Literature DB >> 10022607

Nuclear matrix proteins specific for subtypes of human hematopoietic cells.

C Gerner1, G Sauermann.   

Abstract

Nuclear matrices were prepared from isolated subtypes of human hematopoietic cells and from cultured leukemia cells. The nuclear matrix proteins were analyzed by high-resolution two-dimensional gel electrophoresis and computer-assisted image analysis. While more than 200 protein spots were shared among the cells, about 50 distinct spots were found characteristic for individual cells or groups of related cells. This allowed to differentiate between hematopoietic cells and nonhematopoietic cells, lymphocytes and myeloid cells, monocytes, neutrophils, and promyelocytic leukemia cells. B and T lymphocytes could not be differentiated. Myeloid cells with their polymorph nuclei were characterized by the presence of 13 and by the absence of seven distinct spots, as well as by low concentrations of nuclear lamins and of heterogeneous nuclear ribonucleoproteins. Neutrophils with multilobular nuclei displayed six additional spots, while lacking 18 nuclear matrix protein spots. The nuclear matrix of proliferating cells showed three distinct spots in addition to proliferating cell nuclear antigen, increased concentrations of numatrin (B23), and heterogeneous nuclear ribonucleoproteins. The described cell-specific nuclear matrix proteins may represent new markers for hematopoietic cells.

Entities:  

Mesh:

Substances:

Year:  1999        PMID: 10022607

Source DB:  PubMed          Journal:  J Cell Biochem        ISSN: 0730-2312            Impact factor:   4.429


  6 in total

1.  Lamins regulate cell trafficking and lineage maturation of adult human hematopoietic cells.

Authors:  Jae-Won Shin; Kyle R Spinler; Joe Swift; Joel A Chasis; Narla Mohandas; Dennis E Discher
Journal:  Proc Natl Acad Sci U S A       Date:  2013-11-04       Impact factor: 11.205

2.  Label-free mass spectrometry exploits dozens of detected peptides to quantify lamins in wildtype and knockdown cells.

Authors:  Joe Swift; Takamasa Harada; Amnon Buxboim; Jae-Won Shin; Hsin-Yao Tang; David W Speicher; Dennis E Discher
Journal:  Nucleus       Date:  2013-12-06       Impact factor: 4.197

3.  Regulation of Metnase's TIR binding activity by its binding partner, Pso4.

Authors:  Brian D Beck; Sung S Lee; Robert Hromas; Suk-Hee Lee
Journal:  Arch Biochem Biophys       Date:  2010-04-20       Impact factor: 4.013

4.  Transformation resistance in a premature aging disorder identifies a tumor-protective function of BRD4.

Authors:  Patricia Fernandez; Paola Scaffidi; Elke Markert; Ji-Hyeon Lee; Sushil Rane; Tom Misteli
Journal:  Cell Rep       Date:  2014-10-02       Impact factor: 9.423

5.  Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair.

Authors:  Brian D Beck; Su-Jung Park; Young-Ju Lee; Yaritzabel Roman; Robert A Hromas; Suk-Hee Lee
Journal:  J Biol Chem       Date:  2008-02-08       Impact factor: 5.157

6.  Proteome signatures of inflammatory activated primary human peripheral blood mononuclear cells.

Authors:  Verena J Haudek-Prinz; Philip Klepeisz; Astrid Slany; Johannes Griss; Anastasia Meshcheryakova; Verena Paulitschke; Goran Mitulovic; Johannes Stöckl; Christopher Gerner
Journal:  J Proteomics       Date:  2012-07-16       Impact factor: 4.044

  6 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.