Domain 36 of Tropoelastin in Elastic Fiber Formation
Autor: | Hiroshi Wachi, Fumiaki Sato, Risa Nonaka |
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Rok vydání: | 2014 |
Předmět: |
Mutant
Pharmaceutical Science Elastic fiber assembly Fibrillins Contractile Proteins Tropoelastin medicine Animals Protein Interaction Domains and Motifs Cells Cultured Pharmacology chemistry.chemical_classification Extracellular Matrix Proteins integumentary system biology Chemistry Microfilament Proteins General Medicine medicine.anatomical_structure Microfibrils biology.protein Biophysics Cattle RNA Splicing Factors Microfibril Glycoprotein Elastin Elastic fiber Protein Binding Cysteine |
Zdroj: | Biological and Pharmaceutical Bulletin. 37:698-702 |
ISSN: | 1347-5215 0918-6158 |
DOI: | 10.1248/bpb.b13-00933 |
Popis: | Elastic fiber assembly is a complex stepwise process involving multiple different proteins and enzymes. Domain 36, encoded by the last exon of the elastin gene, is recognized to be an important domain for deposition onto microfibrils, an essential step in elastic fiber assembly. However, the role of domain 36 in elastic fiber assembly has not been clarified. Here, we utilized our established in vitro assembly model to identify the importance of domain 36 for the assembly process. Our results showed that the lack of domain 36 in bovine tropoelastin results in deficient elastic fiber assembly. A similar result was obtained with the point mutation of two cysteine residues and the deletion of the Lysine-Arginine-Lysine-Arginine (RKRK) sequence in domain 36. Double immunofluorescence of tropoelastin and fibrillin-1, a main component of microfibrils, demonstrated reduced localization of these mutant tropoelastin molecules on fibrillin-1 fibers. Moreover, the binding affinity of these mutants to fibrillin-1 and microfibril-associated glycoprotein (MAGP) was significantly decreased. These data indicate that domain 36 of tropoelastin facilitates elastic fiber assembly by interacting with microfibrils via two cysteine residues and the RKRK sequence. |
Databáze: | OpenAIRE |
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