Soluble epidermal growth factor receptor isoforms in non-small cell lung cancer tissue and in blood

Maramotti, Sally; Paci, Massimiliano; Miccichè, Francesca; Ciarrocchi, Alessia; Cavazza, Alberto; Bortoli, Maida De; Vaghi, E.; Formisano, Debora; Canovi, Laura; Sgarbi, Giorgio; Bongarzone, Italia

doi:10.1016/j.lungcan.2011.11.018

Cited by 19 publications

(22 citation statements)

References 23 publications

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“…Despite some reports showing increased values in affected patients, [36][37][38] most studies (and those including a higher number of subjects) reported a decrease of serum EGFR in cancer patients, with a proportional impact on survival. 18,[39][40][41][42][43][44] This supports the hypothesis that serum EGFR could be a different isoform with a physiological and tumorprotective role in the control of the EGFR-regulated signaling. 34 Similarly, we observed a reduction of serum EGFR in OSCC patients, but it was not possible to recognize any important impact on survival.…”

Section: Discussionsupporting

confidence: 78%

“…In the international literature, several studies have evaluated the diagnostic potential of serum EGFR in other tumors (in particular breast, lung, and ovarian tumors) with conflicting results. Despite some reports showing increased values in affected patients, most studies (and those including a higher number of subjects) reported a decrease of serum EGFR in cancer patients, with a proportional impact on survival . This supports the hypothesis that serum EGFR could be a different isoform with a physiological and tumor‐protective role in the control of the EGFR‐regulated signaling .…”

Section: Discussionmentioning

confidence: 69%

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Epidermal growth factor receptor detection in serum and saliva as a diagnostic and prognostic tool in oral cancer

et al. 2017

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Section: Discussionsupporting

confidence: 78%

Section: Discussionmentioning

confidence: 69%

Epidermal growth factor receptor detection in serum and saliva as a diagnostic and prognostic tool in oral cancer

et al. 2017

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“…The kinase domain of isoform1 of ErbB1 did not show any significant similarities with that of the other three isoforms ( Figure 1). Previous studies have demonstrated that only the first isoform is essentially involved in lung cancer (www.uniprot.org/uniprot/P00533) [9]. On the contrary, the kinase domains of all the five isoforms of ErbB2 show significant similarities (Figure 2).…”

Section: Sequence and Structure Analysismentioning

confidence: 90%

“…Although ErbB1 has four isoforms produced by alternative splicing, only the first isoform is primarily involved in lung cancer (www.uniprot. org/uniprot/P00533) [9]. ErbB2 has five isoforms (www.uniprot.org/ uniprot/P04626).…”

Section: Sequence and Structure Analysismentioning

confidence: 99%

A Holistic In Silico Approach to Find Novel Inhibitors for Erbb1 and Erbb2 Kinases

Hu¹,

Dong²,

Zhang³

2016

J Microb Biochem Technol

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“…HER-1 is a glycosylated transmembrane protein belonging to the tyrosine kinases ErbB family of receptors, which are key regulators of several biological processes, is implicated in tumor development and it is highly expressed in many human tumors, and also in 40-80 % of patients with non-small cell lung cancer (NSCLC) (Cohen 2001;Maramotti et al 2012). NSE is a glycolitic enzyme that provides information to cancer course and treatment outcome of small cell lung carcinoma (SCLC) (Fu et al 2012), and CEA is a glycoprotein involved in cell adhesion, and it is the most widely investigated tumor biomarker in various tumors such as colorectal, stomach, pancreas, liver, ovarian, breast, prostate, thyroid, bladder, kidney, and lung (Qu et al 2013;Grunnet and Sorensen 2012).…”

Section: Introductionmentioning

confidence: 99%

Stochastic sensors based on maltodextrins for screening of whole blood for neuron specific enolase, carcinoembryonic antigen and epidermal growth factor receptor

Comnea-Stancu

Staden

et al. 2015

Microsyst Technol

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Bayley and Cremer 2001;Coulter 1953). By monitoring the ionic current modulations induced by the passage of analytes of interest through the nanopore at a fixed applied potential, the concentration of the analyte can be obtained by the frequency of occurrence (1/t on ) of the recorded blockage events, while the mean residence time (t off ) of the analyte allows to determine its identity (Zhao et al. 2008). In nanopore sensing, each analyte produces a characteristic signature (t off ), and this allows several analytes to be quantitated simultaneously van Staden and Moldoveanu 2014a, b).Maltodextrins are nanostructured materials with native channels due to their helix structure. Thus they were considered as materials for designing stochastic sensors proposed for the screening of three biomarkers: neuron specific enolase (NSE), carcinoembryonic antigen (CEA) and epidermal growth factor receptor (EGFR/HER-1). Maltodextrins ( Fig. 1) are carbohydrates derived from maize starch and are a group of oligosaccharides (long chainpolysaccharides) composed of glucose, with dextrose equivalent (DE) less than 20. Dextrose equivalent is a measure of reducing power of starch-derived polysaccharides/oligosaccharides compared with d-glucose on a dry-weight basis: the higher the DE, the greater the extent of starch hydrolysis. They are obtained by acidic and/or enzymatic hydrolysis of corn starch, with subsequent drying to make free flowing powders. They usually contain glucose, depending on the degree and method of hydrolysis. Therefore, maltodextrins are also called glucose polymers (Al-Khatib et al. 2001;Preis et al. 2014;Wang and Wang 2000). Along the time, maltodextrins have been used as chiral selectors for separation of the enantiomers of chiral drugs by capillary electrophoresis (Watanabe et al. 1999;Fakhari et al. 2013;D'Hulst and Verbeke 1992), for the design of enantioselective, potentiometric membrane electrodes (EPMEs) Abstract Stochastic sensors based on maltodextrins with different dextrose equivalent were proposed for the assay of three lung cancer biomarkers: neuron specific enolase, carcinoembryonic antigen and epidermal growth factor receptor. The two sensors proposed can determine simultaneously NSE, CEA and HER-1 in whole blood samples (qualitative and quantitative), with recoveries higher than 97.00 %, and low RSD (%), lower than 0.1 %. This screening test may serve for fast and early detection of lung cancer.

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Soluble epidermal growth factor receptor isoforms in non-small cell lung cancer tissue and in blood

Cited by 19 publications

References 23 publications

Epidermal growth factor receptor detection in serum and saliva as a diagnostic and prognostic tool in oral cancer

Epidermal growth factor receptor detection in serum and saliva as a diagnostic and prognostic tool in oral cancer

A Holistic In Silico Approach to Find Novel Inhibitors for Erbb1 and Erbb2 Kinases

Stochastic sensors based on maltodextrins for screening of whole blood for neuron specific enolase, carcinoembryonic antigen and epidermal growth factor receptor

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