Proteoglycans and dental biology: the first review

Listik, Eduardo; Gaschler, Juliana Azevedo Marques; Matias, Murilo; Feres, Murilo Fernando Neuppmann; Toma, Leny; Nahás-Scocate, Ana Carla Raphaelli

doi:10.1016/j.carbpol.2019.115199

Cited by 20 publications

(15 citation statements)

References 158 publications

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“…The SLRP family, which participate in matrix structural organization as ubiquitous ECM components, comprise five classes (I-V) according to the numbers of exons, interspaced amino acid residues and LRR motifs 14 - 16 . Accumulating evidence suggests that the SLRP family are associated with a wide spectrum of biological processes 17 , such as embryogenesis 18 , regeneration 19 and tumor progression 20 .…”

Section: Discussionmentioning

confidence: 99%

PODNL1 promotes cell proliferation and migration in glioma via regulating Akt/mTOR pathway

Geng

Zuo

et al. 2020

J. Cancer

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Background and Aims: Emerging studies have determined that the small leucine-rich proteoglycan (SLRP) family can aggravate tumor progression. However, the biological function of podocan-like protein 1 (PODNL1), a novel member of the SLRP family, has not been investigated. Therefore, our study focused on the function and regulatory mechanism of PODNL1 in glioma. Methods: Both the Gene Expression Profiling Interactive Analysis (GEPIA) and the Chinese Glioma Genome Atlas (CGGA) database were used to analyze the expression level and survival risk of PODNL1 in glioma. Quantitative real-time polymerase chain reaction (qRT-PCR) and Western blot were applied to detect the mRNA and protein expression, respectively. Celltiter-Glo and colony formation assays were used to evaluate cell proliferation. Migration capacity was measured by Transwell and wound healing assays. Flow cytometry was utilized to assess the apoptotic rate. Results: The expression of PODNL1 predicted the poor prognosis in glioma patients. Silencing of PODNL1 inhibited cell proliferation, migration, and induced epithelial-like phenotype. In addition, knockdown of PODNL1 also induced cell apoptosis. Moreover, the cell growth and migration inhibited by PODNL1 knockdown could be partially rescued with Akt activator. Conversely, PODNL1 overexpression promoted cell growth and migration, which were suppressed by Akt inhibitor. Conclusions: PODNL1, a promising predictive indicator of poor prognosis, resulted in greater proliferation, migration and epithelial-mesenchymal transition (EMT) process. Moreover, PODNL1 promoted aggressive glioma behavior by activating Akt/mTOR pathway, providing a novel therapeutic target for glioma.

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Section: Discussionmentioning

confidence: 99%

PODNL1 promotes cell proliferation and migration in glioma via regulating Akt/mTOR pathway

Geng

Zuo

et al. 2020

J. Cancer

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“…Additionally, GAGs are often modified by sulfate groups, except for the single nonsulfated GAG: hyaluronic acid, which is not involved in PG formation. 17 According to sulfation locations, such GAGs as chondroitin sulfate (CS) can be subdivided further (Figure 2), and these different sulfation patterns can enrich the functional diversity of PGs. 18 As for the linkage region, heparin, heparan sulfate (HS), chondroitin sulfate (CS), and dermatan sulfate (DS) are O-linked to a serine residue in the core protein by tetrasaccharide (Figure 1).…”

Section: Structure Of Pgsmentioning

confidence: 99%

Proteoglycans in the periodontium: A review with emphasis on specific distributions, functions, and potential applications

Chen

Guan

Han

et al. 2021

J of Periodontal Research

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Proteoglycans (PGs) are typically macromolecules that are composed of a linkage sugar, core proteins, and glycosaminoglycans (GAGs) (Figure 1). 1 As PGs are ubiquitously distributed intracellularly, pericellularly, extracellularly or on the cell surfaces, they can have profound effects on numerous physiological and pathological processes such as tissue development, wound repair, metabolic dysfunction, and carcinogenesis. [2][3][4][5] Thus, researchers are exploring new avenues for preventing or curing diseases by harnessing PGs. 6 Furthermore, several PGs have been reported to reside and function in teeth 7-9 and the periodontium. [10][11][12] The significance of the periodontium cannot be overemphasized because it is made up of the gingiva, periodontal ligament, alveolar bone, and cementum that stabilizes, supports, and protects teeth in alveolar sockets. 13 Once the periodontium is destroyed irreversibly, teeth will risk loss or extraction, further impairing chewing function, esthetics, and quality of life. 14 Considering the close associations of PGs with tissue biology, we aim to shed light on comprehensive interactions between PGs and the periodontium to pave the way for further research on

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“…Moreover, PGs can be glycosylated by more than one kind of GAG [ 22 , 23 ]. GAG chains can interact with a wide variety of signaling macromolecules to regulate fundamental biological processes [ 20 ] and, thus, bestow PGs with a plethora of structural and functional variations [ 18 ].…”

Section: Proteoglycansmentioning

confidence: 99%

“…The PGs can be classified based on their location as intracellular (e.g., serglycin), at the cell membrane (e.g., betaglycan), pericellular (e.g., perlecan), and away from the cell or “extracellular” (e.g., biglycan). The small leucine-rich proteoglycans (SLRPs) are a prominent component of extracellular PGs, comprising the largest class of PGs [ 22 ]. Serglycin is the only intracellular PG, initially identified in granules of mast cells, where it stabilizes proteases that are released upon inflammation [ 25 ].…”

Section: Proteoglycansmentioning

confidence: 99%

Proteoglycans in the Pathogenesis of Hormone-Dependent Cancers: Mediators and Effectors

Tzanakakis

Giatagana

Kuskov

et al. 2020

Cancers

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Hormone-dependent cancers exhibit high morbidity and mortality. In spite of advances in therapy, the treatment of hormone-dependent cancers remains an unmet health need. The tumor microenvironment (TME) exhibits unique characteristics that differ among various tumor types. It is composed of cancerous, non-cancerous, stromal, and immune cells that are surrounded and supported by components of the extracellular matrix (ECM). Therefore, the interactions among cancer cells, stromal cells, and components of the ECM determine cancer progression and response to therapy. Proteoglycans (PGs), hybrid molecules consisting of a protein core to which sulfated glycosaminoglycan chains are bound, are significant components of the ECM that are implicated in all phases of tumorigenesis. These molecules, secreted by both the stroma and cancer cells, are crucial signaling mediators that modulate the vital cellular pathways implicated in gene expression, phenotypic versatility, and response to therapy in specific tumor types. A plethora of deregulated signaling pathways contributes to the growth, dissemination, and angiogenesis of hormone-dependent cancers. Specific inputs from the endocrine and immune systems are some of the characteristics of hormone-dependent cancer pathogenesis. Importantly, the mechanisms involved in various aspects of cancer progression are executed in the ECM niche of the TME, and the PG components crucially mediate these processes. Here, we comprehensively discuss the mechanisms through which PGs affect the multifaceted aspects of hormone-dependent cancer development and progression, including cancer metastasis, angiogenesis, immunobiology, autophagy, and response to therapy.

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Proteoglycans and dental biology: the first review

Cited by 20 publications

References 158 publications

PODNL1 promotes cell proliferation and migration in glioma via regulating Akt/mTOR pathway

PODNL1 promotes cell proliferation and migration in glioma via regulating Akt/mTOR pathway

Proteoglycans in the periodontium: A review with emphasis on specific distributions, functions, and potential applications

Proteoglycans in the Pathogenesis of Hormone-Dependent Cancers: Mediators and Effectors

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