Characterization of a subfamily of zinc finger genes expressed in human hematopoietic cell lines

1991 ◽  
Vol 5 (S1) ◽  
pp. 59-60
Author(s):  
M. Munaro ◽  
D. Petroni ◽  
M. Di Fazio ◽  
P. Comi ◽  
S. Ottolenghi
Keyword(s):  
Cell Lines ◽  
Zinc Finger ◽  
Hematopoietic Cell ◽  
Zinc Finger Genes ◽  
Hematopoietic Cell Lines

Utilization of human hematopoietic cell lines for the propagation and characterization of HBLV (human herpesvirus 6)

1988 ◽  
Vol 42 (5) ◽  
pp. 787-791 ◽  
Author(s):  
Dharam V. Ablashi ◽  
Paolo Lusso ◽  
Chia-Ling Hung ◽  
S. Zaki Salahuddin ◽  
Steven F. Josephs ◽  
...  
Keyword(s):  
Cell Lines ◽  
Human Herpesvirus ◽  
Hematopoietic Cell ◽  
Human Herpesvirus 6 ◽  
Herpesvirus 6 ◽  
Hematopoietic Cell Lines

Generation and Characterization of Human Hematopoietic Cell Lines Expressing Factor VIII

2002 ◽  
Vol 11 (4) ◽  
pp. 695-704 ◽  
Author(s):  
T. Tonn ◽  
C. Herder ◽  
S. Becker ◽  
E. Seifried ◽  
M. Grez
Keyword(s):  
Factor Viii ◽  
Cell Lines ◽  
Hematopoietic Cell ◽  
Hematopoietic Cell Lines

Malignant hematopoietic cell lines: In vitro models for the study of primary mediastinal B-cell lymphomas

2015 ◽  
Vol 39 (1) ◽  
pp. 18-29 ◽  
Author(s):  
Hans G. Drexler ◽  
Stefan Ehrentraut ◽  
Stefan Nagel ◽  
Sonja Eberth ◽  
Roderick A.F. MacLeod
Keyword(s):  
B Cell ◽  
Cell Lines ◽  
In Vitro Models ◽  
Hematopoietic Cell ◽  
B Cell Lymphomas ◽  
Hematopoietic Cell Lines

scholarly journals Collagen type VI in the human bone marrow microenvironment: a strong cytoadhesive component

Blood ◽  
1995 ◽  
Vol 86 (5) ◽  
pp. 1740-1748 ◽  
Author(s):  
G Klein ◽  
CA Muller ◽  
E Tillet ◽  
ML Chu ◽  
R Timpl
Keyword(s):  
Bone Marrow ◽  
Cell Lines ◽  
Triple Helix ◽  
Collagen Type ◽  
Hematopoietic Cell ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Collagen Vi ◽  
Collagen Type Vi ◽  
Hematopoietic Cell Lines

Collagen type VI, which forms characteristic microfibrillar structures, is assembled from three individual alpha(VI) chains that form a short triple helix and two adjacent globular domains. Expression of all three alpha (VI) collagen chains in the human bone marrow (BM) microenvironment could be detected by chain-specific antibodies in tissue sections and in the adherent stromal layer of long-term BM cultures. In functional studies, collagen type VI was shown to be a strong adhesive substrate for various hematopoietic cell lines and light-density BM mononuclear cells. The adhesive site within the molecule seems to be restricted to the triple helical domain of all three alpha (VI) chains, because individual alpha (VI) chains were not active in the attachment assays. Adhesion of the hematopoietic cell lines to collagen VI was dose-dependent and could be inhibited by heparin. Although the triple helix contains several RGD sequences, adhesion of the hematopoietic cell types to collagen VI could be blocked neither by RGD-containing peptides nor by a neutralizing antibody to the beta 1 integrin subunit. In combination with an antiadhesive substrate, the binding properties of collagen VI could be downregulated. These data suggest that this collagen type may play an important role in the adhesion of hematopoietic cells within the BM microenvironment.

scholarly journals Siderocalin/Lcn2/NGAL/24p3 Does Not Drive Apoptosis Through Gentisic Acid Mediated Iron Withdrawal in Hematopoietic Cell Lines

PLoS ONE ◽  
2012 ◽  
Vol 7 (8) ◽  
pp. e43696 ◽  
Author(s):  
Colin Correnti ◽  
Vera Richardson ◽  
Allyson K. Sia ◽  
Ashok D. Bandaranayake ◽  
Mario Ruiz ◽  
...  
Keyword(s):  
Cell Lines ◽  
Hematopoietic Cell ◽  
Gentisic Acid ◽  
Hematopoietic Cell Lines

Characterization of Spi-B, a transcription factor related to the putative oncoprotein Spi-1/PU.1

1992 ◽  
Vol 12 (10) ◽  
pp. 4297-4304 ◽  
Author(s):  
D Ray ◽  
R Bosselut ◽  
J Ghysdael ◽  
M G Mattei ◽  
A Tavitian ◽  
...  
Keyword(s):  
Dna Binding ◽  
Cell Lines ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
New Gene ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal ◽  
Hematopoietic Cell Lines

We have cloned a human cDNA from a new gene, spi-B, on the basis of its homology with the DNA-binding domain of the Spi-1/PU.1 putative oncogene product. spi-B codes for a protein of 262 amino acids presenting 43% overall identity with Spi-1. Its highly basic carboxy-terminal region exhibits 34% sequence identity with the DNA-binding domain of the Ets-1 protein. We showed that the Spi-B protein is able to bind the purine-rich sequence (PU box) recognized by Spi-1/PU.1 and to activate transcription of a reporter plasmid containing PU boxes. Chromosome in situ hybridization allowed us to map spi-B to the 19q13.3-19q13.4 region of the human genome. spi-B, like spi-1, was found to be expressed in various murine and human hematopoietic cell lines except T lymphoid cell lines.

Sign in / Sign up

Export Citation Format

Share Document