Journal ArticleDOI
Lumican expression is positively correlated with the differentiation and negatively with the growth of human osteosarcoma cells
Dragana Nikitovic,Aikaterini Berdiaki,Alexandros Zafiropoulos,Pavlos Katonis,Aristidis Tsatsakis,Nikos K. Karamanos,George N. Tzanakakis +6 more
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TLDR
Examination of the expression of lumican in moderately differentiated and well‐differentiated human osteosarcoma cell lines of high and low metastatic capability suggests that lumican expression may be positively correlation with the differentiation and negatively correlated with the progression of osteosARcoma.Citations
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Extracellular matrix structure.
TL;DR: The complex ECM structure is emphasized as to provide a better understanding of its dynamic structural and functional multipotency and the implication of the various families of ECM macromolecules in health and disease is presented.
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Proteoglycan form and function: A comprehensive nomenclature of proteoglycans
Renato V. Iozzo,Liliana Schaefer +1 more
TL;DR: The proposed nomenclature encompasses forty-three distinct proteoglycan-encoding genes and many alternatively-spliced variants and is based on three criteria: Cellular and subcellular location, overall gene/protein homology, and the utilization of specific protein modules within their respective protein cores.
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Proteoglycans in cancer biology, tumour microenvironment and angiogenesis
TL;DR: Decorin and growth control, and genetic evidence for a role for decorin in carcinogenesis and mechanism of decorin action: suppression of β‐catenin and Myc levels are presented.
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Proteoglycans in health and disease: novel roles for proteoglycans in malignancy and their pharmacological targeting.
TL;DR: Enhanced understanding of the regulation of PG metabolism and the involvement of PGs in cancer may offer a novel approach to cancer therapy by targeting the tumor microenvironment.
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Proteoglycans remodeling in cancer: Underlying molecular mechanisms.
TL;DR: This review summarizes the proteoglycans remodeling and their novel biological roles in malignancies with particular emphasis to the underlying molecular mechanisms.
References
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Journal ArticleDOI
Role of integrins in cell invasion and migration
John Hood,David A. Cheresh +1 more
TL;DR: As cancer cells undergo metastasis — invasion and migration of a new tissue — they penetrate and attach to the target tissue's basal matrix, which allows the cancer cell to pull itself forward into the tissue.
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The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth.
TL;DR: These proteoglycans are tissue organizers, orienting and ordering collagen fibrils during ontogeny and in pathological processes such as wound healing, tissue repair, and tumor stroma formation, and three-dimensional modeling of their prototype protein core proposes a flexible, arch-shaped binding surface suitable for strong and distinctive interactions with ligand proteins.
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Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases
Laurent Ameye,Marian F. Young +1 more
TL;DR: Although the distinct phenotypes developed by the different singly deficient mice point to distinct in vivo function for each SLRP, the analysis of the double-deficient mice also demonstrates the existence of rescuing/compensation mechanisms, indicating some functional overlap within the SLRP family.
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Interactions between integrin receptors and fibronectin are required for calvarial osteoblast differentiation in vitro
TL;DR: The results indicate that direct osteoblast interactions with the extracellular matrix are mediated by a select group of integrin receptors that includes alpha5ss1, alpha3ss1 and alpha8ss1.
Journal ArticleDOI
TGF‐β signaling: A tale of two responses
Rod A. Rahimi,Edward B. Leof +1 more
TL;DR: TGF‐β signaling in epithelial cells and fibroblasts is reviewed with a focus on understanding the mechanisms of TGF‐ β versatility, which is implicated in promoting carcinogenesis and fibrotic diseases.