scholarly journals Gfi1:Green Fluorescent Protein Knock-in Mutant Reveals Differential Expression and Autoregulation of the Growth Factor Independence 1 (Gfi1) Gene during Lymphocyte Development

2004 ◽  
Vol 279 (39) ◽  
pp. 40906-40917 ◽  
Author(s):  
Raif Yücel ◽  
Christian Kosan ◽  
Florian Heyd ◽  
Tarik Möröy
Keyword(s):  
Green Fluorescent Protein ◽  
Growth Factor ◽  
Differential Expression ◽  
Fluorescent Protein ◽  
Lymphocyte Development ◽  
Green Fluorescent

Green fluorescent protein-transgenic mice: immune functions and their application to studies of lymphocyte development

2000 ◽  
Vol 70 (3) ◽  
pp. 165-171 ◽  
Author(s):  
Naoto Kawakami ◽  
Naoki Sakane ◽  
Fumiko Nishizawa ◽  
Mutsumi Iwao ◽  
So-ichiro Fukada ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Transgenic Mice ◽  
Fluorescent Protein ◽  
Lymphocyte Development ◽  
Immune Functions ◽  
Green Fluorescent

scholarly journals Trafficking of TrkA-Green Fluorescent Protein Chimerae during Nerve Growth Factor-induced Differentiation

2002 ◽  
Vol 278 (10) ◽  
pp. 8706-8716 ◽  
Author(s):  
Jérôme Jullien ◽  
Vincent Guili ◽  
Edmund A. Derrington ◽  
Jean-Luc Darlix ◽  
Louis F. Reichardt ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Fluorescent Protein ◽  
Induced Differentiation ◽  
Nerve Growth ◽  
Green Fluorescent

scholarly journals The family of hepatoma-derived growth factor proteins: characterization of a new member HRP-4 and classification of its subfamilies

2002 ◽  
Vol 366 (2) ◽  
pp. 491-500 ◽  
Author(s):  
Frank DIETZ ◽  
Sebastian FRANKEN ◽  
Kenya YOSHIDA ◽  
Hideji NAKAMURA ◽  
Joachim KAPPLER ◽  
...  
Keyword(s):  
Amino Acids ◽  
Green Fluorescent Protein ◽  
Growth Factor ◽  
Fluorescent Protein ◽  
Chondroitin Sulphate ◽  
Human Fibroblasts ◽  
Heparan Sulphate ◽  
Factor Activity ◽  
Hek 293 ◽  
Green Fluorescent

Hepatoma-derived growth factor (HDGF)-related proteins (HRPs) comprise a family of polypeptides named after HDGF, which was identified by its mitogenic activity towards fibroblasts. In the present study, we describe a hitherto unknown HRP, termed HRP-4. The cDNA of bovine HRP-4 (bHRP-4) predicts a polypeptide of 235 amino acids. Northern- and Western-blot analyses of various bovine tissues demonstrated that HRP-4 is only expressed in the testis. Recombinantly produced bHRP-4 and murine HDGF (mHDGF) histidine-tagged polypeptides display growth-factor activity for cultured primary human fibroblasts at an optimum concentration of 1ng/ml in serum-free medium. The growth-factor activity declines with increasing concentrations to reach background levels at 1μg/ml. The expression of the fusion proteins, bHRP-4–green fluorescent protein and mHDGF–green fluorescent protein, in HEK-293 cells demonstrates nuclear localization of the proteins. bHRP-4 and mHDGF bind to the glycosaminoglycans heparin and heparan sulphate, but not to chondroitin sulphate. Affinity constants determined for these interactions are between 6 and 42nM. Comparison of the bHRP-4 amino acid sequence with HRP-1–3 and p52/75/lens epithelium-derived growth factor (LEDGF) shows that these proteins share a conserved N-terminal part of 91 amino acids but have C-termini of different lengths and charge. This demonstrates the modular structure of these proteins and allows its classification into three groups based on charge, size and sequence comparison. HRP-4, HRP-1 and HDGF are small acidic proteins, HRP-3 is a small basic protein, and HRP-2 and p52/75/LEDGF are larger basic proteins.

scholarly journals Kinetic Analysis of Smad Nucleocytoplasmic Shuttling Reveals a Mechanism for Transforming Growth Factor β-Dependent Nuclear Accumulation of Smads

2005 ◽  
Vol 25 (22) ◽  
pp. 9845-9858 ◽  
Author(s):  
Bernhard Schmierer ◽  
Caroline S. Hill
Keyword(s):  
Green Fluorescent Protein ◽  
Growth Factor ◽  
Nuclear Export ◽  
Transforming Growth Factor ◽  
Fluorescent Protein ◽  
Transforming Growth Factor Β ◽  
Nuclear Accumulation ◽  
Nucleocytoplasmic Shuttling ◽  
Green Fluorescent

ABSTRACT Upon transforming growth factor β (TGF-β) stimulation, Smads accumulate in the nucleus, where they regulate gene expression. Using fluorescence perturbation experiments on Smad2 and Smad4 fused to either enhanced green fluorescent protein or photoactivatable green fluorescent protein, we have studied the kinetics of Smad nucleocytoplasmic shuttling in a quantitative manner in vivo. We have obtained rate constants for import and export of Smad2 and show that the cytoplasmic localization of Smad2 in uninduced cells reflects its nuclear export being more rapid than import. We find that TGF-β-induced nuclear accumulation of Smad2 is caused by a pronounced drop in the export rate of Smad2 from the nucleus, which is associated with a strong decrease in nuclear mobility of Smad2 and Smad4. TGF-β-induced nuclear accumulation involves neither a release from cytoplasmic retention nor an increase in Smad2 import rate. Hence, TGF-β-dependent nuclear accumulation of Smad2 is caused exclusively by selective nuclear trapping of phosphorylated, complexed Smad2. The proposed mechanism reconciles signal-dependent nuclear accumulation of Smad2 with its continuous nucleocytoplasmic cycling properties.

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