Identification of a new chromogranin B fragment (314–365) in endocrine tumors

A rabbit antiserum was raised against the fragment (350–365) of human chromogranin B corresponding to the C-terminal end of a putative proteolytic fragment generated by the cleavage of a dibasic doublet located in position 366–367 of the precursor. A radioimmunoassay was developed. Chromatographic a...

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Published in:	Peptides (New York, N.Y. : 1980) Vol. 16; no. 2; pp. 231 - 236
Main Authors:	Woussen-Colle, Marie-Claire, Gourlet, Philippe, Vandermeers, André, Vandermeers-Piret, Marie-Claire, D'Haens, Jean, Velkeniers, Brigitte, Robberechi, Patrick
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 1995
Subjects:	Adenoma - chemistry Amino Acid Sequence Animals Carcinoid Tumor - chemistry Chromogranin B Chromogranin B fragment Chromogranin B proteolysis Chromogranins - analysis Endocrine Gland Neoplasms - chemistry Endocrine tumors Gastrinoma - chemistry Humans Immune Sera Liver Neoplasms - chemistry Liver Neoplasms - secondary Molecular Sequence Data Pancreatic Neoplasms - chemistry Peptide Fragments - analysis Pituitary Neoplasms - chemistry Rabbits - immunology Radioimmunoassay Thyroid Neoplasms - chemistry Vipoma - chemistry Chromogranin B fragment Endocrine tumors Chromogranin B proteolysis
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Summary:	A rabbit antiserum was raised against the fragment (350–365) of human chromogranin B corresponding to the C-terminal end of a putative proteolytic fragment generated by the cleavage of a dibasic doublet located in position 366–367 of the precursor. A radioimmunoassay was developed. Chromatographic analysis of 10 endocrine tumor extracts (one liver metastasis of a gastrinoma, one liver metastasis of a medullary carcinoma of the thyroid, one VIPoma, one insulinoma, one nonsecreting pancreatic endocrine tumor, one local recurrence of a gut carcinoid, two pituitary gonadotropinoma, and two nonsecreting pituitary adenomas) revealed the presence of two forms of immunoreactive material. The most abundant form had an apparent molecular weight of 4500 and was purified to homogeneity by successive reverse-phase HPLC chromatographies and partially sequenced. The N-terminal sequence of the peptide, established by automated Edman degradation, was A-S-E-E-E-P-E-Y-G-E-E-I-K-G-Y-P-G-V-Q and corresponded to the 314–332 sequence of human chromogranin B. Taking into account the specificity of the antiserum used for peptide identification, we deduced that the purified peptide was chromogranin B(314–365) and represented a new form generated by limited proteolysis of chromogranin B.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0196-9781 1873-5169
DOI:	10.1016/0196-9781(94)00176-6