کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8325228 | 1539932 | 2011 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The matrilins: Modulators of extracellular matrix assembly
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کلمات کلیدی
COMPp.c.DTDSTPseudoachondroplasiaPSACHvon Willebrand factor AVWAEGFhpfiNOSCOX-2Osteoarthritis - استئوآرتریت(آرتروز)MED - باpost coitum - بعد از جفت گیریMultiple epiphyseal dysplasia - دیسپلازی epiphyseal چندگانهhours post fertilization - ساعت پس از لقاحinducible nitric oxide synthase - سنتاز اکسید نیتریک القاییCyclooxygenase-2 - سیکلوکوکسیژناز2epidermal growth factor - عامل رشد اپیدرمیCartilage - غضروف یا کارتیلاژ Matrilin - ماتریلینCartilage oligomeric matrix protein - پروتئین ماتریکس oligomeric غضروفیCollagen - کلاژنchondrodysplasia - کندرویدا پلاسسیا
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The matrilins form a family of oligomeric extracellular adaptor proteins that are most strongly expressed in cartilage but also present in many other extracellular matrices. Matrilins bind to different types of collagen fibrils, to other noncollagenous proteins and to aggrecan. They thereby support matrix assembly by connecting fibrillar components and mediating interactions between these and the aggrecan gel. The binding avidity of a matrilin can be varied by alternative splicing, proteolytic processing and formation of homo- and heterooligomers. Such changes in matrilin structure may lead to a modulation of extracellular matrix assembly. Some matrilins bind weakly to α1β1 integrin and cell surface proteoglycans, but even though matrilins play a role in mechanotransduction and matrilin-3 activates the expression of osteoarthritis-associated genes the physiological relevance of matrilin-cell interactions is unclear. Matrilin knockout mice do not display pronounced phenotypes, which points to a redundancy within the protein family or with functionally related proteins. In man, dominant mutations in the von Willebrand factor A like domain of matrilin-3 lead to a protein retention in the endoplasmic reticulum that causes multiple epiphyseal dysplasia by initiating a cell stress response. In contrast, a mutation in an EGF domain of matrilin-3 that is associated with hand osteoarthritis and disc degeneration does not interfere with secretion but instead with extracellular assembly of matrix structures. In this review we summarize such information on matrilin structure and function that we believe is important for the understanding of extracellular matrix assembly and for deciphering pathophysiological mechanisms in diseases causing skeletal malformations or cartilage degeneration.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 43, Issue 3, March 2011, Pages 320-330
Journal: The International Journal of Biochemistry & Cell Biology - Volume 43, Issue 3, March 2011, Pages 320-330
نویسندگان
Andreas R. Klatt, Ann-Kathrin A. Becker, Cristian D. Neacsu, Mats Paulsson, Raimund Wagener,