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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Main Authors: Chisa Shukunami, DDS, PhD, Yuki Yoshimoto, DVM, PhD, Aki Takimoto, PhD, Hiroshi Yamashita, PhD, Yuji Hiraki, PhD
Format: Article
Language:English
Published: Elsevier 2016-11-01
Series:Japanese Dental Science Review
Subjects:
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.
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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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