Gene expression of periostin in the early stage of fracture healing detected by cDNA microarray analysis

Nakazawa, Tetsuro; Nakajima, Arata; Seki, Naohiko; Okawa, Akihiko; Kato, Masaki; Moriya, Hisao; Amizuka, Norio; Einhorn, Thomas A.; Yamazaki, Masashi

doi:10.1016/j.orthres.2003.10.007

Cited by 129 publications

(45 citation statements)

References 19 publications

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“…Periostin has been shown also to have a role in bone, tooth and heart formation during development (26, 27) and is only re-expressed and upregulated in adult tissue after vascular, skeletal or bone injuries (28, 29). Periostin is similarly overexpressed in human cancers (14), (30).…”

Section: Discussionmentioning

confidence: 99%

Periostin, a Cell Adhesion Molecule, Facilitates Invasion in the Tumor Microenvironment and Annotates a Novel Tumor-Invasive Signature in Esophageal Cancer

et al. 2010

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Human squamous cell cancers are the most common epithelially derived malignancies. One example is esophageal squamous cell carcinoma (ESCC), which is associated with a high mortality rate (1) that is related to a propensity for invasion and metastasis (2). Here we report that periostin, a highly expressed cell adhesion molecule, is a key component of a novel tumor invasive signature obtained from an organotypic culture model of engineered ESCC. This tumor invasive signature classifies with human ESCC microarrays, underscoring its utility in human cancer. Genetic modulation of periostin promotes tumor cell migration and invasion as revealed in gain of and loss of function experiments. Inhibition of EGFR signaling and restoration of wild-type p53 function were each found to attenuate periostin, suggesting interdependence of two common genetic alterations with periostin function. Collectively, our studies reveal periostin as an important mediator of ESCC tumor invasion and they indicate that organotypic (3D) culture can offer an important tool to discover novel biologic effectors in cancer.

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Section: Discussionmentioning

confidence: 99%

Periostin, a Cell Adhesion Molecule, Facilitates Invasion in the Tumor Microenvironment and Annotates a Novel Tumor-Invasive Signature in Esophageal Cancer

et al. 2010

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“…Although the exact function of periostin in bones remains elusive, its continuous expression from development to postnatal life as well as up-regulation during fracture healing underlines its importance in bone maintenance and regeneration (41). Because MSCs represent a specific bone stem cell pool participating in bone development and repair (42,43), we propose that MSC-derived periostin is a key player in these processes.…”

Section: Discussionmentioning

confidence: 97%

Periostin, a Member of a Novel Family of Vitamin K-dependent Proteins, Is Expressed by Mesenchymal Stromal Cells

Coutu

Monette

et al. 2008

Journal of Biological Chemistry

158

136

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The modification of glutamic acid residues to ␥-carboxyglutamic acid (Gla) is a post-translational modification catalyzed by the vitamin K-dependent enzyme ␥-glutamylcarboxylase. Despite ubiquitous expression of the ␥-carboxylation machinery in mammalian tissues, only 12 Gla-containing proteins have so far been identified in humans. Because bone tissue is the second most abundant source of Gla-containing proteins after the liver, we sought to identify Gla proteins secreted by bone marrow-derived mesenchymal stromal cells (MSCs). We used a proteomics approach to screen the secretome of MSCs with a combination of two-dimensional gel electrophoresis and tandem mass spectrometry. The most abundant Gla-containing protein secreted by MSCs was identified as periostin, a previously unrecognized ␥-carboxylated protein. In silico amino acid sequence analysis of periostin demonstrated the presence of four consensus ␥-carboxylase recognition sites embedded within fasciclin-like protein domains. The carboxylation of periostin was confirmed by immunoprecipitation and purification of the recombinant protein. Carboxylation of periostin could be inhibited by warfarin in MSCs, demonstrating its dependence on the presence of vitamin K. We were able to demonstrate localization of carboxylated periostin to bone nodules formed by MSCs in vitro, suggesting a role in extracellular matrix mineralization. Our data also show that another fasciclin I-like protein, ␤ig-h3, contains Gla. In conclusion, periostin is a member of a novel vitamin K-dependent ␥-carboxylated protein family characterized by the presence of fasciclin domains. Furthermore, carboxylated periostin is produced by bone-derived cells of mesenchymal lineage and is abundantly found in mineralized bone nodules in vitro.

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“…In adults, periostin is re-expressed during fracture repair or in response to mechanical stress when bone development and remodeling is required [30]. A complete picture of the differential expression of the periostin isoforms is needed to understand the role of the variants in bone development, maturation, and repair.…”

Section: Role Of Periostin In Health and Diseasementioning

confidence: 99%

The role of periostin in tissue remodeling across health and disease

Conway

Izuhara

Kudo

et al. 2013

Cell. Mol. Life Sci.

331

313

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Periostin, also termed osteoblast-specific factor 2, is a matricellular protein with known functions in osteology, tissue repair, oncology, cardiovascular and respiratory systems, and in various inflammatory settings. However, most of the research to date has been conducted in divergent and circumscribed areas meaning that the overall understanding of this intriguing molecule remains fragmented. Here, we integrate the available evidence on periostin expression, its normal role in development, and whether it plays a similar function during pathologic repair, regeneration, and disease in order to bring together the different research fields in which periostin investigations are ongoing. In spite of the seemingly disparate roles of periostin in health and disease, tissue remodeling as a response to insult/injury is emerging as a common functional denominator of this matricellular molecule. Periostin is transiently upregulated during cell fate changes, either physiologic or pathologic. Combining observations from various conditions, a common pattern of events can be suggested, including periostin localization during development, insult and injury, epithelial–mesenchymal transition, extracellular matrix restructuring, and remodeling. We propose mesenchymal remodeling as an overarching role for the matricellular protein periostin, across physiology and disease. Periostin may be seen as an important structural mediator, balancing appropriate versus inappropriate tissue adaption in response to insult/injury.

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Gene expression of periostin in the early stage of fracture healing detected by cDNA microarray analysis

Cited by 129 publications

References 19 publications

Periostin, a Cell Adhesion Molecule, Facilitates Invasion in the Tumor Microenvironment and Annotates a Novel Tumor-Invasive Signature in Esophageal Cancer

Periostin, a Cell Adhesion Molecule, Facilitates Invasion in the Tumor Microenvironment and Annotates a Novel Tumor-Invasive Signature in Esophageal Cancer

Periostin, a Member of a Novel Family of Vitamin K-dependent Proteins, Is Expressed by Mesenchymal Stromal Cells

The role of periostin in tissue remodeling across health and disease

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