Processing and assembly of fibrillin-1
نویسندگان
چکیده
منابع مشابه
Fibrillin assembly requires fibronectin.
Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and nonelastic extracellular matrices. Proper assembly mechanisms are central to the formation and function of these microfibrils, and their properties are often compromised in pathological circumstances such as in Marfan syndrome and in other fibrillinopathies. Here, we have used human dermal fibroblasts to ana...
متن کاملFibrillin-1 microfibril deposition is dependent on fibronectin assembly.
Newly deposited microfibrils strongly colocalise with fibronectin in primary fibroblasts. Microfibril formation is grossly inhibited by fibronectin depletion, but rescued by supplementation with exogenous cellular fibronectin. As integrin receptors are key determinants of fibronectin assembly, we investigated whether they also influenced microfibril deposition. Analysis of beta1-integrin-recept...
متن کاملProcessing of the fibrillin-1 carboxyl-terminal domain.
To investigate the processing and general properties of the fibrillin-1 carboxyl-terminal domain, three protein expression constructs have been developed as follows: one without the domain, one with the domain, and one with a mutation near the putative proteolytic processing site. The constructs have been expressed in two eukaryotic model systems, baculoviral and CHO-K1. Post-translational modi...
متن کاملRegulation of fibrillin carboxy-terminal furin processing
Fibrillins are large cysteine-rich glycoproteins (~350 kDa) which form the molecular scaffold of a class of beaded microfibrils that are key structural elements of dynamic connective tissues (Kielty and Shuttleworth, 1995). These microfibrils are extensible polymers which act as a structural lattice for elastin deposition during elastic fibre formation (Mecham and Heusar, 1991). Linkage of the ...
متن کاملThe Tight Skin Mouse: Demonstration of Mutant Fibrillin-1 Production and Assembly into Abnormal Microfibrils
Mice carrying the Tight skin (Tsk) mutation harbor a genomic duplication within the fibrillin-1 (Fbn 1) gene that results in a larger than normal in-frame Fbn 1 transcript. In this study, the consequences of the Tsk mutation for fibrillin-containing microfibrils have been examined. Dermal fibroblasts from Tsk/+ mice synthesized and secreted both normal fibrillin (approximately 330 kD) and the m...
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ژورنال
عنوان ژورنال: International Journal of Experimental Pathology
سال: 2008
ISSN: 0959-9673
DOI: 10.1046/j.1365-2613.2000.0145z.x