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Comparative proteomic analysis of secreted proteins from nasopharyngeal carcinoma-associated stromal fibroblasts and normal fibroblasts.

ABSTRACT: Since the concept of the secretome (ensemble of proteins secreted and/or shed from cells) was proposed, it has become an attractive and challenging proteomic technology in recent years. However, secretome analysis still faces some difficulties mainly related to sample collection and preparation. In the present study, we established a reliable method for extracting secreted proteins by ultrafiltration centrifugation and conducting secretomic analysis. Accumulating evidence suggests that carcinoma-associated stromal fibroblasts (CAFs) play an important role in cancer initiation and progression. To investigate the expression patterns of secreted proteins from fibroblasts and to identify the secreted proteins involved in nasopharyngeal carcinoma (NPC) carcinogenesis, we conducted comparative secretome analysis between CAFs and normal fibroblasts. After two-dimensional gel electrophoresis (2-D PAGE), 11 significant spots were differentially expressed and identified by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS). These proteins may take part in the regulation of the tumor micro-environment through different processes. The expression level of galectin-1 in the CAF supernatant was also determined by ELISA. This study provides useful information and new clues for the further understanding of the regulatory mechanisms of CAFs in the NPC microenvironment.

SUBMITTER: Ge S

PROVIDER: S-EPMC3438594 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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Comparative proteomic analysis of secreted proteins from nasopharyngeal carcinoma-associated stromal fibroblasts and normal fibroblasts.

Ge Shenglei S Mao Yitao Y Yi Yan Y Xie Dinghua D Chen Zhuchu Z Xiao Zhiqiang Z

Experimental and therapeutic medicine 20120213 5

Since the concept of the secretome (ensemble of proteins secreted and/or shed from cells) was proposed, it has become an attractive and challenging proteomic technology in recent years. However, secretome analysis still faces some difficulties mainly related to sample collection and preparation. In the present study, we established a reliable method for extracting secreted proteins by ultrafiltration centrifugation and conducting secretomic analysis. Accumulating evidence suggests that carcinoma ...[more]

PMID: 22969981

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Project description:BackgroundThe anaerobic Gram-positive bacterium Propionibacterium acnes is a human skin commensal that resides preferentially within sebaceous follicles; however, it also exhibits many traits of an opportunistic pathogen, playing roles in a variety of inflammatory diseases such as acne vulgaris. To date, the underlying disease-causing mechanisms remain ill-defined and knowledge of P. acnes virulence factors remains scarce. Here, we identified proteins secreted during anaerobic cultivation of a range of skin and clinical P. acnes isolates, spanning the four known phylogenetic groups.ResultsCulture supernatant proteins of P. acnes were separated by two-dimensional electrophoresis (2-DE) and all Coomassie-stained spots were subsequently identified by MALDI mass spectrometry (MALDI-MS). A set of 20 proteins was secreted in the mid-exponential growth phase by the majority of strains tested. Functional annotation revealed that many of these common proteins possess degrading activities, including glycoside hydrolases with similarities to endoglycoceramidase, β-N-acetylglucosaminidase and muramidase; esterases such as lysophospholipase and triacylglycerol lipase; and several proteases. Other secreted factors included Christie-Atkins-Munch-Petersen (CAMP) factors, glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and several hypothetical proteins, a few of which are unique to P. acnes. Strain-specific differences were apparent, mostly in the secretion of putative adhesins, whose genes exhibit variable phase variation-like sequence signatures.ConclusionsOur proteomic investigations have revealed that the P. acnes secretome harbors several proteins likely to play a role in host-tissue degradation and inflammation. Despite a large overlap between the secretomes of all four P. acnes phylotypes, distinct differences between predicted host-tissue interacting proteins were identified, providing potential insight into the differential virulence properties of P. acnes isolates. Thus, our data presents a rich resource for guiding much-needed investigations on P. acnes virulence factors and host interacting properties.

Dataset Information

Comparative proteomic analysis of secreted proteins from nasopharyngeal carcinoma-associated stromal fibroblasts and normal fibroblasts.

Publications

Comparative proteomic analysis of secreted proteins from nasopharyngeal carcinoma-associated stromal fibroblasts and normal fibroblasts.

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