Molecular forms of katacalcin, calcitonin gene-related peptide and gastrin-releasing peptide, in a human medullary thyroid carcinoma.

Abstract

Peptides synthesized by a human medullary thyroid carcinoma were purified to homogeneity by reverse-phase high performance liquid chromatography and structurally characterized by determination of amino acid composition, amino acid sequence, and fast atom bombardment mass spectra. The katacalcin-related material in the tumor extract was heterogeneous. Katacalcin (1-21) represented the predominant molecular form but metabolites, identified as katacalcin (1-20), (1-19), (1-15) and (1-13), were also identified in high concentration. Calcitonin gene-related peptide-I was isolated from the tumor but calcitonin gene-related peptide-II was absent. A minor component of calcitonin gene-related peptide-like immunoreactivity was of higher molecular weight and may represent an incompletely processed form of the prohormone. Gastrin-releasing peptide (1-27) and gastrin-releasing peptide (18-27) (neuromedin C) were isolated from the tumor but gastrin-releasing peptide (14-27) and bombesin were absent.

• Authors: J M Conlon, G P McGregor, G Wallin, L Grimelius, L Thim
• Journal: Cancer research (Cancer Res) Vol. 48 Issue 9 Pg. 2412-6 (May 01 1988) ISSN: 0008-5472 [Print] United States
• PMID: 3258543 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amino Acids
• Neuropeptides
• Peptide Fragments
• Peptides
• Gastrin-Releasing Peptide
• katacalcin
• Calcitonin
• Calcitonin Gene-Related Peptide

Topics

• Adult
• Amino Acid Sequence
• Amino Acids (analysis)
• Calcitonin (analysis, isolation & purification)
• Calcitonin Gene-Related Peptide
• Carcinoma (analysis)
• Gastrin-Releasing Peptide
• Humans
• Male
• Neuropeptides (analysis, isolation & purification)
• Peptide Fragments (analysis, isolation & purification)
• Peptides (analysis, isolation & purification)
• Thyroid Neoplasms (analysis)