Molecular characterization and function of tenomodulin, a marker of tendons and ligaments that integrate musculoskeletal components
Tendons and ligaments are dense fibrous bands of connective tissue that integrate musculoskeletal components in vertebrates. Tendons connect skeletal muscles to the bone and function as mechanical force transmitters, whereas ligaments bind adjacent bones together to stabilize joints and restrict unw...
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Format: | Article |
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Elsevier
2016-11-01
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Series: | Japanese Dental Science Review |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S1882761616300072 |
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author | Chisa Shukunami, DDS, PhD Yuki Yoshimoto, DVM, PhD Aki Takimoto, PhD Hiroshi Yamashita, PhD Yuji Hiraki, PhD |
author_facet | Chisa Shukunami, DDS, PhD Yuki Yoshimoto, DVM, PhD Aki Takimoto, PhD Hiroshi Yamashita, PhD Yuji Hiraki, PhD |
author_sort | Chisa Shukunami, DDS, PhD |
collection | DOAJ |
description | Tendons and ligaments are dense fibrous bands of connective tissue that integrate musculoskeletal components in vertebrates. Tendons connect skeletal muscles to the bone and function as mechanical force transmitters, whereas ligaments bind adjacent bones together to stabilize joints and restrict unwanted joint movement. Fibroblasts residing in tendons and ligaments are called tenocytes and ligamentocytes, respectively. Tenomodulin (Tnmd) is a type II transmembrane glycoprotein that is expressed at high levels in tenocytes and ligamentocytes, and is also present in periodontal ligament cells and tendon stem/progenitor cells. Tnmd is related to chondromodulin-1 (Chm1), a cartilage-derived angiogenesis inhibitor, and both Tnmd and Chm1 are expressed in the CD31− avascular mesenchyme. The conserved C-terminal hydrophobic domain of these proteins, which is characterized by the eight Cys residues to form four disulfide bonds, may have an anti-angiogenic function. This review highlights the molecular characterization and function of Tnmd, a specific marker of tendons and ligaments. |
first_indexed | 2024-12-11T15:42:08Z |
format | Article |
id | doaj.art-59412829ce914130bac4edfce7f2fd03 |
institution | Directory Open Access Journal |
issn | 1882-7616 |
language | English |
last_indexed | 2024-12-11T15:42:08Z |
publishDate | 2016-11-01 |
publisher | Elsevier |
record_format | Article |
series | Japanese Dental Science Review |
spelling | doaj.art-59412829ce914130bac4edfce7f2fd032022-12-22T00:59:47ZengElsevierJapanese Dental Science Review1882-76162016-11-01524849210.1016/j.jdsr.2016.04.003Molecular characterization and function of tenomodulin, a marker of tendons and ligaments that integrate musculoskeletal componentsChisa Shukunami, DDS, PhD0Yuki Yoshimoto, DVM, PhD1Aki Takimoto, PhD2Hiroshi Yamashita, PhD3Yuji Hiraki, PhD4Department of Molecular Biology and Biochemistry, Division of Basic Life Sciences, Institute of Biomedical and Health Sciences, Hiroshima University, Hiroshima 734-8553, JapanDepartment of Molecular Biology and Biochemistry, Division of Basic Life Sciences, Institute of Biomedical and Health Sciences, Hiroshima University, Hiroshima 734-8553, JapanDepartment of Cellular Differentiation, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8507, JapanDepartment of Molecular Biology and Biochemistry, Division of Basic Life Sciences, Institute of Biomedical and Health Sciences, Hiroshima University, Hiroshima 734-8553, JapanDepartment of Cellular Differentiation, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8507, JapanTendons and ligaments are dense fibrous bands of connective tissue that integrate musculoskeletal components in vertebrates. Tendons connect skeletal muscles to the bone and function as mechanical force transmitters, whereas ligaments bind adjacent bones together to stabilize joints and restrict unwanted joint movement. Fibroblasts residing in tendons and ligaments are called tenocytes and ligamentocytes, respectively. Tenomodulin (Tnmd) is a type II transmembrane glycoprotein that is expressed at high levels in tenocytes and ligamentocytes, and is also present in periodontal ligament cells and tendon stem/progenitor cells. Tnmd is related to chondromodulin-1 (Chm1), a cartilage-derived angiogenesis inhibitor, and both Tnmd and Chm1 are expressed in the CD31− avascular mesenchyme. The conserved C-terminal hydrophobic domain of these proteins, which is characterized by the eight Cys residues to form four disulfide bonds, may have an anti-angiogenic function. This review highlights the molecular characterization and function of Tnmd, a specific marker of tendons and ligaments.http://www.sciencedirect.com/science/article/pii/S1882761616300072TenomodulinChondromoulin-1ScleraxisTendonLigamentAnti-angiogenic factor |
spellingShingle | Chisa Shukunami, DDS, PhD Yuki Yoshimoto, DVM, PhD Aki Takimoto, PhD Hiroshi Yamashita, PhD Yuji Hiraki, PhD Molecular characterization and function of tenomodulin, a marker of tendons and ligaments that integrate musculoskeletal components Japanese Dental Science Review Tenomodulin Chondromoulin-1 Scleraxis Tendon Ligament Anti-angiogenic factor |
title | Molecular characterization and function of tenomodulin, a marker of tendons and ligaments that integrate musculoskeletal components |
title_full | Molecular characterization and function of tenomodulin, a marker of tendons and ligaments that integrate musculoskeletal components |
title_fullStr | Molecular characterization and function of tenomodulin, a marker of tendons and ligaments that integrate musculoskeletal components |
title_full_unstemmed | Molecular characterization and function of tenomodulin, a marker of tendons and ligaments that integrate musculoskeletal components |
title_short | Molecular characterization and function of tenomodulin, a marker of tendons and ligaments that integrate musculoskeletal components |
title_sort | molecular characterization and function of tenomodulin a marker of tendons and ligaments that integrate musculoskeletal components |
topic | Tenomodulin Chondromoulin-1 Scleraxis Tendon Ligament Anti-angiogenic factor |
url | http://www.sciencedirect.com/science/article/pii/S1882761616300072 |
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