کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10913874 | 1088643 | 2010 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Heparin-derived heparan sulfate mimics to modulate heparan sulfate-protein interaction in inflammation and cancer
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کلمات کلیدی
FGFRP-selectin glycoprotein ligand 1FGF1Heparan sulfatesGlcAPSGL-1HSPGHGFIL-8ECMFGF2GAGGlcNAcN-acetyl glucosamine - N-استیل گلوکوزامینantithrombin III - آنتی ترومبین IIIGlucuronic acid - اسید گلوکورونیکinflammation - التهاب( توروم) Interleukin-8 - اینترلوکین -8Cancer - سرطانCytokines - سیتوکین هاHepatocyte growth factor - عامل رشد هپاتوسیتGrowth factor - فاکتور رشدVascular endothelial growth factor - فاکتور رشد اندوتلیال عروقیVascular Endothelial Growth Factor (VEGF) - فاکتور رشد اندوتلیال عروقی (VEGF)Fibroblast growth factor-1 - فیبروبلاست رشد فاکتور -1fibroblast growth factor-2 - فیبروبلاست رشد فاکتور 2Extracellular matrix - ماتریکس خارج سلولیHeparan sulfate - هپاران سولفاتHeparins - هپارینHeparan sulfate proteoglycan - هپارین سولفات پروتئگلیکانHeparin-binding proteins - پروتئین های اتصال دهنده هپارینChemokines - کرموین هاGlycosaminoglycan - گلیکوزآمینوگلیکانfibroblast growth factor receptor - گیرنده فاکتور رشد فیبروبلاست
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
تحقیقات سرطان
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Heparin-derived heparan sulfate mimics to modulate heparan sulfate-protein interaction in inflammation and cancer Heparin-derived heparan sulfate mimics to modulate heparan sulfate-protein interaction in inflammation and cancer](/preview/png/10913874.png)
چکیده انگلیسی
The heparan sulfate (HS) chains of heparan sulfate proteoglycans (HSPG) are “ubiquitous” components of the cell surface and the extracellular matrix (EC) and play important roles in the physiopathology of developmental and homeostatic processes. Most biological properties of HS are mediated by interactions with “heparin-binding proteins” and can be modulated by exogenous heparin species (unmodified heparin, low molecular weight heparins, shorter heparin oligosaccharides and various non-anticoagulant derivatives of different sizes). Heparin species can promote or inhibit HS activities to different extents depending, among other factors, on how closely their structure mimics the biologically active HS sequences. Heparin shares structural similarities with HS, but is richer in “fully sulfated” sequences (S domains) that are usually the strongest binders to heparin/HS-binding proteins. On the other hand, HS is usually richer in less sulfated, N-acetylated sequences (NA domains). Some of the functions of HS chains, such as that of activating proteins by favoring their dimerization, often require short S sequences separated by rather long NA sequences. The biological activities of these species cannot be simulated by heparin, unless this polysaccharide is appropriately chemically/enzymatically modified or biotechnologically engineered. This mini review covers some information and concepts concerning the interactions of HS chains with heparin-binding proteins and some of the approaches for modulating HS interactions relevant to inflammation and cancer. This is approached through a few illustrative examples, including the interaction of HS and heparin-derived species with the chemokine IL-8, the growth factors FGF1 and FGF2, and the modulation of the activity of the enzyme heparanase by these species. Progresses in sequencing HS chains and reproducing them either by chemical synthesis or semi-synthesis, and in the elucidation of the 3D structure of oligosaccharide-protein complexes, are paving the way for rational approaches to the development of HS-inspired drugs in the field of inflammation and cancer, as well in other therapeutic fields.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Matrix Biology - Volume 29, Issue 6, July 2010, Pages 442-452
Journal: Matrix Biology - Volume 29, Issue 6, July 2010, Pages 442-452
نویسندگان
Benito Casu, Annamaria Naggi, Giangiacomo Torri,