Heparan sulfate and cell division

Porcionatto, Marimélia; Nader, Helena B.; Dietrich, Carl P.

doi:10.1590/s0100-879x1999000500006

Cited by 18 publications

(11 citation statements)

References 31 publications

(24 reference statements)

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“…Many reports have suggested that heparan sulfate proteoglycans play a role in growth control, cell spreading, cellular recognition, cellular adhesion, and signaling, possibly as co-receptors with integrins and cell-cell adhesion molecules, including fibronectin, vi-tronectin, laminins, and the fibrillar collagens (1)(2)(3)(8)(9)(10)(11)(12). In addition, several papers have described high affinity association of heparin-like molecules with growth factors, implying that the effects of heparan sulfate on cell growth are likely to be mediated by growth factors (13)(14)(15)(16)(17)(18). This review focuses on the possible roles of syndecan core proteins and heparan sulfate chains in cell signaling.…”

Section: Introductionmentioning

confidence: 99%

<a name="home"></a>Specific structural features of syndecans and heparan sulfate chains are needed for cell signaling

Lopes

Dietrich

Nader

2006

Braz J Med Biol Res

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The syndecans, heparan sulfate proteoglycans, are abundant molecules associated with the cell surface and extracellular matrix and consist of a protein core to which heparan sulfate chains are covalently attached. Each of the syndecan core proteins has a short cytoplasmic domain that binds cytosolic regulatory factors. The syndecans also contain highly conserved transmembrane domains and extracellular domains for which important activities are becoming known. These protein domains locate the syndecan on cell surface sites during development and tumor formation where they interact with other receptors to regulate signaling and cytoskeletal organization. The functions of cell surface heparan sulfate proteoglycan have been centered on the role of heparan sulfate chains, located on the outer side of the cell surface, in the binding of a wide array of ligands, including extracellular matrix proteins and soluble growth factors. More recently, the core proteins of the syndecan family transmembrane proteoglycans have also been shown to be involved in cell signaling through interaction with integrins and tyrosine kinase receptors.

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Section: Introductionmentioning

confidence: 99%

<a name="home"></a>Specific structural features of syndecans and heparan sulfate chains are needed for cell signaling

Lopes

Dietrich

Nader

2006

Braz J Med Biol Res

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“…[22][23][24][25][26][27][28] Therefore, the increased heparanase mRNA expression observed might be related to the decrease of HS and RCC development.…”

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confidence: 99%

Heparanase expression and glycosaminoglycans profile in renal cell carcinoma

Batista¹,

Matos

Machado³

et al. 2012

Int J of Urology

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Abbreviations & Acronyms CS = chondroitin sulfate DS = dermatan sulfate ECM = extracellular matrix GAG = glycosaminoglycan GAPDH = glyceraldehydes-3-phosphate dehydrogenase HA = hyaluronic acid HS = heparan sulfate mRNA = messenger ribonucleic acid RCC = renal cell carcinoma RNA = ribonucleic acid Abstract: A better understanding of the molecular mechanisms of renal cell carcinogenesis could contribute to a decrease in the mortality rate of this disease. The aim of this study was to evaluate the glycosaminoglycans profile and heparanase expression in renal cell carcinoma. The study included 24 patients submitted to nephrectomy with confirmed pathological diagnosis of renal cell carcinoma. The majority of the samples (87.5%) were classified in the initial stage of renal cell carcinoma (clinical stages I and II). Heparanase messenger ribonucleic acid expression was evaluated by quantitative realtime reverse transcription polymerase chain reaction, and sulfated glycosaminoglycans were identified and quantified by agarose gel electrophoresis of renal cell carcinoma samples or non-neoplastic tissues obtained from the same patients (control group). The sulfated glycosaminoglycans and hyaluronic acid were analyzed in urine samples of the patients before and after surgery. The data showed a significant statistical increase in chondroitin sulfate, and a decrease in heparan sulfate and dermatan sulfate present in neoplastic tissues compared with non-neoplastic tissues. Higher heparanase messenger ribonucleic acid expression in the neoplastic tissues was also shown, compared with the non-neoplastic tissues. The urine glycosaminoglycans profile showed no significant difference between renal cell carcinoma and control samples. Extracellular matrix changes observed in the present study clarify that heparanase is possibly involved with heparan sulfate turnover, and that heparanase and the glycosaminoglycans can modulate initial events of renal cell carcinoma development.

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“…They have been involved in several biological effects (1,(3)(4)(5), such as extracellular matrix (ECM) assembly (6) and cell surface-ECM receptors for growth factors and hormones (2,5,7) or have had a role in biological processes such as cell-cell recognition (8) and control of cell growth (9). The fact that several ECM proteins, such as fibronectin (10), laminin (11), thrombospondin (12), vitronectin (13), type IV collagen (14), and tenascin (15), have GAG binding sites adds credence to the postulated multiple roles of proteoglycans.…”

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confidence: 99%