Isolation and structural characterization of thymosin-β4 from a human medullary thyroid carcinoma

1988 ◽  
Vol 118 (1) ◽  
pp. 155-159 ◽  
Author(s):  
J. M. Conlon ◽  
L. Grimelius ◽  
G. Wallin ◽  
L. Thim
Keyword(s):  
Amino Acid ◽  
Thyroid Carcinoma ◽  
Medullary Thyroid Carcinoma ◽  
Amino Acid Residues ◽  
Thymosin Β4 ◽  
High Concentration ◽  
Medullary Thyroid ◽  
Calf Thymus ◽  
Wet Weight

ABSTRACT An extract of a tumour metastases from a human medullary thyroid carcinoma contained a high concentration (at least 2·9 nmol/g wet weight) of the immunoregulatory peptide, thymosin-β4. The peptide was isolated as a mixture of two components with free and blocked NH2-terminal amino acid residues, the latter form predominating (approximately 98% of the total). The primary structure of the peptide was established by automated Edman degradation after cleavage with cyanogen bromide. The amino acid sequence of human thymosin-β4 was identical to thymosin-β4 previously isolated from calf thymus. Further studies are warranted to determine whether thymosin-β4 production is a useful marker for thyroid and other tumours. J. Endocr. (1988) 118, 155–159

scholarly journals 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

1988 ◽  
Vol 256 (1) ◽  
pp. 245-250 ◽  
Author(s):  
J M Conlon ◽  
L Grimelius ◽  
L Thim
Keyword(s):  
Amino Acid ◽  
Thyroid Carcinoma ◽  
Medullary Thyroid Carcinoma ◽  
High Molecular Mass ◽  
High Yield ◽  
Medullary Thyroid ◽  
C Terminus ◽  
Mass Form

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.

Cloning and characterization of two alternatively spliced rat α-amidating enzyme cDNAs from rat medullary thyroid carcinoma

1990 ◽  
Vol 279 (1) ◽  
pp. 87-96 ◽  
Author(s):  
Arthur H. Bertelsen ◽  
Gary A. Beaudry ◽  
Elizabeth A. Galella ◽  
Barry N. Jones ◽  
Martha L. Ray ◽  
...  
Keyword(s):  
Thyroid Carcinoma ◽  
Medullary Thyroid Carcinoma ◽  
Medullary Thyroid ◽  
Alternatively Spliced

scholarly journals Molecular characterization of the desmoplastic tumor stroma in medullary thyroid carcinoma

2007 ◽  
Author(s):  
Oskar Koperek ◽  
Christian Scheuba ◽  
Christina Puri ◽  
Peter Birner ◽  
Christian Haslinger ◽  
...  
Keyword(s):  
Thyroid Carcinoma ◽  
Medullary Thyroid Carcinoma ◽  
Molecular Characterization ◽  
Tumor Stroma ◽  
Medullary Thyroid

scholarly journals Characterization of Human Medullary Thyroid Carcinoma Glycosphingolipids Identifies Potential Cancer Markers

2021 ◽  
Vol 22 (19) ◽  
pp. 10463
Author(s):  
Karin Säljö ◽  
Anders Thornell ◽  
Chunsheng Jin ◽  
Olov Norlén ◽  
Susann Teneberg
Keyword(s):  
Thyroid Carcinoma ◽  
Medullary Thyroid Carcinoma ◽  
Variable Intensity ◽  
Medullary Thyroid ◽  
Thyroid Glands ◽  
Gd3 Ganglioside ◽  
Major Acid ◽  
Potential Cancer

Medullary thyroid carcinoma (MTC) accounts for only 1–2% of thyroid cancers; however, metastatic MTC is a mortal disease with no cure. In this study, glycosphingolipids were isolated from human MTCs and characterized by mass spectrometry and binding of carbohydrate recognizing ligands. The tissue distribution of selected compounds was investigated by immunohistochemistry. The amount of acid glycosphingolipids in the MTCs was higher than in the normal thyroid glands. The major acid glycosphingolipid was the GD3 ganglioside. Sulfatide and the gangliosides GM3 and GD1a were also present. The majority of the complex non-acid glycosphingolipids had type 2 (Galβ4GlcNAc) core chains, i.e., the neolactotetraosylceramide, the Lex, H type 2 and x2 pentaosylceramides, the Ley and A type 2 hexaosylceramides, and the A type 2 heptaosylceramide. There were also compounds with globo (GalαGalβ4Glc) core, i.e., globotriaosylceramide, globotetraosylceramide, the Forssman pentaosylceramide, and the Globo H hexaosylceramide. Immunohistochemistry demonstrated an extensive expression av Ley in the MTC cells and also a variable intensity and prevalence of Globo H and Lex. One individual with multiple endocrine neoplasia type 2B expressed the Forssman determinant, which is rarely found in humans. This study of human MTC glycosphingolipids identifies glycans that could serve as potential tumor-specific markers.

scholarly journals Amino Acid-Modified Calcitonin Immunization Induces Tumor Epitope-Specific Immunity in a Transgenic Mouse Model for Medullary Thyroid Carcinoma

Endocrinology ◽  
2008 ◽  
Vol 149 (11) ◽  
pp. 5627-5634 ◽  
Author(s):  
Margret Wuttke ◽  
Claudia Papewalis ◽  
Yvonne Meyer ◽  
Caroline Kessler ◽  
Benedikt Jacobs ◽  
...  
Keyword(s):  
T Cells ◽  
Amino Acid ◽  
Mouse Model ◽  
Thyroid Carcinoma ◽  
Medullary Thyroid Carcinoma ◽  
Transgenic Mouse ◽  
Transgenic Mouse Model ◽  
Medullary Thyroid ◽  
Tumor Outgrowth ◽  
Control Protein

Up to now, no relevant tumor antigen has been identified in medullary thyroid carcinoma (MTC). The aim of the present study was to prove the concept of an immunization with an amino acid-modified calcitonin (CT) for the treatment of MTC in a transgenic mouse model. Amino acid-modified (human) CT has been chosen for vaccination because of its higher binding affinity to the murine H2-Kb-MHC molecule. Mice were immunized over 6 months with monthly injections of amino acid-modified CT-pulsed dendritic cells. For enumeration of tumor epitope-specific CD8+ cytotoxic T cells, tetramer analyses were performed. CT peptide-treated mice revealed a mean 0.73 ± 0.45 and 0.91 ± 0.59% positive cells, depending on the two tetramers tested, whereas no increase was seen in control protein-immunized mice (0.08–0.12% tetramer-positive cells). Importantly, the subset of CT-specific CD8+ T cells also showed a high expression of interferon-γ. In line with these results, CT-immunized mice also showed an intratumor infiltration with CD8+ T lymphocytes. Importantly, we also found a diminished tumor outgrowth of −57% and a decrease of the serum CT levels (2.0 ± 0.1 pg/ml) compared with control protein-immunized Ret/Cal mice (3.0 ± 0.4 pg/ml). In summary, we show that amino acid-modified CT is recognized from the immune system leading to a specific antitumor immune response and a diminished tumor outgrowth in transgenic MTC mice. The results are of potential importance because they might be applicable to patients with metastatic spread of a MTC.

Establishment and characterization of a novel cell line of medullary thyroid carcinoma from a dog

2019 ◽  
Vol 55 (7) ◽  
pp. 559-566
Author(s):  
Kumiko Okano ◽  
Yosuke Uematsu ◽  
Kazumi Nibe ◽  
Masao Yamashita ◽  
Satoshi Suzuki ◽  
...  
Keyword(s):  
Thyroid Carcinoma ◽  
Cell Line ◽  
Medullary Thyroid Carcinoma ◽  
Medullary Thyroid
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