Homotypic fibrillin-1 interactions in microfibril assembly

Marson, A.; Rock, M.J.; Cain, S.A.; Freeman, L.J.; Morgan, A.; Mellody, K.; Shuttleworth, C.A.; Baldock, C.; Kielty, C.M.

Journal of Biological Chemistry 280(6): 5013-5021

2005


ISSN/ISBN: 0021-9258
PMID: 15569675
DOI: 10.1074/jbc.m409029200
Accession: 013136356

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Abstract
We have defined the homotypic interactions of fibrillin-1 to obtain new insights into microfibril assembly. Dose-dependent saturable high affinity binding was demonstrated between N-terminal fragments, between furin processed C-terminal fragments, and between these N- and C-terminal fragments. The N terminus also interacted with a downstream fragment. A post-furin cleavage site C-terminal sequence also interacted with the N terminus, with itself and with the furin-processed fragment. No other homotypic fibrillin-1 interactions were detected. Some terminal homotypic interactions were inhibited by other terminal sequences, and were strongly calcium-dependent. Treatment of an N-terminal fragment with N-ethylmaleimide reduced homotypic binding. Microfibril-associated glycoprotein-1 inhibited N- to C-terminal interactions but not homotypic N-terminal interactions. These fibrillin-1 interactions are likely to regulate pericellular fibrillin-1 microfibril assembly.