Abnormal intracellular trafficking of high affinity nerve growth factor receptor, Trk, in stable transfectants expressing presenilin 1 protein

2005 ◽  
Vol 137 (1-2) ◽  
pp. 70-76 ◽  
Author(s):  
Tadanori Hamano ◽  
Tatsuro Mutoh ◽  
Takeshi Tabira ◽  
Wataru Araki ◽  
Masaru Kuriyama ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Intracellular Trafficking ◽  
Growth Factor Receptor ◽  
Nerve Growth Factor Receptor ◽  
Presenilin 1 ◽  
Nerve Growth ◽  
Stable Transfectants ◽  
High Affinity

scholarly journals Interaction with TrkA Immobilizes gp75 in the High Affinity Nerve Growth Factor Receptor Complex

1995 ◽  
Vol 270 (5) ◽  
pp. 2133-2138 ◽  
Author(s):  
David E. Wolf ◽  
Christine A. McKinnon ◽  
Marie-Claire Daou ◽  
Robert M. Stephens ◽  
David R. Kaplan ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Growth Factor Receptor ◽  
Nerve Growth Factor Receptor ◽  
Receptor Complex ◽  
Nerve Growth ◽  
High Affinity

Production of a Monoclonal Antibody Directed against the High-Affinity Nerve Growth Factor Receptor

1999 ◽  
Vol 14 (2) ◽  
pp. 68-72 ◽  
Author(s):  
E. Tagliabue ◽  
C. Ghirelli ◽  
L. Lombardi ◽  
F. Castiglioni ◽  
L. Asnaghi ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Neuroblastoma Cell ◽  
Growth Factor Receptor ◽  
Nerve Growth Factor Receptor ◽  
Receptor Internalization ◽  
Growth Modulation ◽  
Nerve Growth ◽  
High Affinity

The high-affinity nerve growth factor receptor corresponds to the tyrosine protein kinase encoded by the proto-oncogene trkA. Different findings suggest that nerve growth factor (NGF) can be operative in the growth modulation of tumor cell lines possessing high-affinity binding sites for this molecule. Using as immunizing material the SKNBE neuroblastoma cell line transfected with proto-trkA we produced a monoclonal antibody (MAb) able to recognize the high-affinity nerve growth factor receptor. The selected MAb, designated MGR12, is directed against an epitope present on the extracellular domain of the receptor since it showed reactivity on living trkA-expressing cells and was able to immunoprecipitate the proto-trkA molecule. The MGR12 MAb is directed against a non-functional epitope since it neither inhibited NGF binding nor induced receptor internalization. This new reagent appears to be an appropriate tool for analyzing the expression of high-affinity nerve growth factor receptor in tumors of different origin and for elucidating its involvement in tumor progression.

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