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Article ; Online: Over-Expression of RNA Processing, Heat Shock, and DNA Repair Proteins in Breast Tumor Compared to Normal Tissue.

Yen, Ten-Yang / Wong, Richard / Pizzo, Donald / Thein, Moe / Macher, Bruce A / Timpe, Leslie C

2020 , Page(s) e2000044

Abstract: This study identifies the main changes in protein expression in human breast tumors compared to normal breast tissue. Malignant tumors (32) and normal breast tissue samples (23), from formaldehyde-fixed, paraffin-embedded specimens are subjected to ... ...

Abstract	This study identifies the main changes in protein expression in human breast tumors compared to normal breast tissue. Malignant tumors (32) and normal breast tissue samples (23), from formaldehyde-fixed, paraffin-embedded specimens are subjected to discovery proteomics using liquid chromatography/tandem mass spectrometry, with spectral counts for quantitation. The dataset contains 1406 proteins. Differential expression is measured using a method that takes advantage of estimates of the percentage of tumor on a slide. This analysis shows that the major classes of proteins over-expressed by tumors are RNA-binding, heat shock and DNA repair proteins. RNA-binding proteins, including heterogeneous nuclear ribonucleoproteins (HNRNPs), SR splice factors (SRSF) and elongation factors form the largest group. Comparison with results from another study demonstrates that the RNA-binding proteins are associated specifically with malignant transformation, rather than with cell proliferation. HNRNP and SRSF proteins help define splice sites in normal cells. Their over-expression may dysregulate splicing, which in turn has the potential to promote malignant transformation.
Language	English
Publishing date	2020-07-14
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2032093-0
ISSN	1615-9861 ; 1615-9853
ISSN (online)	1615-9861
ISSN	1615-9853
DOI	10.1002/pmic.202000044
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Article ; Online: Glycoproteins in Claudin-Low Breast Cancer Cell Lines Have a Unique Expression Profile.

Yen, Ten-Yang / Bowen, Spencer / Yen, Roger / Piryatinska, Alexandra / Macher, Bruce A / Timpe, Leslie C

Journal of proteome research

2017 Volume 16, Issue 4, Page(s) 1391–1400

Abstract: Claudin proteins are components of epithelial tight junctions; a subtype of breast cancer has been defined by the reduced expression of mRNA for claudins and other genes. Here, we characterize the expression of glycoproteins in breast cell lines for the ... ...

Abstract	Claudin proteins are components of epithelial tight junctions; a subtype of breast cancer has been defined by the reduced expression of mRNA for claudins and other genes. Here, we characterize the expression of glycoproteins in breast cell lines for the claudin-low subtype using liquid chromatography/tandem mass spectrometry. Unsupervised clustering techniques reveal a group of claudin-low cell lines that is distinct from nonmalignant, basal, and luminal lines. The claudin-low cell lines express F11R, EPCAM, and other proteins at very low levels, whereas CD44 is expressed at a high level. Comparison of mRNA expression to glycoprotein expression shows modest correlation; the best agreement occurs when the mRNA expression level is lowest and little or no protein is detected. These findings from cell lines are compared to those for tumor samples by the Clinical Proteomic Tumor Analysis Consortium (CPTAC). The CPTAC samples contain a group low in CLDN3. The samples low in CLDN3 proteins share many differentially expressed glycoproteins with the claudin-low cell lines. In contrast to the situation for cell lines or patient samples classified as claudin-low by RNA expression, however, most of the tumor samples low in CLDN3 protein express the estrogen receptor or HER2. These tumor samples express CD44 protein at low rather than high levels. There is no correlation between CLDN3 gene expression and protein expression in these CPTAC samples; hence, the claudin-low subtype defined by gene expression is not the same group of tumors as that defined by low expression of CLDN3 protein.
MeSH term(s)	Biomarkers, Tumor/biosynthesis ; Biomarkers, Tumor/genetics ; Breast Neoplasms/genetics ; Breast Neoplasms/pathology ; Cell Line, Tumor ; Claudin-3/biosynthesis ; Claudin-3/genetics ; Female ; Gene Expression Regulation, Neoplastic ; Glycoproteins/biosynthesis ; Glycoproteins/genetics ; Humans ; Hyaluronan Receptors/biosynthesis ; Hyaluronan Receptors/genetics ; Mass Spectrometry/methods ; Prognosis ; Proteomics ; Receptor, ErbB-2/biosynthesis ; Receptor, ErbB-2/genetics
Chemical Substances	Biomarkers, Tumor ; CD44 protein, human ; CLDN3 protein, human ; Claudin-3 ; Glycoproteins ; Hyaluronan Receptors ; ERBB2 protein, human (EC 2.7.10.1) ; Receptor, ErbB-2 (EC 2.7.10.1)
Language	English
Publishing date	2017-04-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.6b00470
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Article: Proteins at membrane surfaces-a review of approaches.

Macher, Bruce A / Yen, Ten-Yang

Molecular bioSystems

2007 Volume 3, Issue 10, Page(s) 705–713

Abstract: Membrane proteins are critical for normal cellular differentiation and function, and alterations in these proteins often leads to cell dysfunction and disease. Membrane proteomics aims to identify the membrane protein constituents, their ... ...

Abstract	Membrane proteins are critical for normal cellular differentiation and function, and alterations in these proteins often leads to cell dysfunction and disease. Membrane proteomics aims to identify the membrane protein constituents, their posttranslational modifications, protein-protein interactions, and dynamics. Efforts to identify membrane proteins and elucidate their dynamics have been plagued by the challenges presented by studying water insoluble proteins that are distributed among a range of membranes in a cell and often occur at a relatively low abundance. This brief review presents a summary of the literature related to membrane proteomics with an emphasis on efforts to develop effective protocols for the enrichment of membrane proteins, particularly those located in the plasma membrane.
MeSH term(s)	Amino Acid Sequence ; Biotin ; Chromatography, Affinity ; Detergents ; Electrophoresis, Gel, Two-Dimensional ; Lectins ; Membrane Proteins/chemistry ; Membrane Proteins/isolation & purification ; Models, Molecular ; Molecular Sequence Data ; Polysaccharides/chemistry ; Proteomics ; Solubility ; Solvents ; Tandem Mass Spectrometry
Chemical Substances	Detergents ; Lectins ; Membrane Proteins ; Polysaccharides ; Solvents ; Biotin (6SO6U10H04)
Language	English
Publishing date	2007-10
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	2188635-0
ISSN	1742-2051 ; 1742-206X
ISSN (online)	1742-2051
ISSN	1742-206X
DOI	10.1039/b708581h
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: The Galalpha1,3Galbeta1,4GlcNAc-R (alpha-Gal) epitope: a carbohydrate of unique evolution and clinical relevance.

Macher, Bruce A / Galili, Uri

Biochimica et biophysica acta

2007 Volume 1780, Issue 2, Page(s) 75–88

Abstract: In 1985, we reported that a naturally occurring human antibody (anti-Gal), produced as the most abundant antibody (1% of immunoglobulins) throughout the life of all individuals, recognizes a carbohydrate epitope Galalpha1-3Galbeta1-4GlcNAc-R (the alpha- ... ...

Abstract	In 1985, we reported that a naturally occurring human antibody (anti-Gal), produced as the most abundant antibody (1% of immunoglobulins) throughout the life of all individuals, recognizes a carbohydrate epitope Galalpha1-3Galbeta1-4GlcNAc-R (the alpha-gal epitope). Since that time, an extensive literature has developed on discoveries related to the alpha-gal epitope and the anti-Gal antibody, including the barrier they form in xenotransplantation and their reciprocity in mammalian evolution. This review covers these topics and new avenues of clinical importance related to this unique antigen/antibody system (alpha-gal epitope/anti-Gal) in improving the efficacy of viral vaccines and in immunotherapy against cancer.
MeSH term(s)	Animals ; Cancer Vaccines/immunology ; Evolution, Molecular ; Galactosyltransferases/genetics ; Galactosyltransferases/metabolism ; Humans ; Immunoglobulin G/blood ; Immunoglobulin G/immunology ; Substrate Specificity ; Transplantation, Heterologous ; Trisaccharides/immunology ; Trisaccharides/metabolism ; Viral Vaccines/immunology
Chemical Substances	Cancer Vaccines ; Immunoglobulin G ; Trisaccharides ; Viral Vaccines ; alpha-galactosyl epitope ; Galactosyltransferases (EC 2.4.1.-) ; N-acetyllactosaminide alpha-1,3-galactosyltransferase (EC 2.4.1.87)
Language	English
Publishing date	2007-11-22
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2007.11.003
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Article: Determination of glycosylation sites and disulfide bond structures using LC/ESI-MS/MS analysis.

Yen, Ten-Yang / Macher, Bruce A

Methods in enzymology

2006 Volume 415, Page(s) 103–113

Abstract: Significant progress has been made in discovering and cloning a host of proteins, including a range of glycoproteins. The availability of their predicted amino acid sequences provides useful information, including potential N-linked glycosylation sites. ... ...

Abstract	Significant progress has been made in discovering and cloning a host of proteins, including a range of glycoproteins. The availability of their predicted amino acid sequences provides useful information, including potential N-linked glycosylation sites. However, only a limited number of protein structures have been solved, and very little is known about the structures of membrane proteins. One of the important structural elements of a protein is its disulfide bonds. These covalent bonds place conformational constraints on the overall protein structure, and thus, their identification provides important structural information. A second important posttranslational modification found in proteins is N-linked glycosylation. Although potential sites of N-linked glycosylation can be predicted from a protein's primary sequence based on the presence of N-X-S/T sequences, not all of the predicted sites will be glycosylated. Therefore, N-linked glycosylation sites must be located by structural analysis. We have developed a simple and sensitive method for determining the presence of free cysteine (Cys) residues and disulfide-bonded Cys residues, as well as the N-linked glycosylation sites in glycoproteins by liquid chromatography/electrospray ionization-tandem mass spectrometry (LC/ESI-MS/MS) in combination with protein database searching using the programs Sequest and Mascot. The details of our method are described in this chapter.
MeSH term(s)	Chromatography, Liquid/methods ; Cysteine/chemistry ; Disulfides ; Glycosylation ; Peptides/chemistry ; Peptides/genetics ; Spectrometry, Mass, Electrospray Ionization/methods
Chemical Substances	Disulfides ; Peptides ; Cysteine (K848JZ4886)
Language	English
Publishing date	2006
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ISSN	0076-6879
ISSN	0076-6879
DOI	10.1016/S0076-6879(06)15007-7
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Article: Glycoproteins in Claudin-Low Breast Cancer Cell Lines Have a Unique Expression Profile

Yen, Ten-Yang / Bowen Spencer / Yen Roger / Piryatinska Alexandra / Macher Bruce A / Timpe Leslie C

Journal of Proteome Research. 2017 Apr. 07, v. 16, no. 4

2017

Abstract	Claudin proteins are components of epithelial tight junctions; a subtype of breast cancer has been defined by the reduced expression of mRNA for claudins and other genes. Here, we characterize the expression of glycoproteins in breast cell lines for the claudin-low subtype using liquid chromatography/tandem mass spectrometry. Unsupervised clustering techniques reveal a group of claudin-low cell lines that is distinct from nonmalignant, basal, and luminal lines. The claudin-low cell lines express F11R, EPCAM, and other proteins at very low levels, whereas CD44 is expressed at a high level. Comparison of mRNA expression to glycoprotein expression shows modest correlation; the best agreement occurs when the mRNA expression level is lowest and little or no protein is detected. These findings from cell lines are compared to those for tumor samples by the Clinical Proteomic Tumor Analysis Consortium (CPTAC). The CPTAC samples contain a group low in CLDN3. The samples low in CLDN3 proteins share many differentially expressed glycoproteins with the claudin-low cell lines. In contrast to the situation for cell lines or patient samples classified as claudin-low by RNA expression, however, most of the tumor samples low in CLDN3 protein express the estrogen receptor or HER2. These tumor samples express CD44 protein at low rather than high levels. There is no correlation between CLDN3 gene expression and protein expression in these CPTAC samples; hence, the claudin-low subtype defined by gene expression is not the same group of tumors as that defined by low expression of CLDN3 protein.
Keywords	breast neoplasms ; breasts ; cell lines ; epithelium ; estrogen receptors ; gene expression ; genes ; glycoproteins ; liquid chromatography ; messenger RNA ; patients ; protein synthesis ; proteome ; proteomics ; tandem mass spectrometry ; tight junctions
Language	English
Dates of publication	2017-0407
Size	p. 1391-1400.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021%2Facs.jproteome.6b00470
Database	NAL-Catalogue (AGRICOLA)

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Article: Mining the Breast Cancer Proteome for Predictors of Drug Sensitivity.

Timpe, Leslie C / Li, Dian / Yen, Ten-Yang / Wong, Judi / Yen, Roger / Macher, Bruce A / Piryatinska, Alexandra

Journal of proteomics & bioinformatics

2015 Volume 8, Issue 9, Page(s) 204–211

Abstract: Approximately 20 drugs have been approved by the FDA for breast cancer treatment, yet predictive biomarkers are known for only a few of these. The identification of additional biomarkers would be useful both for drugs currently approved for breast cancer ...

Abstract	Approximately 20 drugs have been approved by the FDA for breast cancer treatment, yet predictive biomarkers are known for only a few of these. The identification of additional biomarkers would be useful both for drugs currently approved for breast cancer treatment and for new drug development. Using glycoprotein expression data collected via mass spectrometry, in conjunction with statistical models constructed by elastic net or lasso regression, we modeled quantitatively the responses of breast cancer cell lines to ~90 drugs. Lasso and elastic net regression identified HER2 as a predictor protein for lapatinib, afatinib, gefitinib and erlotinib, which target HER2 or the EGF receptor, thus providing an internal control for the approach. Two additional protein datasets and two RNA datasets were also tested as sources of predictor proteins for modeling drug sensitivity. Protein expression measured by mass spectrometry gave models with higher coefficients of determination than did reverse phase protein array (RPPA) predictor data. Further, cross validation of the elastic net models shows that, for many drugs, the prediction error is lower when the predictor data is from proteins, rather than mRNA expression measured on microarrays. Drugs that could be modeled effectively include PI3K inhibitors, Akt inhibitors, paclitaxel and docetaxel, rapamycin, everolimus and temsirolimus, gemcitabine and vinorelbine. Strikingly, this modeling approach with protein predictors often succeeds for drugs that are targeted agents, even when the nominal target is not in the dataset.
Language	English
Publishing date	2015-10-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	2451945-5
ISSN	0974-276X
ISSN	0974-276X
DOI	10.4172/jpb.1000370
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Article: Site-directed mutagenesis of glutamate 317 of bovine alpha-1,3Galactosyltransferase and its effect on enzyme activity: implications for reaction mechanism.

Molina, Patricia / Knegtel, Ronald M A / Macher, Bruce A

Biochimica et biophysica acta

2007 Volume 1770, Issue 8, Page(s) 1266–1273

Abstract: Bovine alpha1,3galactosyltransferase (alpha1,3GalT) transfers galactose from UDP-alpha-galactose to terminal beta-linked galactosyl residues with retention of configuration of the incoming galactose residue. The epitope synthesized has been shown to be ... ...

Abstract	Bovine alpha1,3galactosyltransferase (alpha1,3GalT) transfers galactose from UDP-alpha-galactose to terminal beta-linked galactosyl residues with retention of configuration of the incoming galactose residue. The epitope synthesized has been shown to be critical for xenotransplantation. According to a proposed double-displacement reaction mechanism, glutamate-317 (E317) is thought to be the catalytic nucleophile. The proposed catalytic role of E317 involves an initial nucleophilic attack with inversion of configuration and formation of a covalent sugar-enzyme intermediate between E317 and galactose from the donor substrate, followed by a second nucleophilic attack performed by the acceptor substrate with a second inversion of configuration. To determine whether E317 of alpha1,3GalT is critical for enzyme activity, site-directed mutagenesis was used to substitute alanine, aspartic acid, cysteine and histidine for E317. If the proposed reaction mechanism for the alpha1,3GalT enzyme is correct, E317D and E317H would produce active enzymes since they can act as nucleophiles. The non-conservative mutation E317A and conservative mutation E317C are predicted to produce inactive or very low activity enzymes since the E317A mutant cannot engage in a nucleophilic attack, and the E317C mutant would trap the galactose residue. The results obtained demonstrate that E317D and E317H mutants retained activity, albeit significantly less than the wild-type enzyme. Additionally, both E317A and E317C mutant also retained enzyme activity, suggesting that E317 is not the catalytic nucleophile proposed in the double-displacement mechanism. Therefore, either a different amino acid may act as the catalytic nucleophile or the reaction must proceed by a different mechanism.
MeSH term(s)	Animals ; Binding Sites ; Cattle ; Galactosyltransferases/genetics ; Galactosyltransferases/metabolism ; Glutamic Acid/genetics ; Kinetics ; Models, Molecular ; Mutagenesis, Site-Directed ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Substrate Specificity
Chemical Substances	Glutamic Acid (3KX376GY7L) ; Galactosyltransferases (EC 2.4.1.-)
Language	English
Publishing date	2007-08
Publishing country	Netherlands
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2007.04.012
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Article: Overcoming challenges and opening new opportunities in glycoproteomics.

Yen, Ten-Yang / Dutta, Sucharita M / Litsakos-Cheung, Christina / Corona, Alejandro A / Timpe, Leslie C / Macher, Bruce A

Biomolecules

2014 Volume 3, Issue 2, Page(s) 270–286

Abstract: Glycoproteomics has emerged as a prime area of interest within the field of proteomics because glycoproteins have been shown to function as biomarkers for disease and as promising therapeutic targets. A significant challenge in the study of glycoproteins ...

Abstract	Glycoproteomics has emerged as a prime area of interest within the field of proteomics because glycoproteins have been shown to function as biomarkers for disease and as promising therapeutic targets. A significant challenge in the study of glycoproteins is the fact that they are expressed in relatively low abundance in cells. In response, various enrichment methods have been developed to improve the detection of glycoproteins. One such method involves their capture via oxidation of their glycan chains and covalent attachment with hydrazide resins which, when catalyzed by PNGase F, release N-linked glycans and convert the glycosite Asn to Asp; this conversion is identifiable with LC/ESI-MS/MS as a corresponding increase of 0.984 Da in molecular weight. The present study builds on this body of work, providing evidence of three additional strategies that improve glycoprotein identification: (1) use of a high resolution mass spectrometer-the Q Exactive MS-which delivers 2-3 times more glycoprotein identifications than a low resolution MS; (2) optimization of instrument settings and database search parameters to reduce misidentification of N-linked glycopeptides to ~1 percent; and (3) labeling glycopeptides with (18)O during PNGase F treatment to locate N-linked glycosites within peptides containing multiple N-linked sequons.
Language	English
Publishing date	2014-04-18
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2701262-1
ISSN	2218-273X
ISSN	2218-273X
DOI	10.3390/biom3020270
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Article: Cell surface and secreted protein profiles of human thyroid cancer cell lines reveal distinct glycoprotein patterns.

Arcinas, Arthur / Yen, Ten-Yang / Kebebew, Electron / Macher, Bruce A

Journal of proteome research

2009 Volume 8, Issue 8, Page(s) 3958–3968

Abstract: Cell surface proteins have been shown to be effective therapeutic targets. In addition, shed forms of these proteins and secreted proteins can serve as biomarkers for diseases, including cancer. Thus, identification of cell surface and secreted proteins ... ...

Abstract	Cell surface proteins have been shown to be effective therapeutic targets. In addition, shed forms of these proteins and secreted proteins can serve as biomarkers for diseases, including cancer. Thus, identification of cell surface and secreted proteins has been a prime area of interest in the proteomics field. Most cell surface and secreted proteins are known to be glycosylated, and therefore, a proteomics strategy targeting these proteins was applied to obtain proteomic profiles from various thyroid cancer cell lines that represent the range of thyroid cancers of follicular cell origin. In this study, we oxidized the carbohydrates of secreted proteins and those on the cell surface with periodate and isolated them via covalent coupling to hydrazide resin. The glycoproteins obtained were identified from tryptic peptides and N-linked glycopeptides released from the hydrazide resin using two-dimensional liquid chromatography-tandem mass spectrometry in combination with the gas phase fractionation. Thyroid cancer cell lines derived from papillary thyroid cancer (TPC-1), follicular thyroid cancer (FTC-133), Hurthle cell carcinoma (XTC-1), and anaplastic thyroid cancer (ARO and DRO-1) were evaluated. An average of 150 glycoproteins were identified per cell line, of which more than 57% are known cell surface or secreted glycoproteins. The usefulness of the approach for identifying thyroid cancer associated biomarkers was validated by the identification of glycoproteins (e.g., CD44, galectin 3 and metalloproteinase inhibitor 1) that have been found to be useful markers for thyroid cancer. In addition to glycoproteins that are commonly expressed by all of the cell lines, we identified others that are only expressed in the more well-differentiated thyroid cancer cell lines (follicular, Hurthle cell and papillary), or by cell lines derived from undifferentiated tumors that are uniformly fatal forms of thyroid cancer (i.e., anaplastic). On the basis of the results obtained, a set of glycoprotein biomarker candidates for thyroid cancer is proposed.
MeSH term(s)	Biomarkers, Tumor/metabolism ; Cell Line, Tumor ; Electrophoresis, Gel, Two-Dimensional ; Glycoproteins/metabolism ; Glycosylation ; Humans ; Hydrazines/chemistry ; Membrane Proteins/metabolism ; Neoplasm Proteins/metabolism ; Peptide Fragments/metabolism ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/metabolism ; Periodic Acid/chemistry ; Proteomics/methods ; Reproducibility of Results ; Subcellular Fractions/metabolism ; Tandem Mass Spectrometry ; Thyroid Neoplasms/metabolism
Chemical Substances	Biomarkers, Tumor ; Glycoproteins ; Hydrazines ; Membrane Proteins ; Neoplasm Proteins ; Peptide Fragments ; Periodic Acid (10450-60-9) ; metaperiodate (B45A1BUM4Q) ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (EC 3.5.1.52)
Language	English
Publishing date	2009-06-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2078618-9
ISSN	1535-3893
ISSN	1535-3893
DOI	10.1021/pr900278c
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