The human keratinocyte two‐dimensional gel protein database: Update 1993

Celis, Julio E.; Rasmussen, Hanne H.; Olsen, Eydfinnur; Madsen, Peder; Leffers, Henrik; Honoré, Bent; Dejgaard, Kurt; Gromov, Paul; Hoffmann, Hans Jürgen; Nielsen, Morten S.; Vassilev, Alex; Vintermyr, Olav Karsten; Hao, Junshan; Celis, Ariana; Basse, Bodil; Lauridsen, Jette B.; Ratz, Gitte P.; Andersen, Anders H.; Walbum, Else; Kjærgaard, Inge; Puype, Magda; Damme, Josef Van; Vandekerckhove, Joël

doi:10.1002/elps.11501401178

Cited by 75 publications

(43 citation statements)

References 92 publications

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“…Because COPI was purified to near homogeneity before two-dimensional gel analysis, it is unlikely that this is the result of a fortuitous cross-reactivity with a similarly sized group of unrelated proteins. This result is further confirmed by the finding of 3-4 ␤-COP immunoreactive species in two-dimensional gels of total human keratinocyte extracts (29).…”

Section: Fig 2 Two Dimensional Ief/sds-page Reveals Heterogeneity Osupporting

confidence: 67%

Biochemical Heterogeneity and Phosphorylation of Coatomer Subunits

Sheff¹,

Lowe²,

Kreis

et al. 1996

Journal of Biological Chemistry

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The coat protomer complex I (COPI) family of coat proteins are involved in the assembly of membrane-associated coats thought to mediate vesicular transport between the endoplasmic reticulum and the Golgi complex, between adjacent Golgi cisternae, and possibly in the endocytic pathway. We investigated whether this heterogeneity in the sites of COPI action might be reflected in biochemical heterogeneity of one or more COPI subunits. A simplified method was devised to purify the cytosolic COPI precursor complex, coatomer, from rat liver cytosol. The individual subunits were analyzed by high resolution two dimensional gel electrophoresis and mass spectroscopic analysis of tryptic peptides. Considerable charge heterogeneity was observed, particularly for the ␤-COP and ␦-COP subunits. The multiple species detected, however, did not appear to reflect the presence of distinct translation products but rather a significant degree of protein phosphorylation. The observed pI of ␤-COP was sensitive to alkaline phosphatase digestion. Moreover, isolation of coatomer from metabolically labeled tissue culture cells demonstrated directly that both ␤-COP and ␦-COP, but no other coatomer subunits, were serine-phosphorylated. COPI phosphorylation may regulate coatomer assembly, membrane recruitment, or the specificity of coatomerorganelle interaction.

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Section: Fig 2 Two Dimensional Ief/sds-page Reveals Heterogeneity Osupporting

confidence: 67%

Biochemical Heterogeneity and Phosphorylation of Coatomer Subunits

Sheff¹,

Lowe²,

Kreis

et al. 1996

Journal of Biological Chemistry

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“…Identification of known polypeptides and evaluation of expression level of TA01 and TA02 polypeptides Some human polypeptides were identified on the 2-DE gel by comparison of our 2-DE patterns and previously published 2-DE maps (Ochs et al, 1981;Garrels et al, 1989;Bhattacharya et al, 1990;Celis et al, 1992;Bjellqvist et al, 1994). Furthermore, coelectrophoresis of purified polypeptides and subcellular fractions, as well as samples characterized from other laboratories, was very useful for identification of human polypeptides.…”

Section: Methodsmentioning

confidence: 62%

Relationship between TA01 and TA02 polypeptides associated with lung adenocarcinoma and histocytological features

Hirano¹,

Fujioka²,

Franzén³

et al. 1997

Br J Cancer

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Summary TA01 (molecular weight 35.0 kDa, isoelectric point 5.45) and TA02 (molecular weight 35.0 kDa, isoelectric point 5.29) polypeptides were detected using two-dimensional polyacrylamide gel electrophoresis (2-DE). A previous study has shown that these polypeptides are distributed in primary adenocarcinomas and some large -cell carcinomas of the lung. However, various expression levels of TA01 and TA02 polypeptides were demonstrated in adenocarcinoma, while large-cell carcinoma expressed low levels. To evaluate the relationship between the expression of TA01 and TA02 polypeptides and the histocytological features of primary adenocarcinoma of the lung, these two polypeptides were analysed by 2-DE combined with a non-enzymatic sample preparation technique, and their expression levels were compared with the histocytological features of primary lung adenocarcinoma. Out of 57 primary lung adenocarcinoma cases, 46 cases (80.7%) and 52 cases (91.2%) expressed TA01 and TA02 polypeptides respectively. Furthermore, the expression levels of TA01 and TA02 polypeptides correlated with the degree of cellular atypia, structural atypia and histocytological differentiation of primary lung adenocarcinoma. On the other hand, these two polypeptides were not detected in adenocarcinoma of the lung, metastatic from the colon and mammary glands. High expression of TA01 and TA02 polypeptides reflected the differentiation of primary adenocarcinoma in the lung. These two polypeptides are valuable in determining the histocytological differentiation of primary lung adenocarcinoma as well as in distinguishing between primary and metastatic adenocarcinoma of the lung.Keywords: primary adenocarcinoma of the lung; histopathological differentiation; TA01 polypeptide; TA02 polypeptide; two-dimensional polyacrylamide gel electrophoresis Tumour markers can contribute to clinicopathological diagnosis, more accurate evaluation of biological malignancy of the tumour and selection of therapeutic strategy. Products of oncogenes and mutant tumour-suppressor genes are possible candidates for biological tumour markers. Also, histological differentiation antigens could be useful markers in cases of borderline histology.Although some tumour markers (e.g. CEA, CA 19-9 and TPA, etc.) are used in the clinical diagnosis of primary adenocarcinoma of the lung (Vincent et al, 1979;Latanche et al, 1985;Buccheri et al, 1988;Niklinski et al, 1995), there is no specific tumour marker for primary adenocarcinoma of the lung. At present, cell proliferation and products of oncogenes and tumour-suppressor genes in lung adenocarcinoma are attracting attention (M0rkve et al, 1992;Scagliotti et al, 1993;Ebina et al, 1994;Rachwal et al, 1995;Costa et al, 1996) Correspondence to: T Hirano Linnoila et al, 1992) and protein 1 (Barnard et al, 1992). There is a possibility that these polypeptides become specific tumour markers for primary adenocarcinoma of the lung. Such a marker might be useful to distinguish primary and metastatic adenocarcinoma of the lung.We also investigate...

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“…Two-dimensional gel electrophoresis was performed as described by Celis et al [1993], with some minor modifications. Samples were freezedried before solubilization in lysis buffer, and 1% (w/v) CHAPS was added to this lysis buffer and the first-dimension gel medium.…”

Section: Two-dimensional Gel Electrophoresismentioning

confidence: 99%

Major internal nuclear matrix proteins are common to different human cell types

et al. 1997

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The major internal nuclear matrix proteins are common to different human cell types Mattern, K.A.; Goethem, R.E.M.; de Jong, L.; van Driel, R. General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. AbstractThe nuclear matrix may be involved in the structural and functional organization of the cell nucleus. However, we still do not understand the molecular basis of the intranuclear fibrogranular network that is part of the nuclear matrix. We recently described a method to identify internal nuclear matrix proteins : J Cell Biochem 62:275-289], which was done by comparing two nuclear matrix preparations: one with and one without the internal structure by using quantitative two-dimensional gel electrophoresis. In the present study, we use the same approach to compare the nuclear matrix proteins of four different human cell types to investigate whether they have a similar internal nuclear matrix protein composition. Major nuclear matrix proteins present in all these cell types likely represent the base of the internal nuclear matrix. We demonstrate that the 25 most abundant internal nuclear matrix proteins are common to all four cell types. Together, these common proteins represent more than 75% of the total internal nuclear matrix protein mass in each cell type. This set of proteins includes B23 and most hnRNP proteins. The quantity of most of these proteins is very similar in the four cell types. The fact that the internal nuclear matrix consists mainly of hnRNP proteins, which may be involved in transcription, transport, and processing of hnRNA, supports the idea that the internal nuclear matrix is the result of these processes. J. Cell. Biochem. 65:42-52. r 1997 Wiley-Liss, Inc.

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The human keratinocyte two‐dimensional gel protein database: Update 1993

Cited by 75 publications

References 92 publications

Biochemical Heterogeneity and Phosphorylation of Coatomer Subunits

Biochemical Heterogeneity and Phosphorylation of Coatomer Subunits

Relationship between TA01 and TA02 polypeptides associated with lung adenocarcinoma and histocytological features

Major internal nuclear matrix proteins are common to different human cell types

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