Osteoblast-specific factor 2: cloning of a putative bone adhesion protein with homology with the insect protein fasciclin I

Takeshita, Satoshi; Kikuno, Reiko; Tezuka, Kenichi; Amann, Egon

doi:10.1042/bj2940271

Cited by 595 publications

(602 citation statements)

References 35 publications

Supporting

Mentioning

566

Contrasting

Unclassified

Order By: Relevance

“…Periostin has a typical signal sequence, followed by a cysteine-rich domain, four repeated and conserved domains and a C-terminal hydrophilic domain (Takeshita et al, 1993;Horiuchi et al, 1999). A similar structure was reported for fasciclin I, a cell adhesion molecule involved in the development of the central nervous system of insects (Zinn et al, 1988), and for the big-h3 molecule, a secreted protein induced by TGF-b1 which promotes the attachment and spreading of fibroblasts (Skonier et al, 1992;LeBaron et al, 1995).…”

Section: Introductionmentioning

confidence: 66%

“…Periostin is a secreted 90 kDa protein originally identified as an osteoblast-specific factor preferentially expressed in the periosteum in bone tissues (Takeshita et al, 1993;Horiuchi et al, 1999). Periostin has a typical signal sequence, followed by a cysteine-rich domain, four repeated and conserved domains and a C-terminal hydrophilic domain (Takeshita et al, 1993;Horiuchi et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Periostin promotes invasiveness and resistance of pancreatic cancer cells to hypoxia-induced cell death: role of the β4 integrin and the PI3k pathway

Baril¹,

Gangeswaran²,

Mahon³

et al. 2006

Oncogene

256

244

View full text Add to dashboard Cite

Pancreatic ductal adenocarcinoma is a devastating disease, characterized by a rapid progression and poor treatment response. Using gene expression profiling of pancreatic cancer tissues, we previously identified periostin as a potential diagnostic and therapeutic target. In this study, we report the overexpression of periostin in a larger set of pancreatic cancer tissues and show that although the periostin transcript is exclusively expressed in tumour cells, the protein product is only detected in the extracellular matrix adjacent to cancer cells. Using an enzyme-linked immunosorbent assay (ELISA) assay, we show significantly increased levels of periostin in the sera of pancreatic cancer patients compared to non-cancer controls. We demonstrate that periostin promotes the invasiveness of tumour cells by increasing the motility of cells without inducing expression of proteases, and enhances the survival of tumour cells exposed to hypoxic conditions. At the molecular level, we provide evidence that the a 6 b 4 integrin complex acts as the cell receptor of periostin in pancreatic cancer cells and that interaction promotes phosphorylation of focal adhesion kinase (FAK) and protein kinase B (AKT) though activation of the PI3 kinase pathway, but not the RAS/MEK/ERK pathway. These findings suggest an important role of periostin in pancreatic cancer and provide a rationale to study periostin for diagnostic and therapeutic applications.

show abstract

Section: Introductionmentioning

confidence: 66%

Section: Introductionmentioning

confidence: 99%

Periostin promotes invasiveness and resistance of pancreatic cancer cells to hypoxia-induced cell death: role of the β4 integrin and the PI3k pathway

Baril¹,

Gangeswaran²,

Mahon³

et al. 2006

Oncogene

256

244

View full text Add to dashboard Cite

show abstract

“…OSF2 is expressed in osteoblasts and lung tissue (Takeshita et al, 1993) and has shown altered expression in a number of human tumors (Gillan et al, 2002;Yoshioka et al, 2002). OSF2 has been suggested to have a tumor suppressor function in human oncogenesis (Yoshioka et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

Exploration of replicative senescence-associated genes in human dermal fibroblasts by cDNA microarray technology

Yoon

Kim

et al. 2004

Experimental Gerontology

109

View full text Add to dashboard Cite

“…Periostin was originally identified as an 811-amino acid protein secreted by murine osteoblasts, which had structural homology to the insect axonal guidance protein fasciclin-1 (Takeshita et al 1993). Originally termed osteoblast specific factor-2 (OSF-2), it was renamed periostin due localized expression in the periosteum and the periodontal ligament (Kruzynska-Frejtag et al 2004).…”

Section: Periostin: a Novel Matricellular Proteinmentioning

confidence: 99%

Functional role of periostin in development and wound repair: implications for connective tissue disease

Hamilton

2008

Journal of Cell Communication and Signaling

175

191

View full text Add to dashboard Cite

Integrity of the extracellular matrix (ECM) is essential for maintaining the normal structure and function of connective tissues. ECM is secreted locally by cells and organized into a complex meshwork providing physical support to cells, tissues, and organs. Initially thought to act only as a scaffold, the ECM is now known to provide a myriad of signals to cells regulating all aspects of their phenotype from morphology to differentiation. Matricellular proteins are a class of ECM related molecules defined through their ability to modulate cell–matrix interactions. Matricellular proteins are expressed at high levels during development, but typically only appear in postnatal tissue in wound repair or disease, where their levels increase substantially. Members of the CCN family, tenascin‐C, osteopontin, secreted protein acidic rich in cysteine (SPARC), bone sialoprotein, thrombospondins, and galectins have all been classed as matricellular proteins. Periostin, a 90 kDa secreted homophilic cell adhesion protein, was recently added to matricellular class of proteins based on its expression pattern and function during development as well as in wound repair. Periostin is expressed in connective tissues including the periodontal ligament, tendons, skin and bone, and is also prominent in neoplastic tissues, cardiovascular disease, as well as in connective tissue wound repair. This review will focus on the functional role of periostin in tissue physiology. Fundamentally, it appears that periostin influences cell behaviour as well as collagen fibrillogenesis, and therefore exerts control over the structural and functional properties of connective tissues in both health and disease. Periostin is a novel matricellular protein with close homology to Drosophila fasciclin 1. In this review, the functional role of periostin is discussed in the context of connective tissue physiology, in development, disease, and wound repair.

show abstract

Osteoblast-specific factor 2: cloning of a putative bone adhesion protein with homology with the insect protein fasciclin I

Cited by 595 publications

References 35 publications

Periostin promotes invasiveness and resistance of pancreatic cancer cells to hypoxia-induced cell death: role of the β4 integrin and the PI3k pathway

Periostin promotes invasiveness and resistance of pancreatic cancer cells to hypoxia-induced cell death: role of the β4 integrin and the PI3k pathway

Exploration of replicative senescence-associated genes in human dermal fibroblasts by cDNA microarray technology

Functional role of periostin in development and wound repair: implications for connective tissue disease

Contact Info

Product

Resources

About