کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10913928 | 1088655 | 2009 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Progression of human bone marrow stromal cells into both osteogenic and adipogenic lineages is differentially regulated by structural conformation of collagen I matrix via distinct signaling pathways
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کلمات کلیدی
BSPAdult human stem cells17-AAG, 17-allylamino-17-demethoxygeldanamycinMGPLPLGLUT4MMPp38HspFABP4ERKRUNX2BMSCsTIMP - زمانbone marrow stromal cells - سلول های استرومایی مغز استخوانbone sialoprotein - سیلوپروتئین استخوانRunt-related transcription factor 2 - عامل رونویسی مرتبط با روت 2Lipoprotein lipase - لیپو پروتئین لیپازmatrix metalloproteinase - ماتریکس متالوپروتئینازTissue inhibitor of metalloproteinase - مهار کننده های متالوپروتئیناز بافتHeat shock protein - پروتئین شوک حرارتMatrix Gla protein - پروتئین ماتریکس Glap38 mitogen-activated protein kinase - پروتئین کیناز متیوژن فعال p38extracellular signal-regulated kinase - کیناز تنظیم شده سیگنال خارج سلولی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
تحقیقات سرطان
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Adult human bone marrow stromal cells (BMSCs) containing or consisting of mesenchymal stem cells (MSCs) are an important source in tissue homeostasis and repair. Although many processes involved in their differentiation into diverse lineages have been deciphered, substantial inroads remain to be gained to synthesize a complete regulatory picture. The present study suggests that structural conformation of extracellular collagen I, the major organic matrix component in musculoskeletal tissues, plays, along with differentiation stimuli, a decisive role in the selection of differentiation lineage. It introduces a novel concept which proposes that structural transition of collagen I matrix regulates cell differentiation through distinct signaling pathways specific for the structural state of the matrix. Thus, on native collagen I matrix inefficient adipogenesis is p38-independent, whereas on its denatured counterpart, an efficient adipogenesis is primarily regulated by p38 kinase. Inversely, osteogenic differentiation occurs efficiently on native, but not on denatured collagen I matrix, with a low commencement threshold on the former and a substantially higher one on the latter. Osteogenesis on collagen I matrices in both structural conformations is fully dependent on ERK. However, whereas on native collagen I matrix osteogenic differentiation is Hsp90-dependent, on denatured collagen I matrix it is Hsp90-independent. The matrix conformation-mediated regulation appears to be one of the mechanisms determining differentiation lineage of BMSCs. It allows a novel interpretation of the bone remodeling cycle, explains the marked physiological aging-related adipogenic shift in musculoskeletal tissues, and can be a principal contributor to adipogenic shift seen in a number of clinical disorders.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Matrix Biology - Volume 28, Issue 5, June 2009, Pages 239-250
Journal: Matrix Biology - Volume 28, Issue 5, June 2009, Pages 239-250
نویسندگان
Josh Mauney, Vladimir Volloch,