0000000000778538

AUTHOR

Heike Schäcke

showing 3 related works from this author

Molecular cloning of a tyrosine kinase gene from the marine spongeGeodia cydonium: a new member belonging to the receptor tyrosine kinase class II fa…

1994

We have isolated and characterized a cDNA from the marine sponge Geodia cydonium coding for a new member of the tyrosine protein kinase (TK) family. The cDNA encodes a protein of M(r) = 68,710, termed GCTK, which is homologous to class II receptor tyrosine kinases (RTKs). GCTK contains conserved amino acids (aa) characteristic of all protein kinases, and the sequences DLATRN and PIRWMATE which are highly specific for TKs. Furthermore, the sequence N-L-Y-x(3)-Y-Y-R is highly homologous to the sequence D-[LIV]-Y-x(3)-Y-Y-R found only in class II RTKs. The sponge TK, when compared with mammalian class II RTKs, shows maximum 31% homology in the TK domain indicating that this the oldest member o…

DNA ComplementaryMolecular Sequence DataReceptor tyrosine kinaseSH3 domainCytosolAnimalsGeodiaAmino Acid SequenceRNA MessengerCloning MolecularKinase activityTyrosineProtein kinase AMolecular BiologyBase SequenceSequence Homology Amino AcidbiologyCell MembraneReceptor Protein-Tyrosine KinasesCell BiologyProtein-Tyrosine Kinasesbiology.organism_classificationBiological EvolutionMolecular biologyPoriferaMolecular WeightBiochemistryROR1biology.proteinTyrosine kinaseMolecular Membrane Biology
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Immunoglobulin-like domain is present in the extracellular part of the receptor tyrosine kinase from the marine sponge Geodia cydonium.

1994

We have isolated and characterized two cDNAs from the marine sponge Geodia cydonium coding for a new member of a receptor tyrosine kinase of class II. The deduced amino acid sequence shows two characteristic domains: (i) the tyrosine kinase domain; and (ii) and immunoglobulin-like domain. The latter part shows high homology to the vertebrate C2 type immunoglobulin domain. This result demonstrates that immunoglobulin domains are not recent achievements of higher animals but exist also in those animals which have diverged from other organisms about 800 million years ago.

DNA ComplementarybiologySequence Homology Amino AcidMolecular Sequence DatamyrImmunoglobulinsReceptor Protein-Tyrosine KinasesImmunoglobulin domainSH2 domainBiological EvolutionReceptor tyrosine kinasePoriferaProtein Structure TertiaryBiochemistryStructural BiologyPhylogeneticsMultigene FamilyROR1biology.proteinAnimalsAmino Acid SequenceMolecular BiologyPeptide sequenceTyrosine kinaseSequence AlignmentJournal of molecular recognition : JMR
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Polymorphism in the immunoglobulin-like domains of the receptor tyrosine kinase from the sponge Geodia cydonium.

1996

Sponges [Porifera] are the phylogenetically oldest phylum of the Metazoa. They are provided with both cellular and humoral allorecognition systems. The underlying molecules are not yet known. To study allorecognition in sponges we first determined the frequency of graft rejection in a natural population of the marine sponge Geodia cydonium. We then determined, for the first time at the molecular level, the degree of sequence polymorphism in segments of one molecule which may be related to sponge allorecognition and host defense: the Ig-like domains from the receptor tyrosine kinase [RTK]. Thirty six pairs of auto- and allografts were assayed, either by parabiotic attachment or insertion of …

Graft RejectionDNA ComplementaryGeodia cydoniumMolecular Sequence DataImmunoglobulinsPolymerase Chain ReactionReceptor tyrosine kinaseMolecular levelSequence Homology Nucleic AcidAnimalsGeodiaAmino Acid SequenceAllorecognitionGene LibraryPolymorphism GeneticGraft rejectionbiologyBase SequenceSequence Homology Amino AcidReceptor Protein-Tyrosine KinasesGeneral MedicineAnatomySequence Analysis DNAbiology.organism_classificationCell biologyPoriferaSpongesurgical procedures operativebiology.proteinAntibodyCell adhesion and communication
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