SwePub
Sök i LIBRIS databas

  Extended search

onr:"swepub:oai:DiVA.org:uu-136509"
 

Search: onr:"swepub:oai:DiVA.org:uu-136509" > Nuclear cysteine ca...

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Nuclear cysteine cathepsin variants in thyroid carcinoma cells

Tedelind, Sofia (author)
Poliakova, Kseniia (author)
Valeta, Amanda (author)
show more...
Hunegnaw, Ruth (author)
Yemanaberhan, Eyoel Lemma (author)
Heldin, Nils-Erik (author)
Uppsala universitet,Institutionen för genetik och patologi
Kurebayashi, Junichi (author)
Weber, Ekkehard (author)
Kopitar-Jerala, Natasa (author)
Turk, Boris (author)
Bogyo, Matthew (author)
Brix, Klaudia (author)
show less...
 (creator_code:org_t)
2010
2010
English.
In: Biological chemistry (Print). - 1431-6730 .- 1437-4315. ; 391:8, s. 923-935
Related links:
https://urn.kb.se/re...
show more...
https://doi.org/10.1...
show less...
  • Journal article (peer-reviewed)
Abstract Subject headings
Close  
  • 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.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Andra medicinska och farmaceutiska grundvetenskaper (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Other Basic Medicine (hsv//eng)

Keyword

cysteine peptidases
HTh7
HTh74
KTC-1
nuclear proteases
Chemistry
Kemi

Publication and Content Type

ref (subject category)
art (subject category)

Find in a library

To the university's database

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view