scholarly journals Differences in Functional Consequences and Signal Transduction Induced by IL-3, IL-5, and Nerve Growth Factor in Human Basophils

2001 ◽  
Vol 167 (4) ◽  
pp. 2282-2291 ◽  
Author(s):  
Katsushi Miura ◽  
Sarbjit S. Saini ◽  
Gail Gauvreau ◽  
Donald W. MacGlashan
Keyword(s):  
Signal Transduction ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Nerve Growth ◽  
Functional Consequences ◽  
Human Basophils

scholarly journals Effect of nerve growth factor on the release of inflammatory mediators by mature human basophils

Blood ◽  
1992 ◽  
Vol 79 (10) ◽  
pp. 2662-2669 ◽  
Author(s):  
SC Bischoff ◽  
CA Dahinden
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Inflammatory Mediators ◽  
Ganglion Cells ◽  
Neuronal Cell ◽  
Cell Types ◽  
Cell Fractionation ◽  
Hematopoietic Growth Factors ◽  
Nerve Growth ◽  
Human Basophils

Abstract Nerve growth factor (NGF) is a neurotrophic cytokine known to regulate the survival and function of peripheral and central neuronal cells. Recently, the spectrum of action could be extended to non-neuronal cell types such as rat mast cells and human B lymphocytes. The present study shows that NGF affects the function of mature human basophils isolated from the peripheral blood of healthy donors. Both murine NGF 7S and recombinant human NGF beta enhance histamine release and strongly modulate the formation of lipid mediators by basophils in response to various stimuli. This priming effect of NGF on basophils occurs rapidly within 10 to 15 minutes of preincubation, is dose-dependent, and requires similarly low concentrations (1 to 40 pmol/L) of human NGF beta as the induction of neurite outgrowth in ganglion cells. Cell fractionation studies indicate that NGF acts directly on human basophils without an involvement of other cell types, suggesting the presence of high-affinity NGF receptors on basophils. NGF by itself (up to 4 nmol/L of human NGF beta) does not induce the release of inflammatory mediators directly. The effect of human NGF on basophil mediator release is similar to that of the hematopoietic growth factors interleukin-3, interleukin-5, and granulocyte-macrophage colony- stimulating factor. The present study further demonstrates that NGF acts as a pleiotropic cytokine at the interface between the nervous and the immune system, and that NGF may be involved in inflammatory processes and hypersensitivity reactions.

Nerve growth factor signal transduction in human B lymphocytes is mediated by gp140trk

1996 ◽  
Vol 26 (9) ◽  
pp. 1985-1992 ◽  
Author(s):  
Isaac Melamed ◽  
Colm A. Kelleher ◽  
Richard A. Franklin ◽  
Chaya Brodie ◽  
Barbara Hempstead ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
B Lymphocytes ◽  
Nerve Growth

Nerve growth factor signal transduction in mature pig oligodendrocytes

1997 ◽  
Vol 50 (5) ◽  
pp. 729-742 ◽  
Author(s):  
H.H. Althaus ◽  
R. Hempel ◽  
S. Kl�ppner ◽  
J. Engel ◽  
T. Schmidt-Schultz ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Nerve Growth

scholarly journals A branched signaling pathway for nerve growth factor is revealed by Src-, Ras-, and Raf-mediated gene inductions.

1993 ◽  
Vol 13 (6) ◽  
pp. 3146-3155 ◽  
Author(s):  
G D'Arcangelo ◽  
S Halegoua
Keyword(s):  
Signal Transduction ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Gene Induction ◽  
Signal Transduction Pathways ◽  
Specific Gene ◽  
Nerve Growth ◽  
Pc12 Cell Line ◽  
Ngf Receptor ◽  
Signaling Components

A myriad of gene induction events underlie nerve growth factor (NGF)-induced differentiation of PC12 cells. To dissect the signal transduction pathways which lead to NGF actions, we have assessed the relative roles of NGF receptor, Src, Ras, and Raf activities in mediating specific gene inductions. We have used the PC12 cell line as well as sublines which inducibly express activated forms of either Src, Ras, or Raf or a dominant inhibitory form of Ras (p21N17 Ras) to study the expression of multiple NGF-inducible mRNAs. The NGF induction of NGFI-A, transin, and VGF mRNAs was mimicked by activated forms of Src, Ras, or Raf and was blocked by p21N17 Ras. The NGF induction of SCG10 mRNA was mimicked only by activated Src and Ras and was blocked by p21N17 Ras, while the induction of Thy-1 mRNA was mimicked only by activated Src and was not blocked by p21N17 Ras. The NGF induction of mRNAs for two sodium channel types was neither mimicked by any activated oncoprotein nor blocked by p21N17 Ras. From these and previous results, we suggest a model in which a linear order of NGF receptor, Src, Ras, and Raf activities is used by NGF to elicit gene inductions. These signaling components define branchpoints in the pathway to specific gene induction events, providing a mechanism for generating a host of diverse NGF actions.

Nerve growth factor in neuronal development and maintenance

1987 ◽  
Vol 132 (1) ◽  
pp. 177-190
Author(s):  
T. P. Misko ◽  
M. J. Radeke ◽  
E. M. Shooter
Keyword(s):  
Signal Transduction ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Nerve Terminal ◽  
Consensus Sequence ◽  
Neuronal Cell ◽  
Retrograde Transport ◽  
Nerve Growth ◽  
Lower Affinity ◽  
Molecular Masses

One of the major roles of nerve growth factor (NGF) is to mediate the selective survival of a proportion of the developing sympathetic and sensory neurones as they innervate their particular target tissues. The underlying basis of this phenomenon is the synthesis of limited amounts of NGF in the target, its secretion around, and uptake by, the nerve terminal and its retrograde transport along axons to the neuronal cell bodies. The cascades of reactions which lead to neuronal survival and maintenance are initiated by signal transduction somewhere in this pathway. Retrograde transport and the initial signal transduction step begin when NGF binds to NGF receptors on the nerve terminal. Receptor-mediated internalization and the survival and maintenance function of NGF are mediated by the higher affinity receptors. These receptors have relative molecular masses of approx. 145,000 and are trypsin-resistant when occupied. In contrast, the larger population of lower affinity receptors have relative molecular masses of 85,000 and are rapidly degraded by trypsin. Clustering of the lower affinity receptors by a variety of agents gives them many of the characteristics of the higher affinity receptors, suggesting receptor interconversion may play a role in NGF actions. The structure of the lower affinity NGF receptor, determined by gene transfer and cloning, shows it to be a unique, heavily glycosylated protein. The extracellular domain is rich in cysteine-containing repeat units while the intracellular domain lacks the consensus sequence for an endogenous kinase activity. It is likely that the higher affinity receptor contains this protein as the NGF binding subunit together with a second protein which determines both the nature of the signal transduction mechanism and the process of internalization.

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