In vitro studies of DNA damage and repair mechanisms induced by BNCT in a poorly differentiated thyroid carcinoma cell line

2018 ◽  
Vol 57 (2) ◽  
pp. 143-152 ◽  
Author(s):  
C. Rodriguez ◽  
M. Carpano ◽  
P. Curotto ◽  
S. Thorp ◽  
M. Casal ◽  
...  
2006 ◽  
Vol 27 (4) ◽  
pp. 353-358 ◽  
Author(s):  
Kathrin Marx ◽  
Detlef Moka ◽  
Klaus Schomäcker ◽  
Thomas Fischer ◽  
Beate Gabruk-Szostak ◽  
...  

Thyroid ◽  
2000 ◽  
Vol 10 (11) ◽  
pp. 939-943 ◽  
Author(s):  
Jan W.A. Smit ◽  
Janny P. Schröder-van der Elst ◽  
Marcel Karperien ◽  
Ivo Que ◽  
Gabri van der Pluijm ◽  
...  

1996 ◽  
Vol 101 (2) ◽  
pp. 247-255 ◽  
Author(s):  
Kazuhiro Nakahashi ◽  
Yoshiteru Kitahori ◽  
Noboru Konishi ◽  
Takeo Ohnishi ◽  
Masahito Sugimura ◽  
...  

2010 ◽  
Vol 391 (8) ◽  
Author(s):  
Sofia Tedelind ◽  
Kseniia Poliakova ◽  
Amanda Valeta ◽  
Ruth Hunegnaw ◽  
Eyoel Lemma Yemanaberhan ◽  
...  

Abstract The cysteine peptidase cathepsin B is important in thyroid physiology by being involved in thyroid prohormone processing initiated in the follicular lumen and completed in endo-lysosomal compartments. However, cathepsin B has also been localized to the extrafollicular space and is therefore suggested to promote invasiveness and metastasis in thyroid carcinomas through, e.g., ECM degradation. In this study, immunofluorescence and biochemical data from subcellular fractionation revealed that cathepsin B, in its single- and two-chain forms, is localized to endo-lysosomes in the papillary thyroid carcinoma cell line KTC-1 and in the anaplastic thyroid carcinoma cell lines HTh7 and HTh74. This distribution is not affected by thyroid stimulating hormone (TSH) incubation of HTh74, the only cell line that expresses a functional TSH-receptor. Immunofluorescence data disclosed an additional nuclear localization of cathepsin B immunoreactivity. This was supported by biochemical data showing a proteolytically active variant slightly smaller than the cathepsin B proform in nuclear fractions. We also demonstrate that immunoreactions specific for cathepsin V, but not cathepsin L, are localized to the nucleus in HTh74 in peri-nucleolar patterns. As deduced from co-localization studies and in vitro degradation assays, we suggest that nuclear variants of cathepsins are involved in the development of thyroid malignancies through modification of DNA-associated proteins.


Thyroid ◽  
2004 ◽  
Vol 14 (11) ◽  
pp. 889-895 ◽  
Author(s):  
Yong Jin Lee ◽  
June-Key Chung ◽  
Jae Hoon Shin ◽  
Joo Hyun Kang ◽  
Jae Min Jeong ◽  
...  

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