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Fig. 4 Chl and CHL1 are substrates for BMP1/Tolloid-like proteinases. (A) A Coomassie-stained SDS–PAGE gel is shown of protein molecular weight markers (lane 1) and of ∼ 55-kDa secreted and purified Chl (lane 2). (B–D) Immunoblotting with anti-FLAG antibody (B and D) or anti-CHL1 antibody (C) is shown for in vitro assays in which recombinant Chl was incubated in the absence (-) or presence (+) of Bmp1a (B) or in which recombinant short, neuralin form of CHL1 (C) or CHL2 (D) was incubated in the absence (o/n) or presence of mammalian BMP1, mTLD, mTLL1, or mTLL2. Positions of the ∼ 30-kDa Chl (B) and ∼ 20-kDa and smaller CHL1 (C) cleavage products are shown. In B and D, asterisks mark the positions of FLAG-tagged BMP1 and related proteinases. Molecular masses (in kDa) are indicated for protein standards.
Reprinted from Developmental Biology, 341(2), Branam, A.M., Hoffman, G.G., Pelegri, F., and Greenspan, D.S., Zebrafish Chordin-like and Chordin Are Functionally Redundant in Regulating Patterning of the Dorsoventral Axis, 444-458, Copyright (2010) with permission from Elsevier. Full text @ Dev. Biol.