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The role of calcium in the organization of fibrillin microfibrils
Author(s) -
Kielty Cay M.,
Shuttleworth C.Adrian
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80829-j
Subject(s) - fibrillin , microfibril , calcium , egta , microbiology and biotechnology , chemistry , fibroblast , biophysics , biology , biochemistry , in vitro , extracellular matrix , cellulose , organic chemistry
The microfibrillar glycoprotein fibrillin has a multidomain structure which contains forty‐three epidermal growth factor‐like motifs with calciumbinding consensus sequences. We have utilized intact microfibrils isolated from human dermal fibroblast cultures to investigate the putative influence of bound calcium on microfibrillar organization and integrity. Incubation with EDTA or EGTA rapidly resulted in gross disruption of microfibril morphology. The treatment induced disorganization of the interbead domains although the regular beaded arrangement was always apparent. These changes were readily reversible on replacing calcium, indicating that the treatment had not compromised microfibrillar integrity. The data localize calcium binding EGF‐like repeats to the interbead domains and indicate that lateral packing of fibrillin monomers is calcium‐dependent. This arrangement suggests how mutations in epidermal growth factor‐like domains of fibrillin might cause the disruption in microfibril organization and interactions which underlies the clinical symptoms of some Marian syndrome patients.