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Updated: Aug 14, 2026

Molecular Analysis of Endothelial-mesenchymal Transition Induced by Transforming Growth Factor-β Signaling
Published on: August 3, 2018
The murine transforming growth factor-beta precursor
Abstract:
Transforming growth factor-beta (TGF-beta) is a homodimeric polypeptide which can act, often in cooperation with other growth factors, as a mitogenic factor for a variety of cells. TGF-beta can also exert growth inhibitory activity on many other cell lines. We have isolated cDNAs coding for the murine TGF-beta cDNA precursor. The deduced amino acid sequence localizes the 112-amino acid long TGF-beta monomer to the C terminus of the precursor. Two areas of the precursor exhibit a marked degree of homology to the human counterpart. One of these regions comprises the mature TGF-beta monomer, while the other corresponds to the NH2 terminus of the precursor and suggests an important biological function for this area. Northern hybridization results identify a major 2.5-kilobase TGF-beta mRNA and several minor TGF-beta mRNA species.
Insights
Researchers isolated mouse transforming growth factor-beta (TGF-beta) cDNAs, revealing the mature TGF-beta monomer and a homologous N-terminal region suggesting biological importance. This study details TGF-beta precursor structure and mRNA expression.
Area of Science:
- Molecular Biology
- Cellular Biology
- Biochemistry
Background:
- Transforming growth factor-beta (TGF-beta) is a polypeptide with dual roles, acting as both a mitogenic and growth inhibitory factor for various cell types.
- Its function often depends on cooperation with other growth factors.
Purpose of the Study:
- To isolate and characterize cDNAs encoding the murine TGF-beta precursor.
- To analyze the deduced amino acid sequence for conserved regions and potential functional domains.
Main Methods:
- Isolation of complementary DNAs (cDNAs) for the murine TGF-beta precursor.
- Deduction of amino acid sequence from cDNA.
- Sequence homology analysis comparing murine and human counterparts.
- Northern hybridization to identify TGF-beta mRNA species.
Main Results:
- The 112-amino acid TGF-beta monomer is localized at the C-terminus of the precursor.
- Two homologous regions were identified between murine and human precursors: one for the mature TGF-beta monomer and another at the N-terminus.
- Northern hybridization revealed a major 2.5-kilobase TGF-beta mRNA and several minor species.
Conclusions:
- The N-terminal region of the TGF-beta precursor shows significant homology to the human counterpart, suggesting a crucial biological function.
- The study provides insights into the structural organization and gene expression of TGF-beta.
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