Serum protein kinase Cα as a diagnostic biomarker of cancers

Kang, Jeong Hun; Mori, Takeshi; Kitazaki, Hirotaro; Niidome, Takuro; Takayama, K.; Nakanishi, Yoichi; Katayama, Yoshiki

doi:10.3233/cbm-130340

Cited by 14 publications

(20 citation statements)

References 22 publications

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“…However, overexpression of PKC-α is directly related to the progression of cancer, and therefore, it can be used as a diagnostic or therapeutic tool in various cell lines (50,51). PKC-α is involved in proliferation of bladder cancer cell lines 5637 and T24.…”

Section: Tumorigenicitymentioning

confidence: 99%

Protein kinase C-α and the regulation of diverse cell responses

Singh

Kumar

Gautam

et al. 2017

Biomolecular Concepts

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Protein kinase C (PKC) comprises a family of lipid-sensitive enzymes that have been involved in a broad range of cellular functions. PKC-α is a member of classical PKC with ubiquitous expression and different cellular localization. This unique PKC isoform is activated by various signals which evoke lipid hydrolysis, after activation it interacts with various adapter proteins and is localized to specific cellular compartments where it is devised to work. The universal expression and activation by various stimuli make it a perfect player in uncountable cellular functions including differentiation, proliferation, apoptosis, cellular transformation, motility, adhesion and so on. However, these functions are not intrinsic properties of PKC-α, but depend on cell types and conditions. The activities of PKC-α are managed by the various pharmacological activators/inhibitors and antisense oligonucleotides. The aim of this review is to elaborate the structural feature, and provide an insight into the mechanism of PKC-α activation and regulation of its key biological functions in different cellular compartments to develop an effective pharmacological approach to regulate the PKC-α signal array.

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Section: Tumorigenicitymentioning

confidence: 99%

Protein kinase C-α and the regulation of diverse cell responses

Singh

Kumar

Gautam

et al. 2017

Biomolecular Concepts

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“…Human serum contains various protein kinases in addition to PKA, [17][18][19] and these kinases could interfere with the specific measurement of sPKA activity in blood samples.…”

Section: Optimization Of On-chip Spka Activity Assay Using Fluorescenmentioning

confidence: 99%

“…While useful, these methods are limited in quantifying PKA activity in mixed samples such as human sera because different kinases can phosphorylate substrates [17][18][19] and thus interfere with specific sPKA activity measurement in blood samples. Therefore, there is a need to develop highly sensitive, specific, and easily manipulatable assays for assessing sPKA activity.…”

Section: Introductionmentioning

confidence: 99%

A peptide array-based serological protein kinase A activity assay and its application in cancer diagnosis

Kong

Jung

Jeon

et al. 2015

Analyst

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Protein kinase A (PKA) plays a crucial role in several biological processes; however, there is no assay with sufficient sensitivity and specificity to determine serological PKA (sPKA) activity. Here we present an on-chip activity assay that employs cysteine-modified kemptide arrays to determine specific sPKA activity in human sera that eliminates the potential contributions of other kinases with a protein kinase peptide inhibitor. The sensitivity of the on-chip sPKA activity assay was greatly enhanced by Triton X-100, with a 0.01 U mL(-1) detection limit. sPKA activity was determined by subtracting nonspecific sPK activity from total sPK activity. Our assay provided greater sensitivity and specificity and more accurate area under the curve values for gastric cancer compared to the total sPK activity assay. sPKA activities in human sera from patients with hepatic (n = 30), gastric (n = 30), lung (n = 30), and colorectal (n = 30) cancers were significantly higher than those in controls (n = 30, p < 10(-4)), but no significant difference in sPKA activities between normal and inflammation groups was observed. These results demonstrate that the on-chip assay accurately measures sPKA activity in human sera and that the sPKA activity may be a potential biomarker for cancer diagnosis.

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“…The hormone can be acetylated and exists therefore in multiple forms and these could be studied and relative ratios determined by MALDI profi ling following immunoprecipitation. In another study the phosphorylation status of a specifi c protein (a target for protein kinase C) was studied from serum samples from mice with and without tumours utilising MALDI analysis and shown to provide diagnostic potential in relation to the ratio of phosphorylated and unphosphorylated peptide [ 41 ]. As well as studying natural protein modifi cations by MALDI profi ling, the formation of organophosphorus adducts of human butyrylcholinesterase was also undertaken by MALDI analysis [ 37 ].…”

Section: Specifi C Protein Analysismentioning

confidence: 99%

MALDI Profiling and Applications in Medicine

Dudley

2014

Advances in Experimental Medicine and Biology

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Matrix-assisted laser desorption ionisation (MALDI) mass spectrometry allows for the rapid profiling of different biomolecular species from both biofluids and tissues. Whilst originally focussed upon the analysis of intact proteins and peptides, MALDI mass spectrometry has found further applications in lipidomic analysis, genotyping, micro-organism identification, biomarker discovery and metabolomics. The combining of multiple profiles data from differing locations across a sample, furthermore, allows for spatial distribution of biomolecules to be established utilising imaging MALDI analysis. This chapter discusses the MALDI process, its usual applications in the field of protein identification via peptide mass fingerprinting before focusing upon advances in the application of the profiling potential of MALDI mass spectrometry and its various applications in biomedicine.

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Serum protein kinase Cα as a diagnostic biomarker of cancers

Abstract: These results suggest that serum activated PKCα is a good biomarker applicable to cancer diagnosis.

Cited by 14 publications

References 22 publications

Protein kinase C-α and the regulation of diverse cell responses

Protein kinase C-α and the regulation of diverse cell responses

A peptide array-based serological protein kinase A activity assay and its application in cancer diagnosis

MALDI Profiling and Applications in Medicine

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