces cell focal adhesion. By utilizing siRNA methods, we determined that NELL‐1 cell surface binding and enhanced cell attachment were dependent on Integrinβ1 expression. Finally, we observed that pre‐coating of culture dishes or PLGA (polylactic‐co‐glycolic acid) scaffold with NELL‐1 resulted in a significant increase in both cell attachment and osteogenic differentiation. Our results identify for the first time a cell surface target of NELL‐1, Integrinβ1, and elucidate new functions of NELL‐1 in promoting cell adherence and osteogenic differentiation. J. Cell. Biochem. 113: 3620–3628, 2012. © 2012 Wiley Periodicals, Inc. NELL‐1 (Nel‐like molecule‐1) is a secreted osteogenic growth factor first identified in human craniosynostosis (CS) patients. NELL‐1 protein has been observed to promote bone and cartilage differentiation and to suppress adipogenesis in both in vitro and in vivo models. Despite these findings, the cell surface receptors of NELL‐1 have remained unknown. In this study, we observed for the first time that NELL‐1 promotes cell adherence in multiple cell lines, including ST2, C3H10T1/2, M2‐10B4, ATDC5, and MC3T3 cells. Additionally, we found that NELL‐1 binds to extracellular Integrinβ1 and induces cell focal adhesion. By utilizing siRNA methods, we determined that NELL‐1 cell surface binding and enhanced cell attachment were dependent on Integrinβ1 expression. Finally, we observed that pre‐coating of culture dishes or PLGA (polylactic‐ co ‐glycolic acid) scaffold with NELL‐1 resulted in a significant increase in both cell attachment and osteogenic differentiation. Our results identify for the first time a cell surface target of NELL‐1, Integrinβ1, and elucidate new functions of NELL‐1 in promoting cell adherence and osteogenic differentiation. J. Cell. Biochem. 113: 3620–3628, 2012. © 2012 Wiley Periodicals, Inc.
Author	Shen, Jia James, Aaron W. Kuroda, Shun'ichi Chung, Jonguk Zhang, James B. Ting, Kang Soo, Chia Ho, Stephanie Niimi, Tomoaki Kim, Toyong M. Lee, Kiho Lee, Kevin S.
Author_xml	– sequence: 1 givenname: Jia surname: Shen fullname: Shen, Jia organization: Dental and Craniofacial Research Institute and Section of Orthodontics, School of Dentistry, University of California, Los Angeles, Los Angeles, California 90095 – sequence: 2 givenname: Aaron W. surname: James fullname: James, Aaron W. organization: Dental and Craniofacial Research Institute and Section of Orthodontics, School of Dentistry, University of California, Los Angeles, Los Angeles, California 90095 – sequence: 3 givenname: Jonguk surname: Chung fullname: Chung, Jonguk organization: Dental and Craniofacial Research Institute and Section of Orthodontics, School of Dentistry, University of California, Los Angeles, Los Angeles, California 90095 – sequence: 4 givenname: Kiho surname: Lee fullname: Lee, Kiho organization: Dental and Craniofacial Research Institute and Section of Orthodontics, School of Dentistry, University of California, Los Angeles, Los Angeles, California 90095 – sequence: 5 givenname: James B. surname: Zhang fullname: Zhang, James B. organization: Dental and Craniofacial Research Institute and Section of Orthodontics, School of Dentistry, University of California, Los Angeles, Los Angeles, California 90095 – sequence: 6 givenname: Stephanie surname: Ho fullname: Ho, Stephanie organization: Dental and Craniofacial Research Institute and Section of Orthodontics, School of Dentistry, University of California, Los Angeles, Los Angeles, California 90095 – sequence: 7 givenname: Kevin S. surname: Lee fullname: Lee, Kevin S. organization: Dental and Craniofacial Research Institute and Section of Orthodontics, School of Dentistry, University of California, Los Angeles, Los Angeles, California 90095 – sequence: 8 givenname: Toyong M. surname: Kim fullname: Kim, Toyong M. organization: Dental and Craniofacial Research Institute and Section of Orthodontics, School of Dentistry, University of California, Los Angeles, Los Angeles, California 90095 – sequence: 9 givenname: Tomoaki surname: Niimi fullname: Niimi, Tomoaki organization: Department of Bioengineering Sciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furocho, Chikusa-ku, Nagoya 464-8601, Japan – sequence: 10 givenname: Shun'ichi surname: Kuroda fullname: Kuroda, Shun'ichi organization: Department of Bioengineering Sciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furocho, Chikusa-ku, Nagoya 464-8601, Japan – sequence: 11 givenname: Kang surname: Ting fullname: Ting, Kang email: kting@dentistry.ucla.edu organization: Dental and Craniofacial Research Institute and Section of Orthodontics, School of Dentistry, University of California, Los Angeles, Los Angeles, California 90095 – sequence: 12 givenname: Chia surname: Soo fullname: Soo, Chia email: bsoo@ucla.edu organization: UCLA and Orthopaedic Hospital, Department of Orthopaedic Surgery and the Orthopaedic Hospital Research Center, University of California, Los Angeles, Los Angeles, California 90095
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Snippet	NELL‐1 (Nel‐like molecule‐1) is a secreted osteogenic growth factor first identified in human craniosynostosis (CS) patients. NELL‐1 protein has been observed... NELL-1 (Nel-like molecule-1) is a secreted osteogenic growth factor first identified in human craniosynostosis (CS) patients. NELL-1 protein has been observed...
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SubjectTerms	3T3 Cells Amino Acid Sequence Animals Blotting, Western CELL ADHERENCE Cell Adhesion Cell Differentiation Cell Proliferation FAK Focal Adhesions Humans Immunohistochemistry Integrin beta1 - genetics Integrin beta1 - metabolism INTEGRINβ1 Lactic Acid - metabolism Mice Molecular Sequence Data NELL-1 Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Osteogenesis OSTEOGENIC DIFFERENTIATION Polyglycolic Acid - metabolism Protein Binding Protein Interaction Mapping RNA, Small Interfering Sequence Alignment ST2
Title	NELL-1 promotes cell adhesion and differentiation via integrinβ1
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