Analysis of activation and function of PI-3K and MEK-ERK signal transduction in human granulocytes

1997 ◽  
Vol 56 (1-3) ◽  
pp. 209
Author(s):  
P Coffer
Keyword(s):  
Signal Transduction ◽  
Human Granulocytes ◽  
And Function

Analysis of activation and function of PI-3K and MEK-ERK signal transduction in human granulocytes

1997 ◽  
Vol 56 ◽  
pp. 209
Author(s):  
P.J. Coffer ◽  
R. Schweizer ◽  
T. Malkoe ◽  
J. Raaljmakers ◽  
J.-W. Lammers ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Human Granulocytes ◽  
And Function

scholarly journals A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction.

1994 ◽  
Vol 14 (11) ◽  
pp. 7404-7413 ◽  
Author(s):  
S Takaki ◽  
H Kanazawa ◽  
M Shiiba ◽  
K Takatsu
Keyword(s):  
Signal Transduction ◽  
Protein Tyrosine Kinase ◽  
Cytoplasmic Domain ◽  
Beta Chain ◽  
Cytoplasmic Domains ◽  
Interleukin 5 ◽  
Alpha Chain ◽  
Gm Csf ◽  
Response Expression ◽  
And Function

Interleukin-5 (IL-5) regulates the production and function of B cells, eosinophils, and basophils. The IL-5 receptor (IL-5R) consists of two distinct membrane proteins, alpha and beta. The alpha chain (IL-5R alpha) is specific to IL-5. The beta chain is the common beta chain (beta c) of receptors for IL-3 and granulocyte-macrophage colony-stimulating factor (GM-CSF). The cytoplasmic domains of both alpha and beta chains are essential for signal transduction. In this study, we generated cDNAs of IL-5R alpha having various mutations in their cytoplasmic domains and examined the function of these mutants by expressing them in IL-3-dependent FDC-P1 cells. The membrane-proximal proline-rich sequence of the cytoplasmic domain of IL-5R alpha, which is conserved among the alpha chains of IL-5R, IL-3R, and GM-CSF receptor (GM-CSFR), was found to be essential for the IL-5-induced proliferative response, expression of nuclear proto-oncogenes such as c-jun, c-fos, and c-myc, and tyrosine phosphorylation of cellular proteins including JAK2 protein-tyrosine kinase. In addition, analysis using chimeric receptors which consist of the extracellular domain of IL-5R alpha and the cytoplasmic domain of beta c suggested that dimerization of the cytoplasmic domain of beta c may be an important step in activating the IL-5R complex and transducing intracellular growth signals.

scholarly journals Mechanism and function of signal transduction by the Wnt/β-catenin and Wnt/Ca2+ pathways

Oncogene ◽  
1999 ◽  
Vol 18 (55) ◽  
pp. 7860-7872 ◽  
Author(s):  
Jeffrey R Miller ◽  
Anne M Hocking ◽  
Jeffrey D Brown ◽  
Randall T Moon
Keyword(s):  
Signal Transduction ◽  
And Function

Enzymatic Synthesis of Glycosphingolipids: A Review

Synthesis ◽  
2021 ◽  
Author(s):  
Qingjiang Li ◽  
Zhongwu Guo
Keyword(s):  
Signal Transduction ◽  
Enzymatic Synthesis ◽  
Biological Activities ◽  
Cell Interaction ◽  
Glycosidic Linkage ◽  
The Past ◽  
Biological Studies ◽  
Hydrophobic Lipid ◽  
Synthetic Methodologies ◽  
And Function

Glycosphingolipids (GSLs) are the major vertebrate glycolipids, which contain two distinctive moieties, a glycan and a ceramide, stitched together by a β-glycosidic linkage. The hydrophobic lipid chains of ceramide can insert into the cell membrane to form “lipid rafts” and anchor the hydrophilic glycan onto the cell surface to generate microdomains and function as signaling molecules. GSLs mediate signal transduction, cell interaction, and many other biological activities, and are also related to many diseases. To meet the need of biological studies, chemists have developed various synthetic methodologies to access GSLs. Among them, the application of enzymes to GSL synthesis has witnessed significant advancements in the past decades. This review summarizes briefly the history and progress of enzymatic GSL synthesis.

scholarly journals Influence of High Pressure on the Dimerization of ToxR, a Protein Involved in Bacterial Signal Transduction

2008 ◽  
Vol 74 (24) ◽  
pp. 7821-7823 ◽  
Author(s):  
Kai Linke ◽  
Nagarajan Periasamy ◽  
Matthias Ehrmann ◽  
Roland Winter ◽  
Rudi F. Vogel
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
High Pressure ◽  
Structure And Function ◽  
Transmembrane Segments ◽  
Bacterial Signal Transduction ◽  
Reporter Strains ◽  
And Function ◽  
First Time

ABSTRACT High hydrostatic pressure (HHP) is suggested to influence the structure and function of membranes and/or integrated proteins. We demonstrate for the first time HHP-induced dimer dissociation of membrane proteins in vivo with Vibrio cholerae ToxR variants in Escherichia coli reporter strains carrying ctx::lacZ fusions. Dimerization ceased at 20 to 50 MPa depending on the nature of the transmembrane segments rather than on changes in the ToxR lipid bilayer environment.

scholarly journals Integrin β4 as a Potential Diagnostic and Therapeutic Tumor Marker

Biomolecules ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 1197
Author(s):  
Haoyu Yang ◽  
Zixuan Xu ◽  
Yuqian Peng ◽  
Jiali Wang ◽  
Yang Xiang
Keyword(s):  
Signal Transduction ◽  
Tumor Marker ◽  
Tumor Invasion ◽  
Epithelial Mesenchymal Transition ◽  
Vital Role ◽  
Structure And Function ◽  
Mesenchymal Transition ◽  
Tumor Tissues ◽  
Integrin Β4 ◽  
And Function

Integrin β4 (ITGβ4) is a class of transmembrane adhesion molecules composed of hemidesmosomes (HDs). Its unique long intracellular domain provides intricate signal transduction functions. These signal transduction effects are especially prominent in tumors. Many recent studies have shown that integrin β4 is differentially expressed in various tumors, and it plays a vital role in tumor invasion, proliferation, epithelial–mesenchymal transition, and angiogenesis. Therefore, we categorize the research related to integrin β4, starting from its structure and function in tumor tissues, and provide a basic description. Based on its structure and function, we believe that integrin β4 can be used as a tumor marker. In clinical practice, it is described as a diagnostic marker for the targeted treatment of cancer and will be helpful in the clinical diagnosis and treatment of tumors.

scholarly journals The Significance of Calcium in Photosynthesis

2019 ◽  
Vol 20 (6) ◽  
pp. 1353 ◽  
Author(s):  
Quan Wang ◽  
Sha Yang ◽  
Shubo Wan ◽  
Xinguo Li
Keyword(s):  
Signal Transduction ◽  
Binding Sites ◽  
Current Knowledge ◽  
Structure And Function ◽  
Biochemical Reactions ◽  
Chloroplast Proteins ◽  
Secondary Messenger ◽  
And Function ◽  
The Relationship ◽  
Physiological And Biochemical

As a secondary messenger, calcium participates in various physiological and biochemical reactions in plants. Photosynthesis is the most extensive biosynthesis process on Earth. To date, researchers have found that some chloroplast proteins have Ca2+-binding sites, and the structure and function of some of these proteins have been discussed in detail. Although the roles of Ca2+ signal transduction related to photosynthesis have been discussed, the relationship between calcium and photosynthesis is seldom systematically summarized. In this review, we provide an overview of current knowledge of calcium’s role in photosynthesis.

scholarly journals Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli

Microbiology ◽  
2010 ◽  
Vol 156 (10) ◽  
pp. 2920-2932 ◽  
Author(s):  
Goran Jovanovic ◽  
Christoph Engl ◽  
Antony J. Mayhew ◽  
Patricia C. Burrows ◽  
Martin Buck
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
Protein Interactions ◽  
Leucine Zipper ◽  
Negative Control ◽  
Stress Conditions ◽  
Bacterial Cells ◽  
Protein Protein Interactions ◽  
Regulatory Complex ◽  
And Function

The phage-shock-protein (Psp) response maintains the proton-motive force (pmf) under extracytoplasmic stress conditions that impair the inner membrane (IM) in bacterial cells. In Escherichia coli transcription of the pspABCDE and pspG genes requires activation of σ 54-RNA polymerase by the enhancer-binding protein PspF. A regulatory network comprising PspF–A–C–B–ArcB controls psp expression. One key regulatory point is the negative control of PspF imposed by its binding to PspA. It has been proposed that under stress conditions, the IM-bound sensors PspB and PspC receive and transduce the signal(s) to PspA via protein–protein interactions, resulting in the release of the PspA–PspF inhibitory complex and the consequent induction of psp. In this work we demonstrate that PspB self-associates and interacts with PspC via putative IM regions. We present evidence suggesting that PspC has two topologies and that conserved residue G48 and the putative leucine zipper motif are determinants required for PspA interaction and signal transduction upon stress. We also establish that PspC directly interacts with the effector PspG, and show that PspG self-associates. These results are discussed in the context of formation and function of the Psp regulatory complex.

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