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Pregled bibliografske jedinice broj: 726661

A soluble ectodomain of LRIG1 inhibits cancer cell growth by attenuating basal and ligand-dependent EGFR activity


Goldoni, Silvia; Iozzo, Rex A.; Kay, Paul; Campbell, Shelly; McQuillan, Angela; Agnew, Chris; Zhu, Jian Xhu; Keene, David R.; Reed, Charles C.; Iozzo, Renato V.
A soluble ectodomain of LRIG1 inhibits cancer cell growth by attenuating basal and ligand-dependent EGFR activity // Oncogene, 26 (2007), 3; 368-381 doi:10.1038/sj.onc.1209803 (međunarodna recenzija, članak, znanstveni)


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Naslov
A soluble ectodomain of LRIG1 inhibits cancer cell growth by attenuating basal and ligand-dependent EGFR activity

Autori
Goldoni, Silvia ; Iozzo, Rex A. ; Kay, Paul ; Campbell, Shelly ; McQuillan, Angela ; Agnew, Chris ; Zhu, Jian Xhu ; Keene, David R. ; Reed, Charles C. ; Iozzo, Renato V.

Izvornik
Oncogene (0950-9232) 26 (2007), 3; 368-381

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
leucine-rich protein; decorin; kekkon1; epidermal growth factor receptor; tumor growth inhibition

Sažetak
Leucine-rich repeats and immunoglobulin-like domains-1 (LRIG1) is a transmembrane protein with an ectodomain containing 15 leucine-rich repeats (LRRs) homologous to mammalian decorin and the Drosophila kekkon1 gene. In this study, we demonstrate that a soluble ectodomain of LRIG1, containing only the LRRs, inhibits ligand independent epidermal growth factor receptor (EGFR) activation and causes growth inhibition of A431, HeLa and MDA-468 carcinoma cells. In contrast, cells that do not express detectable levels of EGFR fail to respond to soluble LRIG1. However, when a functional EGFR gene is introduced in these cells, they become growth-inhibited by soluble LRIG1 protein. Furthermore, we demonstrate the existence of high-affinity (KdĽ10 nM) binding sites on the A431 cells that can be competitively displaced (up to 75%) by molar excess of EGF. Even more powerful effects are obtained with a chimeric proteoglycan harboring the N-terminus of decorin, substituted with a single glycosaminoglycan chain, fused to the LRIG1 ectodomain. Both proteins also inhibit ligand-dependent activation of the EGFR and extracellular signal regulated protein kinase 1/2 signaling in a rapid and dose-dependent manner. These results suggest a novel mechanism of action evoked by a soluble ectodomain of LRIG1 protein that could modulate EGFR signaling and its growthpromoting activity. Attenuation of EGFR activity without physical downregulation of the receptor could represent a novel therapeutic approach toward malignancies in which EGFR plays a primary role in tumor growth and survival.

Izvorni jezik
Engleski

Znanstvena područja
Biologija, Temeljne medicinske znanosti

Napomena
Shelly Pranić je rođena Shelly Campbell



POVEZANOST RADA


Profili:

Avatar Url Shelly Pranić (autor)

Citiraj ovu publikaciju

Goldoni, Silvia; Iozzo, Rex A.; Kay, Paul; Campbell, Shelly; McQuillan, Angela; Agnew, Chris; Zhu, Jian Xhu; Keene, David R.; Reed, Charles C.; Iozzo, Renato V.
A soluble ectodomain of LRIG1 inhibits cancer cell growth by attenuating basal and ligand-dependent EGFR activity // Oncogene, 26 (2007), 3; 368-381 doi:10.1038/sj.onc.1209803 (međunarodna recenzija, članak, znanstveni)
Goldoni, S., Iozzo, R., Kay, P., Campbell, S., McQuillan, A., Agnew, C., Zhu, J., Keene, D., Reed, C. & Iozzo, R. (2007) A soluble ectodomain of LRIG1 inhibits cancer cell growth by attenuating basal and ligand-dependent EGFR activity. Oncogene, 26 (3), 368-381 doi:10.1038/sj.onc.1209803.
@article{article, year = {2007}, pages = {368-381}, DOI = {10.1038/sj.onc.1209803}, keywords = {leucine-rich protein, decorin, kekkon1, epidermal growth factor receptor, tumor growth inhibition}, journal = {Oncogene}, doi = {10.1038/sj.onc.1209803}, volume = {26}, number = {3}, issn = {0950-9232}, title = {A soluble ectodomain of LRIG1 inhibits cancer cell growth by attenuating basal and ligand-dependent EGFR activity}, keyword = {leucine-rich protein, decorin, kekkon1, epidermal growth factor receptor, tumor growth inhibition} }
@article{article, year = {2007}, pages = {368-381}, DOI = {10.1038/sj.onc.1209803}, keywords = {leucine-rich protein, decorin, kekkon1, epidermal growth factor receptor, tumor growth inhibition}, journal = {Oncogene}, doi = {10.1038/sj.onc.1209803}, volume = {26}, number = {3}, issn = {0950-9232}, title = {A soluble ectodomain of LRIG1 inhibits cancer cell growth by attenuating basal and ligand-dependent EGFR activity}, keyword = {leucine-rich protein, decorin, kekkon1, epidermal growth factor receptor, tumor growth inhibition} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
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  • MEDLINE


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