| First Author | Saito S | Year | 1999 |
| Journal | Mol Immunol | Volume | 36 |
| Issue | 3 | Pages | 169-76 |
| PubMed ID | 10403482 | Mgi Jnum | J:55886 |
| Mgi Id | MGI:1339520 | Doi | 10.1016/s0161-5890(99)00035-8 |
| Citation | Saito S, et al. (1999) Characterization of mutated protein encoded by partially duplicated fibrillin-1 gene in tight skin (TSK) mice. Mol Immunol 36(3):169-76 |
| abstractText | Fibrillin-1 (Fbn-1) is a ubiquitous protein present in the extracellular matrix of various organs and it is a major component of microfibrils embedded in the core of elastic fibers. In humans, mutations or deletions of the Fbn-1 gene are associated with several genetic diseases. In addition, several microsatellite alleles near Fbn-1 gene were found associated with diffuse scleroderma. In TSK/+mice, which develop a scleroderma-like syndrome, the Fbn-1 gene exhibits an inframe duplication of exons 17-40. In this study, we report that the synthesis and secretion of wild-type Fbn-1 in TSK/+ is higher than that of the mutated Fbn-1 protein excluding the possibility that TSK genetic defect is due to a loss of the wild allele. We also demonstrate for the first time that TGF-beta, which plays a crucial role in skin fibrosis, binds to both wild- type and mutated Fbn-1. The amount of bound TGF-beta was higher in mutated than wild-type Fbn-1 and appears related to the number of TGF-beta binding motifs. (C) 1999 Elsevier Science Ltd. All rights reserved. |
