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
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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.
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1990 ◽
Vol 279
(1)
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pp. 87-96
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2018 ◽
Vol 57
(3)
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pp. 151-158
1991 ◽
Vol 72
(2)
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pp. 327-335
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1995 ◽
Vol 80
(2)
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pp. 138-149
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2021 ◽
Vol 22
(19)
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pp. 10463