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  • Glogowska, AleksandraDepartment of Human Anatomy and Cell Science, Winnipeg, Manitoba, Canada (författare)

The cytoplasmic domain of proEGF negatively regulates motility and elastinolytic activity in thyroid carcinoma cells

  • Artikel/kapitelEngelska2008

Förlag, utgivningsår, omfång ...

  • Elsevier BV,2008
  • electronicrdacarrier

Nummerbeteckningar

  • LIBRIS-ID:oai:DiVA.org:liu-86922
  • https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-86922URI
  • https://doi.org/10.1593/neo.08580DOI

Kompletterande språkuppgifter

  • Språk:engelska
  • Sammanfattning på:engelska

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  • Ämneskategori:ref swepub-contenttype
  • Ämneskategori:art swepub-publicationtype

Anmärkningar

  • The intracellular domains of the membrane-anchoring regions of some precursors of epidermal growth factor (EGF) family members have intrinsic biologic activities. We have determined the role of the human proEGF cytoplasmic domain (proEGFcyt) as part of the proEGF transmembrane-anchored region (proEGFctF) in the regulation of motility and elastinolytic invasion in human thyroid cancer cells. We found proEGFctF to act as a negative regulator of motility and elastin matrix penetration and the presence of proEGFcyt or proEGF22.23 resulted in a similar reduction in motility and elastinolytic migration. This activity was counteracted by EGF-induced activation of EGF receptor signaling. Decreased elastinolytic migratory activity in the presence of proEGFctF and proEGFcyt/proEGF22.23 coincided with decreased secretion of elastinolytic procathepsin L. The presence of proEGFctF and proEGFcyt/proEGF22.23 coincided with the specific transcriptional up-regulation of t-SNARE member SNAP25. Treatment with siRNA-SNAP25 resulted in motility and elastin migration being restored to normal levels. Epidermal growth factor treatment down-regulated SNAP25 protein by activating EGF receptor-mediated proteasomal degradation of SNAP25. These data provide first evidence for an important function of the cytoplasmic domain of the human proEGF transmembrane region as a novel suppressor of motility and cathepsin L-mediated elastinolytic invasion in human thyroid carcinoma cells and suggest important clinical implications for EGF-expressing tumors.

Ämnesord och genrebeteckningar

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Pyka, JanetteClinics of Surgery, Medical Faculty, Martin Luther University Halle-Wittenberg, Halle, Germany (författare)
  • Kehlen, AstridProbiodrug AG, Weinbergweg, Halle, Germany (författare)
  • Los, Marek JanBioApplications Enterprises, Winnipeg, MB, Canada(Swepub:liu)marlo14 (författare)
  • Perumal, PaulDepartment of Human Anatomy and Cell Science, Winnipeg, Manitoba, Canada (författare)
  • Weber, EkkehardInstitute of Physiological Chemistry, Medical Faculty, Martin Luther University Halle-Wittenberg, Halle, Germany (författare)
  • Cheng, Sheue-yannLaboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-4264, USA (författare)
  • Hoang-Vu, CuongClinics of Surgery, Medical Faculty, Martin Luther University Halle-Wittenberg, Halle, Germany (författare)
  • Klonisch, ThomasDepartment of Human Anatomy and Cell Science; Department of Medical Microbiology and Infectious Diseases, Faculty of Medicine, University of Manitoba, Winnipeg, Canada (författare)
  • Department of Human Anatomy and Cell Science, Winnipeg, Manitoba, CanadaClinics of Surgery, Medical Faculty, Martin Luther University Halle-Wittenberg, Halle, Germany (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:Neoplasia: Elsevier BV10:10, s. 1120-11301522-80021476-5586

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  • Neoplasia (Sök värdpublikationen i LIBRIS)

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