The Structure of the Periostin Gene, Its Transcriptional Control and Alternative Splicing, and Protein Expression

Kudo, Akira

doi:10.1007/978-981-13-6657-4_2

Cited by 18 publications

(13 citation statements)

References 98 publications

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“…Moreover, the EMI domain is essential for the multimerization of POSTN and can promote the cross‐linking of collagen by forming a network structure with fibronectin and tenascin C (Zhu et al 2021). Because of this, POSTN promotes the infiltration and contraction of the ECM (Kudo 2019a). The four‐repeat fasciclin‐like (FAS1) domain, a tandem repeat of four FAS1 domains, was originally a neural cell adhesion molecule found in insects (Clout and Hohenester 2003; Clout et al 2003).…”

Section: The Structure Of Postnmentioning

confidence: 99%

“…With a molecular weight of 90 kDa, POSTN contains an N-terminal secretory signal peptide, followed by a cysteine-rich domain (EMI domain), four tandem repeats of FAS1 domains, and a hydrophilic carboxy-terminal structure domain (CTD). Having been proven to bind to a variety of proteins, including ECM proteins, these different domains have diverse biological functions (Kudo 2017(Kudo , 2019a. Although POSTN does not directly participate in the formation of the ECM, it plays an important role in the interaction between the cell and the surrounding microenvironment due to its fine composition structure.…”

Section: Introductionmentioning

confidence: 99%

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Periostin: an emerging activator of multiple signaling pathways

Wang

Zhu

et al. 2022

J. Cell Commun. Signal.

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Matricellular proteins are responsible for regulating the microenvironment, the behaviors of surrounding cells, and the homeostasis of tissues. Periostin (POSTN), a non‐structural matricellular protein, can bind to many extracellular matrix proteins through its different domains. POSTN usually presents at low levels in most adult tissues but is highly expressed in pathological sites such as in tumors and inflamed organs. POSTN can bind to diverse integrins to interact with multiple signaling pathways within cells, which is one of its core biological functions. Increasing evidence shows that POSTN can activate the TGF‐β, the PI3K/Akt, the Wnt, the RhoA/ROCK, the NF‐κB, the MAPK and the JAK pathways to promote the occurrence and development of many diseases, especially cancer and inflammatory diseases. Furthermore, POSTN can interact with some pathways in an upstream and downstream relationship, forming complicated crosstalk. This article focuses on the interactions between POSTN and different signaling pathways in diverse diseases, attempting to explain the mechanisms of interaction and provide novel guidelines for the development of targeted therapies.

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Section: The Structure Of Postnmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Periostin: an emerging activator of multiple signaling pathways

Wang

Zhu

et al. 2022

J. Cell Commun. Signal.

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“…These findings have suggested that Postn might increase scar formation and myocardial remodelling post myocardial infarction. The human Postn gene forms seven splicing isomers including full-length Postn through alternative splicing between exons 17 and 21 [ 34 ]. Balbi et al proposed in their latest study that exosomes secreted by human explant-derived cardiac progenitor cells (CPC) promoted cardiomyocyte re-entry cycle and proliferation via Postn subtypes expressed on their surface, while recombinant full-length Postn did not yield the same results [ 35 ].…”

Section: Discussionmentioning

confidence: 99%

Candidate genes and their alternative splicing may be potential biomarkers of acute myocardial infarction: a study of mouse model

Liu

Zhang

et al. 2022

BMC Cardiovasc Disord

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Background Acute myocardial infarction (AMI) is one of the leading causes of death in human being, and an effective diagnostic biomarker is still lacking. Whilst some gene association with AMI has been identified by RNA sequencing (RNA-seq), the relationship between alternative splicing and AMI is not clear. Methods We retrieved myocardial tissues within 24 h from mice with induced AMI and sham, and analysed the differentially expressed genes (DEGs) and differential alternative splicing genes (DASGs) by RNA-seq. The Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis and protein interaction network analysis were performed on DEGs-DASGs-overlap genes. PCR was used to verify the expression levels of representative genes and alternative splicing in myocardial tissues of AMI and sham mice. Results 1367 DEGs were identified, including 242 up-regulated and 1125 down-regulated genes, among which there were 42 DASGs. GO analysis showed that the cellular component was primarily enriched in plasma membrane, cell membrane integrity and extracellular region. The molecular function was enriched in protein binding and metal ion binding. The biological process was primarily enriched in cell adhesion, immune system process and cell differentiation. KEGG analysis showed the enrichment was mainly in JAK-STAT and PI3K-AKT signalling pathway. Postn, Fhl1, and Fn1 were low-expressed while Postn alternative splicing was high-expressed in myocardial tissue of AMI mice, which was consistent with sequencing results. Conclusions The pathogenesis of AMI involves differentially expressed genes and differential alternative splicing. These differentially expressed genes and their alternative splicing, especially, Fhl1, Fn1 and Postn may become new biomarkers of AMI.

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“…Basic research suggests that Periostin can regulate bone formation, promote bone development/remodeling, and increase bone strength. It is a key regulator of bone microstructure and plays a very important role in bone metabolism [73,74]. Regarding the clinical study of periostin, showed through crosssectional observation in postmenopausal women that periostin has no significant correlation with the overall BMD [75], but is positively correlated with cortical bone density, negatively correlated with cortical bone porosity.…”

Section: Periostinmentioning

confidence: 99%

Advances in Clinical Application of Bone Mineral Density and Bone Turnover Markers

Li¹,

Yuan²,

Wang³

et al. 2024

Biomechanical Insights Into Osteoporosis

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Bone mineral density is the main basis for the diagnosis of osteoporosis. The measurement methods of bone mineral density include dual X-ray absorptiometry (DXA), quantitative computer tomography (QCT), quantitative ultrasound (QUS), magnetic resonance imaging (MRI) and so on. Currently, bone mineral density measured by dual-energy X-ray absorptiometry (DXA) is the gold standard for the diagnosis of osteoporosis. Bone turnover markers (BTMs) are biochemical products that reflect the activity of bone cells and the metabolic level of bone matrix, and they reflect the dynamic changes of bone tissue in the whole body earlier than bone mineral-density, procollagen type 1 N-terminal propeptide (PINP) and carboxy-terminal cross-linked telopeptide of type 1 collagen (CTX) is sensitive BTMs, widely used in clinical practice, and can predict the occurrence of fractures. Some new markers such as Periostin, AGEs/RAGE, Gelsolin, and Annexin A2 provide new clues for exploring the mechanism of osteoporosis. The combination of the two can better carry out the diagnosis and differential diagnosis of multiple metabolic bone diseases, evaluate the therapeutic response of anti-osteoporotic medicines, and predict fracture risk.

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The Structure of the Periostin Gene, Its Transcriptional Control and Alternative Splicing, and Protein Expression

Cited by 18 publications

References 98 publications

Periostin: an emerging activator of multiple signaling pathways

Periostin: an emerging activator of multiple signaling pathways

Candidate genes and their alternative splicing may be potential biomarkers of acute myocardial infarction: a study of mouse model

Advances in Clinical Application of Bone Mineral Density and Bone Turnover Markers

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