BIOMAT Database Logo BIOMAT Database Logo

Identification of a novel myosin heavy chain gene expressed in the rat larynx. 1996

A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
Department of Surgery/Otolarygology, UCSD Medical School, La Jolla, CA 92093, USA.

Based on reactivity to antibodies against known myosin heavy chains, expression of a novel fast myosin heavy chain (MHC) gene was suspected in the thyroarytenoid (TA) muscle of the rat larynx. The 3' ends of MHC transcripts in the TA were amplified by RT-PCR using a primer to a highly conserved MHC sequence and to the poly(A) tail. The resultant products were cloned and fourteen PCR products were screened by dot-blotting with oligonucleotides specific for known skeletal muscle MHC genes. A clone that reacted weakly to the 2B oligo was sequenced and found to encode a novel fast MHC transcript, termed 2L, that appears to represent an eighth vertebrate skeletal muscle MHC gene. By homology analysis, the 2L sequence is most similar to the extraocular MHC, suggesting a possible evolutionary relationship between MHCs associated with the branchial arches.

UI MeSH Term Description Entries
D007150 Immunohistochemistry Histochemical localization of immunoreactive substances using labeled antibodies as reagents. Immunocytochemistry,Immunogold Techniques,Immunogold-Silver Techniques,Immunohistocytochemistry,Immunolabeling Techniques,Immunogold Technics,Immunogold-Silver Technics,Immunolabeling Technics,Immunogold Silver Technics,Immunogold Silver Techniques,Immunogold Technic,Immunogold Technique,Immunogold-Silver Technic,Immunogold-Silver Technique,Immunolabeling Technic,Immunolabeling Technique,Technic, Immunogold,Technic, Immunogold-Silver,Technic, Immunolabeling,Technics, Immunogold,Technics, Immunogold-Silver,Technics, Immunolabeling,Technique, Immunogold,Technique, Immunogold-Silver,Technique, Immunolabeling,Techniques, Immunogold,Techniques, Immunogold-Silver,Techniques, Immunolabeling
D007830 Larynx A tubular organ of VOICE production. It is located in the anterior neck, superior to the TRACHEA and inferior to the tongue and HYOID BONE. Anterior Commissure, Laryngeal,Anterior Commissure, Larynx,Laryngeal Anterior Commissure,Laryngeal Posterior Commissure,Posterior Commissure, Laryngeal,Posterior Commissure, Larynx,Anterior Commissures, Laryngeal,Anterior Commissures, Larynx,Commissure, Laryngeal Anterior,Commissure, Laryngeal Posterior,Commissure, Larynx Anterior,Commissure, Larynx Posterior,Commissures, Laryngeal Anterior,Commissures, Laryngeal Posterior,Commissures, Larynx Anterior,Commissures, Larynx Posterior,Laryngeal Anterior Commissures,Laryngeal Posterior Commissures,Larynx Anterior Commissure,Larynx Anterior Commissures,Larynx Posterior Commissure,Larynx Posterior Commissures,Posterior Commissures, Laryngeal,Posterior Commissures, Larynx
D008297 Male Males
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
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
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated
D016133 Polymerase Chain Reaction In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships. Anchored PCR,Inverse PCR,Nested PCR,PCR,Anchored Polymerase Chain Reaction,Inverse Polymerase Chain Reaction,Nested Polymerase Chain Reaction,PCR, Anchored,PCR, Inverse,PCR, Nested,Polymerase Chain Reactions,Reaction, Polymerase Chain,Reactions, Polymerase Chain
D017207 Rats, Sprague-Dawley A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company. Holtzman Rat,Rats, Holtzman,Sprague-Dawley Rat,Rats, Sprague Dawley,Holtzman Rats,Rat, Holtzman,Rat, Sprague-Dawley,Sprague Dawley Rat,Sprague Dawley Rats,Sprague-Dawley Rats

Related Publications

A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
Molecular characterization of a novel atrial-specific myosin heavy-chain gene expressed in the chick embryo.
May 1995, European journal of cell biology,
A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
Identification and developmental expression of a novel embryonic myosin heavy-chain gene in chicken.
January 1989, DNA (Mary Ann Liebert, Inc.),
A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
Two distinct nonmuscle myosin-heavy-chain mRNAs are differentially expressed in various chicken tissues. Identification of a novel gene family of vertebrate non-sarcomeric myosin heavy chains.
October 1989, European journal of biochemistry,
A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
Identification of a myosin heavy chain gene from Entamoeba histolytica.
January 1992, Archives of medical research,
A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
A novel myosin heavy chain gene in human chromosome 19q13.3.
July 2003, Gene,
A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
Identification of the structural gene for a myosin heavy-chain in Caenorhabditis elegans.
July 1977, Journal of molecular biology,
A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
Characterization of a developmentally regulated perinatal myosin heavy-chain gene expressed in skeletal muscle.
November 1984, The Journal of biological chemistry,
A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
Identification of the gene for fly non-muscle myosin heavy chain: Drosophila myosin heavy chains are encoded by a gene family.
March 1989, The EMBO journal,
A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
The genome of the diploid anuran Xenopus tropicalis contains a novel array of sarcoplasmic myosin heavy chain genes expressed in larval muscle and larynx.
July 2008, Development genes and evolution,
A L Merati, and S C Bodine, and T Bennett, and H H Jung, and H Furuta, and A F Ryan
Prolactin opens the sensitive period for androgen regulation of a larynx-specific myosin heavy chain gene.
December 1999, Journal of neurobiology,
Copied contents to your clipboard!