Elaboration of nonsomatostatin peptides containing the amino-terminal portion of prosomatostatin in a somatostatin-secreting human medullary thyroid carcinoma cell line

D. C. Aron, G. Mendelsohn, B. A. Roos

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Abstract

We identified a system, the TT human medullary thryoid carcinoma cell line which contained 74.5 ± 26.0 ng (mean ± SD) immunoreactive SRIH/mg protein, for studying the products of SRIH gene expression. The close homology between man and rat for the entire proSRIH and complete homology for a portion of the amino terminus (proSRIH-NTP) permitted the application of a RIA directed toward the amino terminus of rat proSRIH. Immunohistochemical studies of the human TT cell line showed that SRIH and proSRIH-NTP immunoreactivities were present in the same cells. RIA of gel filtration fractions showed that the major cellular proSRIH-NTP-containing species lack SRIH and had an apparent mol wt of 8000. A 10,000-dalton SRIH-containing species coeluting with proSRIH-NTP immunoreactivity, putative proSRIH, also was found. Similar species were found in culture medium. The major cellular and secreted form of SRIH immunoreactivity had a mol wt of 1600 (SRIH). High pressure liquid chromatography revealed that both cellular and secreted 8000-dalton proSRIH-NTP-containing material consisted of a major and several minor species. None of the species contained SRIH. The precise structure of these proSRIH-NTP-containing species and their physiological roles are not known. The fact that proSRIH-NTP-containing species are secreted suggests that they may be functional. Since the processing of proSRIH and consequently the final products appear to be tissue specific, alterations in the relative presence of different forms might reflect specific pathological processes.

Original languageEnglish
Pages (from-to)1237-1242
Number of pages6
JournalJournal of Clinical Endocrinology and Metabolism
Volume62
Issue number6
StatePublished - Jan 1 1986

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Somatostatin
Rats
Cells
High pressure liquid chromatography
Cell Line
Peptides
Medullary Carcinoma
Pathologic Processes
Gene expression
Gel Chromatography
Culture Media
Gels
High Pressure Liquid Chromatography
Tissue
Gene Expression
Processing
Proteins
prosomatostatin
Medullary Thyroid cancer

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology, Diabetes and Metabolism

Cite this

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title = "Elaboration of nonsomatostatin peptides containing the amino-terminal portion of prosomatostatin in a somatostatin-secreting human medullary thyroid carcinoma cell line",
abstract = "We identified a system, the TT human medullary thryoid carcinoma cell line which contained 74.5 ± 26.0 ng (mean ± SD) immunoreactive SRIH/mg protein, for studying the products of SRIH gene expression. The close homology between man and rat for the entire proSRIH and complete homology for a portion of the amino terminus (proSRIH-NTP) permitted the application of a RIA directed toward the amino terminus of rat proSRIH. Immunohistochemical studies of the human TT cell line showed that SRIH and proSRIH-NTP immunoreactivities were present in the same cells. RIA of gel filtration fractions showed that the major cellular proSRIH-NTP-containing species lack SRIH and had an apparent mol wt of 8000. A 10,000-dalton SRIH-containing species coeluting with proSRIH-NTP immunoreactivity, putative proSRIH, also was found. Similar species were found in culture medium. The major cellular and secreted form of SRIH immunoreactivity had a mol wt of 1600 (SRIH). High pressure liquid chromatography revealed that both cellular and secreted 8000-dalton proSRIH-NTP-containing material consisted of a major and several minor species. None of the species contained SRIH. The precise structure of these proSRIH-NTP-containing species and their physiological roles are not known. The fact that proSRIH-NTP-containing species are secreted suggests that they may be functional. Since the processing of proSRIH and consequently the final products appear to be tissue specific, alterations in the relative presence of different forms might reflect specific pathological processes.",
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T1 - Elaboration of nonsomatostatin peptides containing the amino-terminal portion of prosomatostatin in a somatostatin-secreting human medullary thyroid carcinoma cell line

AU - Aron, D. C.

AU - Mendelsohn, G.

AU - Roos, B. A.

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N2 - We identified a system, the TT human medullary thryoid carcinoma cell line which contained 74.5 ± 26.0 ng (mean ± SD) immunoreactive SRIH/mg protein, for studying the products of SRIH gene expression. The close homology between man and rat for the entire proSRIH and complete homology for a portion of the amino terminus (proSRIH-NTP) permitted the application of a RIA directed toward the amino terminus of rat proSRIH. Immunohistochemical studies of the human TT cell line showed that SRIH and proSRIH-NTP immunoreactivities were present in the same cells. RIA of gel filtration fractions showed that the major cellular proSRIH-NTP-containing species lack SRIH and had an apparent mol wt of 8000. A 10,000-dalton SRIH-containing species coeluting with proSRIH-NTP immunoreactivity, putative proSRIH, also was found. Similar species were found in culture medium. The major cellular and secreted form of SRIH immunoreactivity had a mol wt of 1600 (SRIH). High pressure liquid chromatography revealed that both cellular and secreted 8000-dalton proSRIH-NTP-containing material consisted of a major and several minor species. None of the species contained SRIH. The precise structure of these proSRIH-NTP-containing species and their physiological roles are not known. The fact that proSRIH-NTP-containing species are secreted suggests that they may be functional. Since the processing of proSRIH and consequently the final products appear to be tissue specific, alterations in the relative presence of different forms might reflect specific pathological processes.

AB - We identified a system, the TT human medullary thryoid carcinoma cell line which contained 74.5 ± 26.0 ng (mean ± SD) immunoreactive SRIH/mg protein, for studying the products of SRIH gene expression. The close homology between man and rat for the entire proSRIH and complete homology for a portion of the amino terminus (proSRIH-NTP) permitted the application of a RIA directed toward the amino terminus of rat proSRIH. Immunohistochemical studies of the human TT cell line showed that SRIH and proSRIH-NTP immunoreactivities were present in the same cells. RIA of gel filtration fractions showed that the major cellular proSRIH-NTP-containing species lack SRIH and had an apparent mol wt of 8000. A 10,000-dalton SRIH-containing species coeluting with proSRIH-NTP immunoreactivity, putative proSRIH, also was found. Similar species were found in culture medium. The major cellular and secreted form of SRIH immunoreactivity had a mol wt of 1600 (SRIH). High pressure liquid chromatography revealed that both cellular and secreted 8000-dalton proSRIH-NTP-containing material consisted of a major and several minor species. None of the species contained SRIH. The precise structure of these proSRIH-NTP-containing species and their physiological roles are not known. The fact that proSRIH-NTP-containing species are secreted suggests that they may be functional. Since the processing of proSRIH and consequently the final products appear to be tissue specific, alterations in the relative presence of different forms might reflect specific pathological processes.

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