Home | EMILIN- 3, a peculiar member of the EMILIN/Multimerin protein family, has a distinct expression pattern, forms oligomeric assemblies and serves as a pro TGF-
EMILIN- 3, a peculiar member of the EMILIN/Multimerin protein family, has a distinct expression pattern, forms oligomeric assemblies and serves as a pro TGF-
B2 WAGENER/ PAULSSONSchiavinato, A., Becker, A.K., Zanetti, M., Corallo, D., Milanetto, M., Bizzotto, D., Bressan, G.,
Guljelmovic, M., Paulsson, M., Wagener, R., Braghetta, P. and Bonaldo, P., J Biol Chem. 2012 Mar 30;287(14):11498-515. doi: 10.1074/jbc.M111.303578. Epub 2012 Feb 10.
EMILIN-3 is a glycoprotein of the extracellular matrix belonging to a family that contains a characteristic N-terminal cysteine-rich EMI domain. Currently, EMILIN-3 is the least characterized member of the elastin microfibril interface-located protein (EMILIN)/Multimerin family. Using RNA, immunohistochemical, and protein chemistry approaches, we carried out a detailed characterization of the expression and biochemical properties of EMILIN-3 in mouse. During embryonic and postnatal development, EMILIN-3 showed a peculiar and dynamic pattern of gene expression and protein distribution. EMILIN-3 mRNA was first detected at E8.5-E9.5 in the tail bud and in the primitive gut, and at later stages it became abundant in the developing gonads and osteogenic mesenchyme. Interestingly and in contrast to other EMILIN/Multimerin genes, EMILIN-3 was not found in the cardiovascular system. Despite the absence of the globular C1q domain, immunoprecipitation and Western blot analyses demonstrated that EMILIN-3 forms disulfide-bonded homotrimers and higher order oligomers. Circular dichroism spectroscopy indicated that the most C-terminal part of EMILIN-3 has a substantial α-helical content and forms coiled coil structures involved in EMILIN-3 homo-oligomerization. Transfection experiments with recombinant constructs showed that the EMI domain contributes to the higher order self-assembly but was dispensable for homotrimer formation. EMILIN-3 was found to bind heparin with high affinity, a property mediated by the EMI domain, thus revealing a new function for this domain that may contribute to the interaction of EMILIN-3 with other extracellular matrix and/or cell surface molecules. Finally, in vitro experiments showed that EMILIN-3 is able to function as an extracellular regulator of the activity of TGF-β ligands.
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