کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8455263 | 1548014 | 2015 | 19 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Hyaluronan Controls the Deposition of Fibronectin and Collagen and Modulates TGF-β1 Induction of Lung Myofibroblasts
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کلمات کلیدی
ECMDAPIHAS2αSMAEDAextra domain AFBS4-Methyl umbelliferoneTGF-β1DMEM4-MUPBS4′,6-diamidino-2-phenylindole - 4 '، 6-دیامیدینو-2-فنیلینولDMSO - DMSODulbecco's modified Eagle Medium - Eagle Medium اصلاح شده Dulbeccoalpha smooth muscle actin - آلفا آکتیو عضله صافTransforming growth factor-beta 1 - تبدیل فاکتور رشد بتا 1Dimethylsulfoxide - دیمتیل سولفواکسیدfetal bovine serum - سرم جنین گاوPhosphate buffered saline - فسفات بافر شورHuman lung fibroblasts - فیبروبلاست های انسانی ریهFibronectin - فیبرونکتینExtracellular matrix - ماتریکس خارج سلولیMyofibroblast - میوفیبروبلاستHyaluronan - هیالورونانhyaluronan synthase 2 - هیالورونان سنتاز 2Collagen - کلاژن
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
تحقیقات سرطان
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Hyaluronan Controls the Deposition of Fibronectin and Collagen and Modulates TGF-β1 Induction of Lung Myofibroblasts Hyaluronan Controls the Deposition of Fibronectin and Collagen and Modulates TGF-β1 Induction of Lung Myofibroblasts](/preview/png/8455263.png)
چکیده انگلیسی
The contribution of hyaluronan-dependent pericellular matrix to TGF-β1-driven induction and maintenance of myofibroblasts is not understood. Hyaluronan is an extracellular matrix (ECM) glycosaminoglycan important in cell adhesion, proliferation and migration, and is implicated in myofibroblast formation and maintenance. Reduced turnover of hyaluronan has been linked to differentiation of myofibroblasts and potentiation of lung fibrosis. Fibronectin is a fibril forming adhesive glycoprotein that is also upregulated following induction with TGF-β1. Although they are known to bind each other, the interplay between hyaluronan and fibronectin in the pericellular matrix during myofibroblast induction and matrix assembly is not clear. This study addresses the role of hyaluronan and its interaction with fibrillar matrix components during myofibroblast formation. Hyaluronan and fibronectin were increased and co-localized in the ECM following myofibroblast induction by TGF-β1. Inhibition of hyaluronan synthesis in TGF-β1-induced lung myofibroblasts over a 4 day period with 4-methyl umbelliferone (4-MU) further enhanced myofibroblast morphology, caused increased deposition of fibronectin and type I collagen in the ECM, and increased expression of alpha-smooth muscle actin and hyaluronan synthase 2 (HAS2) mRNA. Hyaluronan oligosaccharides or hyaluronidase treatment, which more effectively disrupted the pericellular matrix, had similar effects. CD44 and β1 integrins co-localized in the cell membrane and along some stress fibers. However, CD44 and hyaluronan were specifically excluded from focal adhesions, and associated primarily with cortical actin. Time-lapse imaging of the immediate effects of hyaluronidase digestion showed that hyaluronan matrix primarily mediates attachment of membrane and cortical actin between focal contacts, suggesting that surface adhesion through hyaluronan and CD44 is distinct from focal adhesion through β1 integrins and fibronectin. Fluorescein-labeled hyaluronan bound regularly along fibronectin fibers and co-localized more with β1 integrin and less with CD44. Therefore, the hyaluronan matrix can interfere with the assembly of fibrillar ECM components, and this interplay regulates the degree of myofibroblast formation. These data also suggest that adhesion through hyaluronan matrix impacts cytoskeletal organization, and is potentially part of a clutch mechanism that regulates stick and slip of myofibroblasts by affecting the adhesion to and organization of fibronectin and collagen.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Matrix Biology - Volume 42, March 2015, Pages 74-92
Journal: Matrix Biology - Volume 42, March 2015, Pages 74-92
نویسندگان
Stephen P. Evanko, Susan Potter-Perigo, Loreen J. Petty, Gail A. Workman, Thomas N. Wight,