Role of Matricellular Proteins in Cardiac Allograft Fibrosis

Frerker, Nadine; Kasprzycka, Monika; Mikalsen, Bjørg; Line, Pål–Dag; Scott, Helge; Haraldsen, Guttorm

doi:10.5772/28668

Cited by 2 publications

(2 citation statements)

References 135 publications

(153 reference statements)

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“…Fibroblasts and microvascular endothelial cells have also been shown to express low basal levels of OPN under physiological conditions [17]. The lack of OPN in experimental models of MI injury in rats showed signs of reduced repair as evident by reduced collagen synthesis and deposition in both infarct and non-infarct regions, resulting in ventricular dilation [34]. On the other hand, there appears to be a strong correlation between OPN levels and the severity of several cardiac pathologies [19].…”

Section: Role Of Opn In Heart Diseasementioning

confidence: 99%

Osteopontin: A Promising Therapeutic Target in Cardiac Fibrosis

Mohamed

Gadeau

Hasan

et al. 2019

Cells

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Osteopontin (OPN) is recognized for its significant roles in both physiological and pathological processes. Initially, OPN was recognized as a cytokine with pro-inflammatory actions. More recently, OPN has emerged as a matricellular protein of the extracellular matrix (ECM). OPN is also known to be a substrate for proteolytic cleavage by several proteases that form an integral part of the ECM. In the adult heart under physiological conditions, basal levels of OPN are expressed. Increased expression of OPN has been correlated with the progression of cardiac remodeling and fibrosis to heart failure and the severity of the condition. The intricate process by which OPN mediates its effects include the coordination of intracellular signals necessary for the differentiation of fibroblasts into myofibroblasts, promoting angiogenesis, wound healing, and tissue regeneration. In this review, we discuss the role of OPN in contributing to the development of cardiac fibrosis and its suitability as a therapeutic target.

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Section: Role Of Opn In Heart Diseasementioning

confidence: 99%

Osteopontin: A Promising Therapeutic Target in Cardiac Fibrosis

Mohamed

Gadeau

Hasan

et al. 2019

Cells

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“…POSTN shares a homology with the insect cell adhesion molecule fasciclin I (FASI) and the human

IgH3 (TGFBI) protein, both of which are induced by transforming growth factor-β (TGF-β) [ 8 , 12 ]. Considering the above, POSTN has a similar domain structure to several secreted ECM proteins, such as fibronectin, tenascin-C, and osteopontin; hence, it may be available for action in the stromal cells [ 13 , 14 , 15 ]. In addition, a previous report noted that, in ECM remodeling, POSTN can be effectively induced via various signaling pathways, such as with bone morphogenic protein-2 (BMP 2) to promote inflammation and develop metastatic breast cancer MDA-MB-231 [ 16 ], or with connective tissue growth factor 2, angiotensin II, and mechanical stress.…”

Section: Introductionmentioning

confidence: 99%

Periostin Short Fragment with Exon 17 via Aberrant Alternative Splicing Is Required for Breast Cancer Growth and Metastasis

Ikeda-Iwabu

Taniyama

Katsuragi

et al. 2021

Cells

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Background: Periostin (POSTN) is a 93 kDa matrix protein that helps to regulate collagen gene expression in the extracellular matrix. POSTN overexpression is a prognostic factor in malignant cancers; however, some researchers have observed it in the stroma, whereas others have reported it on tumors. Objective: This study aimed to investigate the function of POSTN on tumors. Methods and Results: We found that POSTN in cancer cells can be detected by using an antibody against the POSTN C-terminal region exon 17 (Ex17 antibody), but not with an antibody against the POSTN N-terminal region exon 12 (Ex12 antibody) in patients with breast cancer. In a fraction secreted from fibroblasts, LC–MS/MS analysis revealed a short fragment of POSTN of approximately 40 kDa with exon 17. In addition, molecular interaction analysis showed that POSTN with exon 17, but not POSTN without exon 17, bound specifically to wnt3a, and the Ex17 antibody inhibited the binding. Conclusion: A short fragment of POSTN with exon 17, which originates in the fibroblasts, is transported to cancer cells, whereas POSTN fragments without exon 17 are retained in the stroma. The Ex17 antibody inhibits the binding between POSTN exon 17 and wnt3a.

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Role of Matricellular Proteins in Cardiac Allograft Fibrosis

Cited by 2 publications

References 135 publications

Osteopontin: A Promising Therapeutic Target in Cardiac Fibrosis

Osteopontin: A Promising Therapeutic Target in Cardiac Fibrosis

Periostin Short Fragment with Exon 17 via Aberrant Alternative Splicing Is Required for Breast Cancer Growth and Metastasis

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