Human anticentromere antibodies: Distribution, characterization of antigens, and effect on microtubule organization

Cox, John V.; Schenk, Eric A.; Olmsted, J.B.

doi:10.1016/0092-8674(83)90236-2

Cited by 119 publications

(47 citation statements)

References 30 publications

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“…In contrast, recent publications have indicated that the kinetochore-specific determinants recognized by CREST sera are protein components of the nuclease-and salt-resistant nuclear matrix and chromosomal scaffold (7,8). Our data are in accord with the findings of Moroi et al However, we wish to note that we have worked only with nuclei, and that the procedures we have applied do not permit the isolation of nuclear matrix (1).…”

Section: Discussioncontrasting

confidence: 53%

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Kinetochore components recognized by human autoantibodies are present on mononucleosomes.

Palmer¹,

Margolis²

1985

Mol. Cell. Biol.

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We have developed a competitive enzyme-linked immunosorbent assay for solubilized kinetochore components, using human CREST (calcinosis, Raynaud's phenomenon, esophageal dysfunction, sclerodactyly, telangiectasia) scleroderma autoimmune antibodies specific for these kinetochore elements. Using this quantitative assay, we found interphase persistent or "pre-kinetochore" components in low-and moderately high-salt (375 mM salt) extracts of micrococcal nuclease-digested rat liver and chicken erythrocyte nuclei. The release of antigen activity from nuclei under these conditions has been correlated with loss of pre-kinetochore foci as determined by immunofluorescence microscopy. Combined biochemical and competition assay analysis of chicken erythrocyte nuclear extracts indicates that pre-kinetochore components are tightly bound to chromatin of mononucleosome size. The conclusions based on competition assay data are supported by a direct binding assay, which confirms that antigens recognized by CREST sera are present on chromatin. These results raise the possibility that the kinetochore-specific chromosomal antigen(s) we have detected substitutes for "standard" mononucleosome components, such as histone HI. Furthermore, they suggest approaches to the isolation of kinetochore-specific DNA sequences from higher eucaryotes.

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Section: Discussioncontrasting

confidence: 53%

“…Two recent publications have indicated that proteins are recognized by CREST sera on immunoblotting, but they have implicated different sets of polypeptides (7,8 …”

Section: Discussionmentioning

confidence: 99%

Kinetochore components recognized by human autoantibodies are present on mononucleosomes.

Palmer¹,

Margolis²

1985

Mol. Cell. Biol.

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“…The immunoglobulins in the immune serum were partially purified with ammonium sulfate precipitation (50%), dissolved in DPBS, extensively dialyzed against DPBS, and then passed through a GST-Sepharose column three times to absorb anti-GST antibody. The anti-MetAP2 antibody was affinity purified using the GST/MetAP2-(224 -478) fusion protein immobilized onto the nitrocellulose membrane (38).…”

Section: Construction Of Pgex Plasmids For Producing Glutathione S-trmentioning

confidence: 99%

Methionine Aminopeptidase 2 Is a New Target for the Metastasis-associated Protein, S100A4

Endo

Takenaga²,

Kuriyama

et al. 2002

Journal of Biological Chemistry

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S100A4 is an EF-hand type calcium-binding protein that regulates tumor metastasis and a variety of cellular processes via interaction with different target proteins.Here we report that S100A4 physically interacts with methionine aminopeptidase 2 (MetAP2), the primary target for potent angiogenesis inhibitors, fumagillin and ovalicin. Using a yeast two-hybrid screen, S100A4 was found to interact with the N-terminal half of MetAP2. In vitro pull-down assays showed that S100A4 associates with MetAP2 in a calcium-dependent manner. In addition, the binding site of S100A4 was found located within the region between amino acid residues 170 and 229 of MetAP2. In vivo interaction of S100A4 with MetAP2 was verified by co-immunoprecipitation analysis. Immunofluorescent staining revealed that S100A4 and MetAP2 were co-localized in both quiescent and basic fibroblast growth factor-treated murine endothelial MSS31 cells, in the latter of which a significant change of intracellular distribution of both proteins was observed. Although the binding of S100A4 did not affect the in vitro methionine aminopeptidase activity of MetAP2, the cytochemical observation suggests a possible involvement of S100A4 in the regulation of MetAP2 activity through changing its localization, thereby modulating the N-terminal methionine processing of nascent substrates. These results may offer an essential clue for understanding the functional role of S100A4 in regulating endothelial cell growth and tumor metastasis.

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“…This work is facilitated by the discovery that human autoantibodies from scleroderma CREST patients specifically recognize centromeres of metaphase chromosomes, as detected by indirect immunofluorescence (25). By using these anticentromere antibodies, a set of centromere-specific proteins from human and other mammalian cells has been identified (2,5). Although there are certain discrepancies among the different reports regarding the number and size of centromere proteins, at least one such protein appears to be consistently encountered (2,5,11,19,23,24,27,31).…”

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confidence: 99%

Purification of a yeast centromere-binding protein that is able to distinguish single base-pair mutations in its recognition site.

Cai¹,

Davis²

1989

Mol. Cell. Biol.

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A centromere-specific DNA-binding protein has been purified to homogeneity by a combination of conventional and sequence-affinity chromatography from the yeast Saccharomyces cerevisiae. This protein (designated CBP-I) has an apparent molecular weight of 16,000. It binds specifically to the CDEI (centromere DNA element I) region of yeast centromere DNA, as shown by the electrophoretic mobility retardation assay and DNase I protection analysis, but does not bind specifically to other regions of yeast centromere DNA such as CDEII and CDEIII. The relative binding affinity of purified CBP-I to five different point mutations of CDEI correlates directly with the previously determined ability of each point mutation to convey centromere function in a mitotic chromosome segregation assay

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Human anticentromere antibodies: Distribution, characterization of antigens, and effect on microtubule organization

Cited by 119 publications

References 30 publications

Kinetochore components recognized by human autoantibodies are present on mononucleosomes.

Kinetochore components recognized by human autoantibodies are present on mononucleosomes.

Methionine Aminopeptidase 2 Is a New Target for the Metastasis-associated Protein, S100A4

Purification of a yeast centromere-binding protein that is able to distinguish single base-pair mutations in its recognition site.

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