The neuropeptide head activator plays an important role for proliferation and determination of stem cells in hydra. By affinity chromatography a 200 kDa head-activator binding protein, HAB, was isolated from the multiheaded mutant of Chlorohydra viridissima. Partial amino acid sequences were used to clone the HAB cDNA which coded for a receptor with a unique alignment of extracellular modules, a transmembrane domain, and a short carboxy-terminal cytoplasmic tail. A mammalian HAB homologue with identical alignment of these modules is expressed early in brain development. Specific antibodies revealed the presence of HAB in hydra as a transmembrane receptor, but also as secreted protein, both capable of binding head activator. Secretion of HAB during regeneration and expression in regions of high determination potential hint at a role for HAB in regulating the concentration and range of action of head activator.
A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form
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W. Hampe, J. Urny, I. Franke, S.A. Hoffmeister-Ullerich, D. Herrmann, C.M. Petersen, J. Lohmann, H.C. Schaller; A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form. Development 15 September 1999; 126 (18): 4077–4086. doi: https://doi.org/10.1242/dev.126.18.4077
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