Structural characterization of a high-molecular-mass form of calcitonin [procalcitonin-(60-116)-peptide] and its corresponding N-terminal flanking peptide [procalcitonin-(1-57)-peptide] in a human medullary thyroid carcinoma.
Four peptides derived from procalcitonin were isolated in high yield from an extract of a human medullary thyroid carcinoma. The peptides were identified as procalcitonin-(1-57)-peptide, procalcitonin-(60-91)-peptide (calcitonin), procalcitonin-(60-116)-peptide and procalcitonin-(96-116)-peptide (katacalcin). Determination of the amino acid sequence of procalcitonin-(1-57)-peptide has demonstrated that the Ala25-Ala26 bond in preprocalcitonin is the site of cleavage of the signal peptide. Procalcitonin-(60-116)-peptide represents calcitonin extended from its C-terminus by the sequence Gly-Lys-Lys-Arg-katacalcin, and its formation is indicative of an aberrant pathway of procalcitonin processing in the tumour cells.
Conlon
J M
JM
Klinische Arbeitsgruppe für Gastrointestinale Endokrinologie, Max-Planck-Gesellschaft, Universität Göttingen.
Grimelius
L
L
Thim
L
L
D000596:Amino Acids / Q000032:analysis; D002116:Calcitonin / Q000302:isolation & purification; D015740:Calcitonin Gene-Related Peptide; D006801:Humans; D008970:Molecular Weight; D009479:Neuropeptides / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis*; D011498:Protein Precursors / Q000302:isolation & purification; D011863:Radioimmunoassay; D013964:Thyroid Neoplasms / Q000032:analysis*
D000596:Amino Acids; C000606589:CALCA protein, human; D009479:Neuropeptides; D010446:Peptide Fragments; D011498:Protein Precursors; D002116:Calcitonin; D015740:Calcitonin Gene-Related Peptide