Sequence analysis and neuronal expression of fasciclin I in grasshopper and drosophila

Zinn, Kai; McAllister, Linda B.; Goodman, Corey S.

doi:10.1016/0092-8674(88)90574-0

Cited by 339 publications

(191 citation statements)

References 29 publications

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“…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). Periostin was found to be overexpressed in various types of human cancer such as lung (Sasaki et al, 2001a), brain (Sasaki et al, 2002), ovary (Gillan et al, 2002), breast (Shao et al, 2004) and colon cancers Tai et al, 2005) and elevated levels have been detected in sera of patients with thymoma (Sasaki et al, 2001b), non-small lung carcinoma (Sasaki et al, 2001c) and breast cancer (Sasaki et al, 2003).…”

Section: Introductionmentioning

confidence: 69%

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

257

244

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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.

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Section: Introductionmentioning

confidence: 69%

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

257

244

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“…Periostin contains an N-terminal secretory signal peptide, followed by a cysteine-rich domain, four internal homologous repeats and a C-terminal hydrophilic domain. The four internal repeats region, the fasciclin domains (Fas), exhibit homology to the axon guidance protein Fasciclin I that is involved in the development of nervous system in invertebrates (Zinn et al, 1988). Interestingly, in invertebrates, it is expressed in neurons and attached to the membrane through a glycosylphosphatidylinositol (GPI) anchor (Elkins et al, 1990), whereas in vertebrates, it is a secreted protein with a much broader expression pattern -including heart, periodontal ligament, fibroblasts and Schwann cells.…”

Section: Introductionmentioning

confidence: 99%

Promotion of periostin expression contributes to the migration of Schwann cells

Sonnenberg-Riethmacher

Miehe

Riethmacher

2015

Journal of Cell Science

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Neuregulin ligands and their ErbB receptors are important for the development of Schwann cells, the glial cells of the peripheral nervous system (PNS). ErbB3 deficiency is characterized by a complete loss of Schwann cells along axons of the peripheral nerves, impaired fasciculation and neuronal cell death. We performed comparative gene expression analysis of dorsal root ganglia (DRG) explant cultures from ErbB3-deficient and wild-type mice in order to identify genes that are involved in Schwann cell development and migration. The extracellular matrix (ECM) gene periostin was found to exhibit the most prominent down regulation in ErbB3-deficient DRG. Expression analysis revealed that the periostin-expressing cell population in the PNS corresponds to Schwann cell precursors and Schwann cells, and is particularly high in migratory Schwann cells. Furthermore, stimulation of Schwann cells with neuregulin-1 (NRG1) or transforming growth factor β (TGFβ-1) resulted in an upregulation of periostin expression. Interestingly, DRG explant cultures of periostindeficient mice revealed a significant reduction of the number of migrating Schwann cells. These data demonstrate that the expression of periostin is stimulated by ErbB ligand NRG1 and influences the migration of Schwann cell precursors.

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“…It contains four fasciclin domains that are also observed in the insect protein fasciclin I, which is involved in neuronal cell-cell adhesion (11,12). Periostin expression is low at baseline in many adult tissues, but is strongly induced and secreted into the ECM after acute injury, as well as in dystrophic skeletal muscle (13).…”

mentioning

confidence: 99%

Deletion of periostin reduces muscular dystrophy and fibrosis in mice by modulating the transforming growth factor-β pathway

Lorts

Schwanekamp

Baudino

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

125

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The muscular dystrophies are broadly classified as muscle wasting diseases with myofiber dropout due to cellular necrosis, inflammation, alterations in extracellular matrix composition, and fatty cell replacement. These events transpire and progress despite ongoing myofiber regeneration from endogenous satellite cells. The degeneration/regeneration response to muscle injury/disease is modulated by the proinflammatory cytokine transforming growth factor-β (TGF-β), which can also profoundly influence extracellular matrix composition through increased secretion of profibrotic proteins, such as the matricellular protein periostin. Here we show that up-regulation and secretion of periostin is pathological and enhances disease in the δ-sarcoglycan null ( Sgcd −/− ) mouse model of muscular dystrophy (MD). Indeed, MD mice lacking the Postn gene showed dramatic improvement in skeletal muscle structure and function. Mechanistically, Postn gene deletion altered TGF-β signaling so that it now enhanced tissue regeneration with reduced levels of fibrosis. Systemic antagonism of TGF-β with a neutralizing monoclonal antibody mitigated the beneficial effects of Postn deletion in vivo. These data suggest that periostin functions as a disease determinant in MD by promoting/allowing the pathological effects of TGF-β, suggesting that inhibition of periostin could represent a unique treatment approach.

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Sequence analysis and neuronal expression of fasciclin I in grasshopper and drosophila

Cited by 339 publications

References 29 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

Promotion of periostin expression contributes to the migration of Schwann cells

Deletion of periostin reduces muscular dystrophy and fibrosis in mice by modulating the transforming growth factor-β pathway

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