A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form.
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A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form. / Hampe, Wolfgang; Urny, J; Franke, I; Hoffmeister-Ullerich, S A; Herrmann, D; Petersen, C M; Lohmann, J; Schaller, H C.
In: DEVELOPMENT, Vol. 126, No. 18, 18, 1999, p. 4077-4086.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form.
AU - Hampe, Wolfgang
AU - Urny, J
AU - Franke, I
AU - Hoffmeister-Ullerich, S A
AU - Herrmann, D
AU - Petersen, C M
AU - Lohmann, J
AU - Schaller, H C
PY - 1999
Y1 - 1999
N2 - 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.
AB - 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.
M3 - SCORING: Zeitschriftenaufsatz
VL - 126
SP - 4077
EP - 4086
JO - DEVELOPMENT
JF - DEVELOPMENT
SN - 0950-1991
IS - 18
M1 - 18
ER -