Proteomic Fingerprints for Potential Application to Early Diagnosis of Severe Acute Respiratory Syndrome

Kang, Xiaojian; Xu, Yang; Wu, Xiaoyi; Liang, Yong; Wang, Chen; Guo, Junhua; Wang, Yajie; Chen, Maohua; Wu, Der-Min; Wang, Youchun; Bi, Shengli; Qiu, Yan; Lu, Ping; Cheng, Jing; Bai, Xia; Hu, Lina; Gao, Xing; Liu, Jingzhong; Wang, Yiping; Song, Yingzhao; Zhang, Liqun; Suo, Fengshuang; Chen, Tongyan; Huang, Zeyu; Zhao, Yunzhuan; Liang, Hong; Pan, Chunqin; Tang, Hong

doi:10.1373/clinchem.2004.032458

Cited by 59 publications

(45 citation statements)

References 25 publications

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“…Previous work has illustrated that AEDs are lifesaving, cost-effective, and easy to use by trained and untrained people. 9,[23][24][25][26]27,28 But, a nearby AED that cannot be located quickly might as well not be there at all. AED registration requirements vary by region, however, and a specific agency is not tasked with tracking and maintaining AED locations and use.…”

Section: Number Of Zipcodesmentioning

confidence: 99%

A Crowdsourcing Innovation Challenge to Locate and Map Automated External Defibrillators

Merchant

Asch

Hershey

et al. 2013

Circ: Cardiovascular Quality and Outcomes

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Section: Number Of Zipcodesmentioning

confidence: 99%

A Crowdsourcing Innovation Challenge to Locate and Map Automated External Defibrillators

Merchant

Asch

Hershey

et al. 2013

Circ: Cardiovascular Quality and Outcomes

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“…A related technology, surface-enhanced laser desorption/ ionization time-of-flight mass spectrometry (SELDI-TOF), combined with computational methodologies, has also been used to determine protein profiles (Solassol et al, 2006). Numerous studies have already shown that this methodology can be used to uncover proteomic expression patterns linked with cancer, and some expression patterns have shown high promises in the detection of early-stage cancers (Petricoin and Liotta, 2004;Kang et al, 2005;Kozak et al, 2005;Jacot et al, 2008).…”

Section: Introductionmentioning

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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“…hydrophobic or hydrophilic mass spectrometer targets) to bind groups of proteins from biological samples and generate distinct mass spectra containing hundreds of peaks (4,5). These so-called proteomic patterns entered mainstream proteomics with the publication of a Lancet study in 2002 (6), which was quickly followed by a significant number of research studies (7)(8)(9)(10)(11)) and reviews (12)(13)(14)(15) describing proteomic patterns capable of discriminating between disease (e.g. ovarian cancer, prostate cancer, etc.)…”

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confidence: 99%

Population Proteomics

Nedelkov

Kiernan

Niederkofler

et al. 2006

Molecular & Cellular Proteomics

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This review outlines the concept of population proteomics and its implication in the discovery and validation of cancer-specific protein modulations. Population proteomics is an applied subdiscipline of proteomics engaging in the investigation of human proteins across and within populations to define and better understand protein diversity. Population proteomics focuses on interrogation of specific proteins from large number of individuals, utilizing top-down, targeted affinity mass spectrometry approaches to probe protein modifications. Deglycosylation, sequence truncations, side-chain residue modifications, and other modifications have been reported for myriad of proteins, yet little is know about their incidence rate in the general population. Such information can be gathered via population proteomics and would greatly aid the biomarker discovery efforts. Discovery of novel protein modifications is also expected from such large scale population proteomics, expanding the protein knowledge database. In regard to cancer protein biomarkers, their validation via population proteomics-based approaches is advantageous as mass spectrometry detection is used both in the discovery and validation process, which is essential for the detection of those structurally modified protein biomarkers. Molecular & Cellular Proteomics 5: 1811-1818, 2006.In the past 5 years proteomics and its subdiscipline clinical proteomics (1-3) have taken a leading role in the discovery of new and improved cancer biomarkers. In its inception, clinical proteomics was an application of high end MS tools for evaluation of proteomic differences in the proteomes between healthy and cancer-bearing individuals. The tools were mainly based on the SELDI technology and utilization of wide specificity surfaces (e.g. hydrophobic or hydrophilic mass spectrometer targets) to bind groups of proteins from biological samples and generate distinct mass spectra containing hundreds of peaks (4, 5). These so-called proteomic patterns entered mainstream proteomics with the publication of a Lancet study in 2002 (6), which was quickly followed by a significant number of research studies (7-11) and reviews (12-15) describing proteomic patterns capable of discriminating between disease (e.g. ovarian cancer, prostate cancer, etc.) and healthy cohorts with relatively high sensitivity and specificity. However, critical assessment of those results quickly followed, outlining significant shortcomings and uncertainties in regard to the reproducibility of the findings, identity of the proteins behind the pattern peaks, and validation of the results (16 -23). Interlaboratory SELDI experiments performed recently alleviated some of the reproducibility concerns (24, 25). Furthermore, current research efforts have led to identification of several proteins behind the discriminating patterns peaks, including serum amyloid A (26), vitamin D-binding protein (27), and apolipoprotein A-II (28), which were identified as potential biomarkers for prostate cancer; haptoglobin (29), apolipopro...

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Proteomic Fingerprints for Potential Application to Early Diagnosis of Severe Acute Respiratory Syndrome

Cited by 59 publications

References 25 publications

A Crowdsourcing Innovation Challenge to Locate and Map Automated External Defibrillators

A Crowdsourcing Innovation Challenge to Locate and Map Automated External Defibrillators

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

Population Proteomics

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