SwePub
Sök i SwePub databas

  Utökad sökning

Träfflista för sökning "WFRF:(Kehlen Astrid) "

Sökning: WFRF:(Kehlen Astrid)

  • Resultat 1-2 av 2
Sortera/gruppera träfflistan
   
NumreringReferensOmslagsbildHitta
1.
  • Glogowska, Aleksandra, et al. (författare)
  • The cytoplasmic domain of proEGF negatively regulates motility and elastinolytic activity in thyroid carcinoma cells
  • 2008
  • Ingår i: Neoplasia. - : Elsevier BV. - 1522-8002 .- 1476-5586. ; 10:10, s. 1120-1130
  • Tidskriftsartikel (refereegranskat)abstract
    • 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.
  •  
2.
  • Mustafa, Tarek, et al. (författare)
  • Expression of the epidermal growth factor seven-transmembrane member CD97 correlates with grading and staging in human oral squamous cell carcinomas
  • 2005
  • Ingår i: Cancer Epidemiology, Biomarkers and Prevention. - 1055-9965 .- 1538-7755. ; 14:1, s. 108-119
  • Tidskriftsartikel (refereegranskat)abstract
    • INTRODUCTION: The oral squamous cell carcinoma (OSCC) is the sixth most common malignant tumor worldwide. No significant better progress has been made in the treatment of OSCCs during the last decades. The heterodimeric CD97 protein is a epidermal growth factor seven-transmembrane family member and was identified as a dedifferentiation marker in thyroid carcinomas. Nothing is known about CD97 in OSCCs. Material andMETHODS: Employing UV-laser microdissection, CD97 and its ligand CD55 were investigated in normal oral mucosa and OSCCs (n = 78) by multiplex reverse transcription-PCR. Frozen sections were investigated by immunohistochemistry. The effects of retinoic acid and sodium butyrate on the CD97/CD55 expression in OSCC cell lines were determined by quantitative PCR, immunocytochemistry, and flow cytometry.RESULTS: Weak CD97 transcripts were expressed in normal mucosa and normal basal epithelial cells revealed specific CD97 immunostaining. Strong CD97 transcripts were detected in pT(3)/T(4) and G3/G4 OSCC tissues, whereas pT(1)/T(2) and G1/G2 carcinomas revealed weak CD97 transcript levels. A weak CD97 immunostaining was observed in pT(1)/T(2) and G1/G2 tumors. By contrast, intensive CD97 immunostaining was detected in pT(3)/T(4) OSCCs and G3/G4 lesions. CD55 gene expression was low in normal mucosa. All OSCCs, irrespective of stage and grading, displayed strong CD55 immunostaining. Sodium butyrate and retinoic acid inhibited CD97 mRNA and protein in OSCC cell lines. Interestingly, CD55 was up-regulated by both substances.CONCLUSION: We identified CD97 as a novel marker of dedifferentiated OSCC. Interaction of CD97 and CD55 may facilitate adhesion of OSCC cells to surrounding surfaces that would result in metastases and bad prognosis.
  •  
Skapa referenser, mejla, bekava och länka
  • Resultat 1-2 av 2

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 Stäng

Kopiera och spara länken för att återkomma till aktuell vy