BIOMAT Database Logo BIOMAT Database Logo

Growth/differentiation factor-10: a new member of the transforming growth factor-beta superfamily related to bone morphogenetic protein-3. 1995

N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
Department of Orthopaedic Surgery, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

We have identified a new member of the transforming growth factor-beta (TGF-beta) superfamily, growth/differentiation factor-10 (GDF-10), which is highly related to bone morphogenetic protein-3 (BMP-3). The nucleotide sequence of GDF-10 encodes a predicted protein of 476 amino acids with a molecular weight of approximately 52,000. The GDF-10 polypeptide contains a potential signal sequence for secretion, a putative RXXR proteolytic processing site, and a carboxy-terminal domain with considerable homology to other known members of the TGF-beta superfamily. In the mature carboxy-terminal domain GDF-10 is more homologous to BMP-3 (83% amino acid sequence identity) than to any other previously identified TGF-beta family member. GDF-10 also shows significant homology to BMP-3 (approximately 30% amino acid sequence identity) in the pro- region of the molecule. Based on these sequence comparisons, GDF-10 and BMP-3 define a new subgroup within the larger TGF-beta superfamily. By Northern analysis, GDF-10 mRNA was detected primarily in murine uterus, adipose tissue, and brain and to a lesser extent in liver and spleen. In addition, GDF-10 mRNA was present in both neonatal and adult bone samples, with higher levels being detected in calvaria than in long bone. These results suggest that GDF10 may play multiple roles in regulating cell differentiation events, including those involved in skeletal morphogenesis. Gdf10 was mapped to the proximal region of mouse chromosome 14 close to a region known to contain a spontaneous recessive mutation that is associated with a craniofacial defect.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D002874 Chromosome Mapping Any method used for determining the location of and relative distances between genes on a chromosome. Gene Mapping,Linkage Mapping,Genome Mapping,Chromosome Mappings,Gene Mappings,Genome Mappings,Linkage Mappings,Mapping, Chromosome,Mapping, Gene,Mapping, Genome,Mapping, Linkage,Mappings, Chromosome,Mappings, Gene,Mappings, Genome,Mappings, Linkage
D005260 Female Females
D006133 Growth Substances Signal molecules that are involved in the control of cell growth and differentiation. Mitogens, Endogenous,Endogenous Mitogens
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D014018 Tissue Distribution Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios. Distribution, Tissue,Distributions, Tissue,Tissue Distributions

Related Publications

N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
Isolation and sequence of the Drosophila virilis 60 A gene, a transforming growth factor-beta superfamily member related to vertebrate bone morphogenetic proteins.
July 1996, Biochimica et biophysica acta,
N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
Bone morphogenetic protein-7 in focus: a member of the transforming growth factor-beta superfamily is implicated in the maintenance of liver health.
May 2007, Hepatology (Baltimore, Md.),
N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
Cloning and characterization of a novel member of the transforming growth factor-beta/bone morphogenetic protein family.
May 1998, The Journal of biological chemistry,
N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
Characterization of growth-differentiation factor 15, a transforming growth factor beta superfamily member induced following liver injury.
May 2000, Molecular and cellular biology,
N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
Osteogenic protein-2. A new member of the transforming growth factor-beta superfamily expressed early in embryogenesis.
December 1992, The Journal of biological chemistry,
N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
Nuclear factor YY1 inhibits transforming growth factor beta- and bone morphogenetic protein-induced cell differentiation.
July 2003, Molecular and cellular biology,
N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
The transforming growth factor-beta superfamily member growth-differentiation factor-15 protects the heart from ischemia/reperfusion injury.
February 2006, Circulation research,
N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
Drosophila 60A gene, another transforming growth factor beta family member, is closely related to human bone morphogenetic proteins.
October 1991, Proceedings of the National Academy of Sciences of the United States of America,
N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
[Transforming growth factor-beta superfamily in the regulation of new bone formation].
March 2002, Zhongguo xiu fu chong jian wai ke za zhi = Zhongguo xiufu chongjian waike zazhi = Chinese journal of reparative and reconstructive surgery,
N S Cunningham, and N A Jenkins, and D J Gilbert, and N G Copeland, and A H Reddi, and S J Lee
Expression and processing of the activin-A/erythroid differentiation factor precursor: a member of the transforming growth factor-beta superfamily.
August 1990, Molecular endocrinology (Baltimore, Md.),
Copied contents to your clipboard!