Global Profiling of Surface Plasma Membrane Proteome of Oviductal Epithelial Cells

Šoštarić, Edita; Georgiou, A. S.; Wong, Chi Huey; Watson, P. F.; Holt, William V.; Fazeli, Alireza

doi:10.1021/pr060366w

Cited by 55 publications

(40 citation statements)

References 44 publications

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“…13,18,21 However, our previous work, 37 together with the successful implementation of a similar approach for the selective enrichment of ICAT-conjugated cysteine-containing peptides, 26 revealed that protein identification and quantification based on the biotinylated peptides are reliable. SILAC with [ 13 C 6 , 15 N 2 ]-L-lysine will render each lysine residue in the proteins from WM-266-4 cells being replaced with a heavy lysine, which results in a mass increase of 8.01 Da.…”

Section: General Strategy For the Comparative Studies Of Cell Surfacementioning

confidence: 97%

Quantitative Analysis of Surface Plasma Membrane Proteins of Primary and Metastatic Melanoma Cells

Qiu

Wang

2008

J. Proteome Res.

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Plasma membrane proteins play critical roles in cell-to-cell recognition, signal transduction and material transport. Because of their accessibility, membrane proteins constitute the major targets for protein-based drugs. Here, we described an approach, which included stable isotope labeling by amino acids in cell culture (SILAC), cell surface biotinylation, affinity peptide purification and LC-MS/MS for the identification and quantification of cell surface membrane proteins. We applied the strategy for the quantitative analysis of membrane proteins expressed by a pair of human melanoma cell lines, WM-115 and WM-266-4, which were derived initially from the primary and metastatic tumor sites of the same individual. We were able to identify more than 100 membrane and membrane-associated proteins from these two cell lines, including cell surface histones. We further confirmed the surface localization of histone H2B and three other proteins by immunocytochemical analysis with confocal microscopy. The contamination from cytoplasmic and other nonmembrane-related sources is greatly reduced by using cell surface biotinylation and affinity purification of biotinylated peptides. We also quantified the relative expression of 62 identified proteins in the two types of melanoma cells. The application to quantitative analysis of membrane proteins of primary and metastatic melanoma cells revealed great potential of the method in the comprehensive identification of tumor progression markers as well as in the discovery of new protein-based therapeutic targets.

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Section: General Strategy For the Comparative Studies Of Cell Surfacementioning

confidence: 97%

Quantitative Analysis of Surface Plasma Membrane Proteins of Primary and Metastatic Melanoma Cells

Qiu

Wang

2008

J. Proteome Res.

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“…The global profiling of oviductal surface membrane proteome by an MS-based approach has led to the identification of more than 270 proteins including APN and various members of the heat-shock protein family (Sostaric et al, 2006). The major GNA-binding proteins of the OAMF, LAMP-1 and 2 as well as ORP150, however, are not listed.…”

Section: Galanthus Nivalis Agglutinin-binding Glycoproteins Of the Ovmentioning

confidence: 99%

Glycobiology of fertilization in the pig

Töpfer‐Petersen¹,

Ekhlasi-Hundrieser²,

Tsolova³

2008

Int. J. Dev. Biol.

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By adopting internal fertilization, the meeting of both gametes -the sperm and the egg -and thus the highly coordinated sequence of interactions leading to fertilization, occur in the female reproductive tract. In mammals, the oviduct has been shown to translate the requirements of the female, coordinating sperm activation (capacitation) and sperm transport with the arrival of the ovulated egg. A hierarchy of carbohydrate-based interactions accompanies these events ranging from the binding of uncapacitated sperm to the oviductal epithelium (establishment of the female sperm reservoir), to the primary and secondary binding processes contributing to gamete recognition and sperm penetration of the oocyte zona pellucida. The current perspective will focus on the carbohydrate-recognition systems in the binding events during fertilization in the pig. The roles of the major carbohydrate-binding proteins, the spermadhesins and the acrosomal serine proteinase, pro/acrosin are discussed under consideration of recent structural data. The glycans and the glycoproteins of the porcine oviduct with a focus on the candidate sperm receptors as well as the zona pellucida N-glycans of prepuberal pigs have been characterized by a mass spectrometric approach. Furthermore, some preliminary data supporting the hypothesis that the zona pellucida has to undergo a maturation process during oocyte development are presented. KEY WORDS: gamete interaction, spermadhesin, acrosin, zona pellucida, glycoprotein, glycan A short review of mammalian fertilizationThe fertilization of an egg by a sperm is the fundamental event in life, as it culminates in the creation of a new individual. In mammals, the meeting of the fertilizing competent sperm and the ovulated egg is the beginning of a highly coordinated sequence of cellular interactions between the haploid gametes, which leads to the formation of the diploid zygote and initiates embryonic development.The first contact between sperm and egg takes place at the outer surface of the surrounding extracellular matrix of the egg, the zona pellucida (ZP). By binding to distinct oligosaccharides of the ZP glycoproteins, the fertilizing sperm recognizes the egg. Upon anchoring the sperm to the egg through the ZP carbohydrates the signaling cascade leading to acrosomal exocytosis of the sperm is activated allowing the sperm to pass through the zona pellucida. The acrosome-reacted sperm in the end interacts and fuses with the egg plasma membrane, which in turn enables the egg to complete meiosis, to initiate the mechanisms to prevent Int.

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“…Biotinylation of proteins at the cell surface with an impermeable reagent followed by specific purification of these proteins using streptavidin has successfully been used for the enrichment and identification of surface proteins (21)(22)(23)(24). The high avidity binding of biotin to streptavidin greatly enhances membrane protein purification, a challenging feat because of the low abundance of membrane proteins in total cellular extracts.…”

mentioning

confidence: 99%

NGALR Is Overexpressed and Regulated by Hypomethylation in Esophageal Squamous Cell Carcinoma

Cui¹,

Shen

et al. 2008

Clinical Cancer Research

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The identification of surface proteins on the plasma membrane of pathogens is of fundamental importance in understanding host-pathogen interactions. Surface proteins of the extracellular parasite Trichomonas are implicated in the initial adherence to mucosal tissue and are likely to play a critical role in the long term survival of this pathogen in the urogenital tract. In this study, we used cell surface biotinylation and multidimensional protein identification technology to identify the surface proteome of six strains of Trichomonas vaginalis with differing adherence capacities to vaginal epithelial cells. A combined total of 411 proteins were identified, and of these, 11 were found to be more abundant in adherent strains relative to less adherent parasites. The mRNA levels of five differentially expressed proteins selected for quantitative RT-PCR analysis mirrored their observed protein levels, confirming their up-regulation in highly adherent strains. As proof of principle and to investigate a possible role in pathogenesis for differentially expressed proteins, gain of function experiments were performed using two novel proteins that were among the most highly expressed surface proteins in adherent strains. Overexpression of either of these proteins, TVAG_244130 or TVAG_166850, in a relatively non-adherent strain increased attachment of transfected parasites to vaginal epithelial cells ϳ2.2-fold. These data support a role in adhesion for these abundant surface proteins. Our analyses demonstrate that comprehensive profiling of the cell surface proteome of different parasite strains is an effective approach to identify potential new adhesion factors as well as other surface molecules that may participate in establishing and maintaining infection by this extracellular pathogen. Molecular & Cellular Proteomics 9:1554 -1566, 2010.

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Global Profiling of Surface Plasma Membrane Proteome of Oviductal Epithelial Cells

Cited by 55 publications

References 44 publications

Quantitative Analysis of Surface Plasma Membrane Proteins of Primary and Metastatic Melanoma Cells

Quantitative Analysis of Surface Plasma Membrane Proteins of Primary and Metastatic Melanoma Cells

Glycobiology of fertilization in the pig

NGALR Is Overexpressed and Regulated by Hypomethylation in Esophageal Squamous Cell Carcinoma

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