Advances in the quantification of protein microarrays

Pratsch, Katja; Wellhausen, Robert; Seitz, Harald

doi:10.1016/j.cbpa.2013.10.024

Cited by 17 publications

(6 citation statements)

References 28 publications

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“…Advantage of gel free attempts for analysis of mitochondrial proteome is improved detection of membrane proteins that are underrepresented in 2-DE analyses 60 . Microscale techniques that comprise protein extraction, fractionation and pro- 62,63 . The ability of microarrays for screening of multiple proteins is advantageous for detection of protein expression changes, protein-protein interactions, and biomarker discovery and validation 64 .…”

Section: Methods For Analysis Of Mitochondrial Proteomementioning

confidence: 99%

“…Analysis of intact proteins by microarrays instead of proteolytic digests can be advantageous for preservation of specific motifs but conjugation of sample with the tag necessary for subsequent detection or signal amplification may denature, damage, or mask the epitope 65 . Antibody cross-reactivity to non-target proteins can also decrease performance in antibody microarrays 62,63 . The potential for utilization of protein microarrays in analysis of renal mitochondria could be in high throughput monitoring of selected pathways by analysis of multiple, predefined set of proteins.…”

Section: Methods For Analysis Of Mitochondrial Proteomementioning

confidence: 99%

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Proteomic approaches to the study of renal mitochondria

Tůma¹,

Kuncová²,

Mareš³

et al. 2016

BIOMED PAP

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Background and Aims. Dysfunction of kidney mitochondria plays a critical role in the pathogenesis of a number of renal diseases. Proteomics represents an untargeted attempt to reveal the remodeling of mitochondrial proteins during disease. Combination of separation methods and mass spectrometry allows identification and quantitative analysis of mitochondrial proteins including protein complexes. The aim of this review is to summarize the methods and applications of proteomics to renal mitochondria. Methods. Using keywords "mitochondria", "kidney", "proteomics", scientific databases (PubMed and Web of knowledge) were searched from 2000 to August 2015 for articles describing methods and applications of proteomics to analysis of mitochondrial proteins in kidney. Included were publications on mitochondrial proteins in kidneys of humans and animal model in health and disease. Results and Conclusion. Proteomics of renal mitochondria has been/is mostly used in diabetes, hypertension, acidosis, nephrotoxicity and renal cancer. Integration of proteomics with other methods for examining protein activity is promising for insight into the role of renal mitochondria in pathological states. Several challenges were identified: selection of appropriate model organism, sensitivity of analytical methods and analysis of mitochondrial proteome in different renal zones/biopsies in the course of various kidney disorders.

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Section: Methods For Analysis Of Mitochondrial Proteomementioning

confidence: 99%

Section: Methods For Analysis Of Mitochondrial Proteomementioning

confidence: 99%

Proteomic approaches to the study of renal mitochondria

Tůma¹,

Kuncová²,

Mareš³

et al. 2016

BIOMED PAP

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show abstract

“…Various techniques are available for the quantification of proteins nowadays, the majority of which rely on the use of antibodies (e.g. ELISA, protein microarrays ). Quantitative immunoassays are widely used because of their accuracy and the fact that they can be implemented even in a basic laboratory setting due to their low cost and simplicity.…”

Section: Inferring Transcription Factor Regulatory Properties From Thmentioning

confidence: 99%

Transcription factor proteomics—Tools, applications, and challenges

Simicevic

Deplancke

2017

Proteomics

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Transcription factors (TFs) are a family of DNA-binding proteins whose gene regulatory capabilities are of vital importance in defining the molecular state of a cell. Despite their biological significance, our understanding of TF behavior and function is still limited. This is because we have so far mostly relied on gene expression data to approximate TF protein levels given that the latter information has been notoriously difficult to obtain due to the relatively low expression levels of many TFs. However, significant advances in mass spectrometry technologies combined with the development of sensitive methodologies aimed at detecting TFs are now allowing a transition from a predominantly qualitative to a quantitative protein landscape. Such a paradigm shift is expected to unravel dynamic aspects of TF function, potentially linking TF copy number fluctuations in cells with specific regulatory functions. This in turn may provide novel insights into the regulatory mechanisms underlying a wide range of fundamental and disease-related biological processes. In this review, we will present the latest advances in mass spectrometry-based TF proteomics and describe novel strategies tailored around the quantification of this important family of DNA-binding proteins.

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“…Among various micro-fabrication techniques, embossing [25][26][27][28][29] provide a simple, low-cost, and high-throughput method to replicate the microstructures of the mold into the polymer substrate. In recent years, devices and systems fabricated by hot embossing have demonstrated great potential for biomedical applications such as cell culture platform [30], DNA arrays [31], protein Shuttle vector between E. coli and P. aeruginosa [35] pEX18Tc Gene replacement vector; Tc r , sacB [36] microarrays [32], nanofluidic devices [33], and biosensors [34]. In the above applications, hot embossing is demonstrated to be a feasible technique to fabricate high precision and high quality patterns from nano to microscale.…”

mentioning

confidence: 99%

Localized fluorescence detection of carbenicillin resistance based on gelatinous substrate with micro-pyramid array structure

Zhang¹,

Jia-ju²,

Zheng³

et al. 2018

J. Micromech. Microeng.

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Recent research has shown that bacteria can complete information exchange with other groups via physical or chemical properties of signal molecules which is known as quorum sensing (QS). The communication of microorganism groups has a valuable function in regulating the physiological behavior of bacteria. In order to explore the cell to cell communication, we fabricated a gelatinous substrate with micrometer scale inverted pyramid array structure, which can confine a large population of bacteria for localized fluorescence detection of Escherichia Coli (E. Coli) under variable growing conditions. The fabricated substrate enables different kinds of bacteria’s segregation physically and communication chemically. A two-step embossing process was developed to replicate the inverted pyramid patterns from a silicon master to the gelatin substrate. The cell to cell communication was verified by the fluorescence detection of the E. Coli. According to the specific changes in quantity and the fluorescence intensity of E. Coli, we have demonstrated that Pseudomonas aeruginosa with different phenotypes suspended out of the matrix present different effects to the growth of E. Coli within the micrometer scale inverted pyramid.

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Advances in the quantification of protein microarrays

Cited by 17 publications

References 28 publications

Proteomic approaches to the study of renal mitochondria

Proteomic approaches to the study of renal mitochondria

Transcription factor proteomics—Tools, applications, and challenges

Localized fluorescence detection of carbenicillin resistance based on gelatinous substrate with micro-pyramid array structure

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