Claus Munck Petersen

A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • W Hampe
  • ,
  • J Urny
  • ,
  • I Franke
  • ,
  • S A Hoffmeister-Ullerich
  • ,
  • D Herrmann, Denmark
  • C M Petersen
  • Jesper Lohmann
  • ,
  • H C Schaller
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.
Original languageEnglish
Pages (from-to)4077-86
Number of pages10
Publication statusPublished - 1999

    Research areas

  • Amino Acid Sequence, Animals, Cloning, Molecular, Ectoderm, Embryo, Nonmammalian, Gene Expression Regulation, Developmental, Hydra, In Situ Hybridization, Membrane Proteins, Molecular Sequence Data, Mutation, Neuropeptides, Pyrrolidonecarboxylic Acid, Receptors, Peptide, Regeneration, Sequence Homology, Amino Acid, Solubility

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