Related Experiment Video
Updated: Aug 12, 2026

18:27
Preparing T Cell Growth Factor from Rat Splenocytes
Published on: October 31, 2007
A second thyroglobulin messenger RNA species (rTg-2) in rat thyrocytes
1Department of Medicine, Mount Sinai School of Medicine, New York, New York 10029.
Molecular Endocrinology (Baltimore, Md.)
|January 1, 1990
Summary
A novel, smaller thyroglobulin (Tg) mRNA, termed rTg-2, was discovered in rat thyroid cells. This thyroid-specific transcript may play a role in thyroid function and autoimmunity.
Area of Science:
- Molecular Biology
- Endocrinology
- Genetics
Background:
- Thyroglobulin (Tg) is a key protein in thyroid hormone synthesis.
- Thyroid-specific transcripts are crucial for understanding thyroid function.
- Previous research focused on the 9.0-kb Tg mRNA.
Purpose of the Study:
- To identify and characterize novel RNA transcripts in rat thyrocytes.
- To investigate the structure and potential function of a newly detected smaller Tg mRNA.
- To explore the relationship of this transcript to known Tg mRNA and the Tg gene.
Main Methods:
- Oligonucleotide probing of RNA from rat thyrocyte cell lines and thyroid tissue.
- RNA characterization including cytoplasmic localization, polyadenylation, and TSH regulation.
- cDNA sequencing and comparison with known Tg sequences from various species.
- Analysis of the junction between shared and unique sequences within the Tg gene.
Main Results:
- A 0.95-kb thyroid-specific RNA (rTg-2 mRNA) was detected in rat thyrocytes.
- rTg-2 mRNA is cytoplasmic, polyadenylated, and TSH-regulated.
- It shares 5' coding information with the 9.0-kb Tg mRNA but has unique 3' sequences.
- The transcript originates at the exon-5/intron-5 boundary of the Tg gene.
Conclusions:
- A previously unreported, smaller Tg mRNA (rTg-2) exists in rat thyroid cells.
- This transcript encodes functionally significant elements of the Tg monomer.
- The polypeptide product of rTg-2 mRNA may be involved in thyroid function and autoimmunity.
Related Concept Videos
What are Second Messengers?
Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...
Transfer RNA Synthesis
One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
Insertion of Single-pass Transmembrane Proteins in the RER
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Receptor Tyrosine Kinases
Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
Small GTPases - Ras and Rho
Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
Three regulatory proteins control their activity:
TGF - β Signaling Pathway
The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...

