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Human epidermal growth factor precursor: cDNA sequence, expression in vitro and gene organization.
Nucleic Acids Research
|November 11, 1986
Summary
Researchers isolated and sequenced human kidney epidermal growth factor (EGF) precursor cDNA. This revealed a 1,207 amino acid protein, structurally similar to mouse EGF, synthesized as a membrane protein.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Epidermal Growth Factor (EGF) plays a crucial role in cellular processes.
- Understanding the structure and gene organization of EGF precursors is vital for comprehending its function.
Purpose of the Study:
- To isolate and sequence complementary DNA (cDNA) clones encoding the human kidney EGF precursor.
- To elucidate the structural organization and gene structure of the human EGF precursor.
Main Methods:
- Isolation and sequencing of human kidney EGF precursor cDNA clones.
- Transfection of COS-7 cells with the human EGF precursor cDNA.
- Analysis of the human EGF precursor gene's exon-intron organization.
Main Results:
- The human EGF precursor is a 1,207 amino acid protein with a conserved structural organization compared to the mouse homolog (66% sequence identity).
- The precursor is synthesized as a membrane protein with the NH2-terminus exposed extracellularly.
- The human EGF precursor gene spans approximately 110 kilobase pairs and comprises 24 exons, with individual exons encoding distinct functional domains.
- Fifteen exons encode protein segments homologous to other known proteins, suggesting a role for exon duplication and shuffling in its evolution.
Conclusions:
- The human kidney EGF precursor exhibits significant structural similarity to its mouse counterpart.
- The gene structure suggests evolutionary mechanisms like exon duplication and shuffling contributed to the EGF precursor's complex domain organization.