Molecular cloning, expression and tissue distribution of glial-cell-line-derived neurotrophic factor family receptor alpha-3 (GFRalpha-3)

Autor: Miroslav Cik, Menelas N. Pangalos, Robert Gordon, Peter Verhasselt, Stefan Masure, Pascal Bonaventure, Josée E. Leysen, Anne Simone Josephine Lesage
Rok vydání: 1998
Předmět:
Receptor complex
Glial Cell Line-Derived Neurotrophic Factor Receptors
Glycosylation
Glycosylphosphatidylinositols
Recombinant Fusion Proteins
Neurturin
Molecular Sequence Data
Nerve Tissue Proteins
Receptors
Cell Surface
Receptors
Nerve Growth Factor
Tropomyosin receptor kinase B
Kidney
Transfection
Polymerase Chain Reaction
Biochemistry
Tropomyosin receptor kinase C
Cell Line
Glial cell line-derived neurotrophic factor
Animals
Humans
Amino Acid Sequence
Glial Cell Line-Derived Neurotrophic Factor
Nerve Growth Factors
Cloning
Molecular
In Situ Hybridization
Insulin-like growth factor 1 receptor
Membrane Glycoproteins
Sequence Homology
Amino Acid
biology
Insulin-like growth factor 2 receptor
Brain
Chromosome Mapping
Molecular biology
Rats
Organ Specificity
biology.protein
Chromosomes
Human
Pair 5
Peptides
Oligopeptides
Sequence Alignment
GDNF family of ligands
Zdroj: European Journal of Biochemistry. 251:622-630
ISSN: 1432-1033
0014-2956
DOI: 10.1046/j.1432-1327.1998.2510622.x
Popis: Neurturin and glial-cell-line-derived neurotrophic factor (GDNF) promote the survival and maintenance of different types of neuronal cells and signal through a receptor complex composed of a ligand binding subunit, either GDNF family receptor alpha-1 (GFRalpha-1) or alpha-2 (GFRalpha-2), together with the cRET membrane-bound protein tyrosine kinase. We have cloned GFRalpha-3, a novel receptor belonging to the GFRalpha family, that is 35% identical by amino acid sequence to both GFRalpha-1 and GFRalpha-2. GFRalpha-3 is a protein composed of 400 amino acid residues with three potential N-linked glycosylation sites together with the features characteristic of a glycosyl-phosphatidylinositol-anchored membrane protein. The heterologous expression of a FLAG-tagged GFRalpha-3 in human embryonic kidney cells showed that the protein is bound to the cell surface via a glycosyl-PtdIns anchor and is glycosylated, with different glycoforms migrating on SDS/PAGE with apparent molecular masses ranging over 43-62 kDa. The gene for GFRalpha-3 was mapped to human chromosome 5 in a region (q31.1-q31.3) where several disease loci, growth factor and growth factor receptor genes have been localized. Using northern blot analysis or reverse-transcription PCR, GFRalpha-3 was shown to be expressed within the nervous system predominantly in the cerebellum and the spinal cord while in peripheral tissues GFRalpha-3 was found to be expressed mostly in the colon, small intestine, pancreas, heart, testis and prostate. Using a GFRalpha-3-specific [35S]cRNA[gammaS] probe, in situ hybridization histochemistry experiments confirmed the expression in the cerebellum.
Databáze: OpenAIRE
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