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Rat pre-prosomatostatin. Structure and processing by microsomal membranes.

R H Goodman, D C Aron, B A Roos

    The Journal of Biological Chemistry
    |May 10, 1983
    PubMed
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    Researchers determined the full sequence of rat pre-prosomatostatin, identifying its processing site. This tetradecapeptide hormone precursor shows high similarity to human forms, suggesting conserved functions.

    Area of Science:

    • Molecular Endocrinology
    • Protein Chemistry
    • Genomics

    Background:

    • Somatostatin, a tetradecapeptide hormone, is derived from a larger precursor, pre-prosomatostatin.
    • Hormone precursor studies suggest a leader sequence at the NH2 terminus of pre-prosomatostatin is cleaved during translation to form prosomatostatin.

    Purpose of the Study:

    • To determine the complete amino acid sequence of rat pre-prosomatostatin.
    • To identify the precise cleavage site of the leader region from prosomatostatin.
    • To compare rat and human pre-prosomatostatin sequences and assess evolutionary conservation.

    Main Methods:

    • Deduction of the complete rat pre-prosomatostatin sequence from cDNA nucleotide sequences.
    • Cell-free translation of medullary thyroid carcinoma mRNA using dog pancreas microsomal membranes.

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  • Partial microsequencing to pinpoint the leader region cleavage site.

    • Main Results:

    • The complete sequence of rat pre-prosomatostatin was determined, comprising 116 amino acids.
    • Cleavage of the leader region occurs between glycine and alanine at positions 24 and 25, yielding a 92-amino acid prosomatostatin.
    • Rat and human pre-prosomatostatin sequences exhibit high homology with only four amino acid substitutions.

    Conclusions:

    • Rat prosomatostatin is processed from a 116-amino acid precursor, with cleavage occurring at a specific site.
    • The high conservation between rat and human pre-prosomatostatin suggests conserved biological functions, potentially including the NH2-terminal regions.