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Human basic fibroblast growth factor gene encodes four polypeptides: three initiate translation from non-AUG codons
1Whittier Institute for Diabetes and Endocrinology, La Jolla, CA 92037.
Summary
Human basic fibroblast growth factor (bFGF) exhibits multiple molecular forms. These diverse bFGF proteins initiate from unusual non-AUG codons, resulting in N-terminal extensions.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Human basic fibroblast growth factor (bFGF) is an angiogenic polypeptide mitogen.
- bFGF is found in various mesoderm- and neuroectoderm-derived tissues.
- Predicted bFGF gene product is 17.8-kDa (155 amino acids) initiated at an ATG codon.
Purpose of the Study:
- To investigate the molecular forms of bFGF expressed in the human cell line SK-HEP-1.
- To identify the initiation sites of different bFGF molecular weight forms.
- To characterize the relationship between the various bFGF proteins.
Main Methods:
- Analysis of molecular forms of bFGF in SK-HEP-1 cell line.
- Identification of translational initiation sites (AUG and non-AUG codons).
- Characterization of N-terminal sequences of bFGF variants.
Main Results:
- SK-HEP-1 cells coexpress four molecular forms of bFGF (17.8, 22.5, 23.1, and 24.2 kDa).
- The 17.8-kDa bFGF initiates at the predicted AUG codon.
- Higher molecular weight bFGF forms initiate at non-AUG codons, representing N-terminal extensions.
Conclusions:
- Human bFGF expression involves initiation at non-AUG codons, generating multiple protein isoforms.
- These findings expand the understanding of bFGF translational regulation.
- Multiple bFGF forms may have distinct biological functions due to N-terminal variations.