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Zebrafish nma is involved in TGFbeta family signaling.
Tsang M, Kim R, de Caestecker MP, Kudoh T, Roberts AB, Dawid IB
(2000) Genesis 28: 47-57
MeSH Terms: Activin Receptors, Type I, Amino Acid Sequence, Animals, Body Patterning, Bone Morphogenetic Proteins, Embryo, Nonmammalian, Female, Gene Expression Regulation, Developmental, In Situ Hybridization, Membrane Proteins, Microinjections, Molecular Sequence Data, Mutation, Protein-Serine-Threonine Kinases, RNA, Radiation Hybrid Mapping, Receptor, Transforming Growth Factor-beta Type I, Receptor, Transforming Growth Factor-beta Type II, Receptors, Transforming Growth Factor beta, Sequence Homology, Amino Acid, Signal Transduction, Xenopus, Xenopus Proteins, Zebrafish, Zebrafish Proteins
Show Abstract · Added January 5, 2011
Bone morphogenetic proteins (BMP) are members of the TGFbeta superfamily of secreted factors with important regulatory functions during embryogenesis. We have isolated the zebrafish gene, nma, that encodes a protein with high sequence similarity to human NMA and Xenopus Bambi. It is also similar to TGFbeta type I serine/theronine kinase receptors in the extracellular ligand-binding domain but lacks a cytoplasmic kinase domain. During development, nma expression is similar to that of bmp2b and bmp4, and analysis in the dorsalized and ventralized zebrafish mutants swirl and chordino indicates that nma is regulated by BMP signaling. Overexpression of nma during zebrafish and Xenopus development resulted in phenotypes that appear to be based on inhibition of BMP signaling. Biochemically, NMA can associate with TGFbeta type II receptors and bind to TGFbeta ligand. We propose that nma is a BMP-regulated gene whose function is to attenuate BMP signaling during development through interactions with type II receptors and ligands.
2 Communities
1 Members
0 Resources
25 MeSH Terms
Molecular cloning of a human, hemicholinium-3-sensitive choline transporter.
Apparsundaram S, Ferguson SM, George AL, Blakely RD
(2000) Biochem Biophys Res Commun 276: 862-7
MeSH Terms: Amino Acid Sequence, Animals, Binding Sites, Biological Transport, COS Cells, Carrier Proteins, Choline, Chromosomes, Human, Pair 2, Cloning, Molecular, Hemicholinium 3, Humans, Ligands, Membrane Transport Proteins, Molecular Sequence Data, Oocytes, Protein Binding, RNA, Messenger, Radiation Hybrid Mapping, Sequence Homology, Amino Acid, Transfection, Xenopus laevis
Show Abstract · Added July 10, 2013
Under many physiological circumstances, Na(+)- and Cl(-)-dependent, hemicholinium-3 (HC-3)-sensitive, high-affinity choline uptake (HACU) in cholinergic neurons is thought to be rate-limiting in the biosynthesis of acetylcholine (ACh). Based on sequence information provided by the Human Genome Project and the recently reported rat CHT1 (rCHT1), we cloned a human CHT cDNA from spinal cord. The hCHT cDNA encodes a protein of 580 amino acids having 93% identity to rCHT1 and 51% identity to the Caenorhabditis elegans homolog CHO-1, and is distantly related to members of the Na(+)-coupled glucose transporter (SGLT) gene family of Na(+)-coupled glucose (SGLT), nucleoside and iodide transporters. Northern blot analysis reveals the expression of a approximately 5 kb transcript in human brain regions rich in cholinergic neurons including the putamen, spinal cord, and medulla. Expression of hCHT cDNA in COS-7 cells results in saturable, Na(+)/Cl(-)-dependent choline uptake (K(m) = 1.2 microM) in membrane vesicles and [(3)H] HC-3 binding (K(d) = 4 nM) in membrane fractions, consistent with characteristics reported in mammalian cholinergic neurons. Using radiation hybrid mapping techniques, we localized the hCHT gene to human chromosome 2q12. These studies elucidate the primary structure and chromosomal localization of hCHT and provide a basis for mechanistic analysis of HACU regulation and an investigation of the role of hCHT in disease states.
Copyright 2000 Academic Press.
1 Communities
1 Members
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21 MeSH Terms