Proteomic analysis reveals successive aberrations in protein expression from healthy mucosa to invasive head and neck cancer

Roesch‐Ely, Mariana; Nees, Matthias; Karsai, Syrus; Ruess, Alexandra; Bogumil, Ralf; Warnken, Uwe; Schnölzer, Martina; Dietz, Andreas; Plinkert, Peter K.; Hofele, Christof; Bosch, Franz X.

doi:10.1038/sj.onc.1209770

Cited by 111 publications

(80 citation statements)

References 40 publications

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“…We found an up-regulated pattern of this protein in tonsillar cancer, a pattern that is well in line with previous publications, stating that this protein is up-regulated in tongue cancer [17]. In contrast, Roesch-Ely and coworkers published a down-regulation of S100A9 in HNSCC [21]. Melle et al investigated a series of head and neck tumors using a classical proteomic approach combined with protein-chip technology.…”

Section: Discussionsupporting

confidence: 69%

Proteomic analysis of protein expression in human tonsillar cancer differentially expressed proteins characterize human tonsillar cancer

Roblick¹,

Bader

Hammarstedt

et al. 2008

Acta Oncologica

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Section: Discussionsupporting

confidence: 69%

Proteomic analysis of protein expression in human tonsillar cancer differentially expressed proteins characterize human tonsillar cancer

Roblick¹,

Bader

Hammarstedt

et al. 2008

Acta Oncologica

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“…Transferrin has been identified by SELDI-TOF as a putative ovarian (Rai et al, 2002;Kozak et al, 2005), colon (Ward et al, 2006) and breast (Goncalves et al, 2006) cancer biomarker. a-and b-Hemoglobin have also been identified as putative markers for ovarian and head and neck cancer (Roesch-Ely et al, 2007). With this in mind, neither transferrin nor hemoglobin can serve as robust breast cancer biomarkers unless they are used in combination with additional validation studies.…”

Section: Discussionmentioning

confidence: 99%

“…From their m/z ratio, the fraction from which they were derived, the ProteinChip surface of capture, as well as data from previously performed serum profiling studies (Rai et al, 2002;Kozak et al, 2005;Goncalves et al, 2006;Ward et al, 2006;Roesch-Ely et al, 2007;Timms et al, 2007), it was possible to identify several other potential protein biomarkers present in the multiprotein index. Thus, the 15 120, 15 870 and 79235 Da proteins that were upregulated in the serum of DCIS patients were identified as a-and b-hemoglobin and transferrin, respectively.…”

Section: Peak Identificationmentioning

confidence: 99%

Serum protein signature may improve detection of ductal carcinoma in situ of the breast

et al. 2009

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Ductal carcinoma in situ (DCIS) of the breast is part of a spectrum of preinvasive lesions that originate within normal breast tissue and progress to invasive breast cancer. The detection of DCIS is important for the reduction of mortality from breast cancer, but the diagnosis of preinvasive breast tumors is hampered by the lack of an adequate detection method. To identify the changes in protein expression during the initial stage of tumorigenesis and to identify the presence of new DCIS markers, we analysed serum from 60 patients with breast cancer and 60 normal controls using mass spectrometry. A 23-protein index was generated that correctly distinguishes the DCIS and control groups with sensitivities and specificities in excess of 80% in two independent cohorts. Two candidate peptides were purified and identified as platelet factor 4 (PF-4) and complement C3a desArg anaphylatoxin (C3a desArg ) using liquid chromatography-tandem mass spectrometry (LC-MS/MS). In an independent serum set of 165 patients, PF-4 and C3a desArg were significantly upregulated in DCIS compared with non-cancerous controls, as validated using western blot and enzyme-linked immunosorbent assay. We conclude that our serum protein-based test, used in conjunction with image-based screening practices, could improve the sensitivity and specificity of breast cancer detection.

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“…Number of cases and spectra from colorectal tumors. proteins that have been found at the corresponding m/z values as described in previous studies (13,14,(23)(24)(25). Such protein peaks exhibited considerable variation amongst the different types of colorectal tissues.…”

Section: Variation Of Spot Histology In Human Colorectal Tumorsmentioning

confidence: 96%

Variability of in situ proteomic profiling and implications for study design in colorectal tumors

Shakhtour

et al. 2007

Int J Oncol

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Abstract. Knowledge of intrinsic tumor heterogeneity is vital for understanding of tumor progression mechanisms as well as for providing efficient treatments. In situ proteomic profiling of tumors is a powerful technology with potential to enhance our understanding of tumor biology, but sources of variability due to patient and tumor heterogeneity are poorly understood and are the topic of this investigation. Clarification of variability within case and between cases is also important for designing future studies. Direct protein profiling by matrixassisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) is a sensitive and powerful technology for obtaining hundreds of protein expression peaks from a thin tissue section. By combining robotic microspotting and laser capture microdissection with MALDI MS, we acquired multiple spectra per case to evaluate inter-and intra-case variability in human colorectal tumor and murine cecal carcinoma. We detected 256 peaks from 164 samples of 111 patients, which consisted of 55 normal colorectal mucosal samples, 24 adenomas, 71 primary carcinomas, and 14 hepatic metastases. In addition, we detected 291 peptide/protein peaks from 34 orthotopically transplanted murine cecal carcinomas and 14 hepatic metastases. In human colorectal samples, we observed that proteomic profiling in adenomas was more homogeneous across patients than in normal mucosa specimens (p=0.0008), but primary carcinoma exhibited greater heterogeneity than normal mucosa and adenomas (both p<0.0001). Murine cecal carcinomas were homogeneous within and between carcinomas, while their hepatic metastases tended toward greater intra-tumor differences (p<0.0001). Inter-and intra-case variability was approximately equal for many protein peaks. Acquiring up to 5 subsamples per case could reduce the total number of cases required, but further reduction from additional subsampling was modest unless intra-case variability comprises a greater proportion of total variation (e.g. >70%). In summary, this study characterizes intra-and inter-case variability of high-throughput protein expression in colorectal tumors, and provides guidance for the sample numbers required for in situ proteomic studies.

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Proteomic analysis reveals successive aberrations in protein expression from healthy mucosa to invasive head and neck cancer

Cited by 111 publications

References 40 publications

Proteomic analysis of protein expression in human tonsillar cancer differentially expressed proteins characterize human tonsillar cancer

Proteomic analysis of protein expression in human tonsillar cancer differentially expressed proteins characterize human tonsillar cancer

Serum protein signature may improve detection of ductal carcinoma in situ of the breast

Variability of in situ proteomic profiling and implications for study design in colorectal tumors

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