 |
|||||
|
|||||
|
|||||
|
|||||
|
|||||
Previous Article | Next Article
The Journal of Neuroscience, January 15, 1999, 19(2):775-782
Evidence for a Role of Truncated trkC Receptor Isoforms in Mouse Development
Mary Ellen Palko, Vincenzo Coppola, and Lino Tessarollo Neural Development Group, Advanced Bioscience Laboratories-Basic Research Program, National Cancer Institute-Frederick Cancer Research and Development Center, Frederick, Maryland 21701
The trkC locus encodes several receptors for neurotrophin-3, including the well studied full-length tyrosine kinase isoform, in addition to receptor isoforms lacking the kinase active domain. TrkC receptors are widely expressed throughout mouse development in many different organs. To investigate the function of truncated receptors in vivo and to identify cell types that are biologically responsive to this gene product, we have overexpressed a physiological truncated trkC isoform in the mouse. Mice overexpressing this receptor develop to term but die in the first postnatal days. High levels of transgene expression result in severe developmental defects in the peripheral nervous system and in the heart. The severity of neuronal losses observed in these animals suggests that truncated receptors may act by sequestering neurotrophin, thus, closely relating this mouse model to the neurotrophin-3-deficient one. Lower levels of exogenous truncated receptor in transgenic mice result in a more modest phenotype and, in some neuronal populations, do not cause neural deficits. Taken together, these data suggest that truncated trkC receptor isoforms may have modulatory functions in development.
Key words: trkC; truncated receptor; development; neurotrophin; trk receptors; transgenic
Copyright © 1999 Society for Neuroscience 0270-6474/99/192775-08$05.00/0
This article has been cited by other articles:
L. Carim-Todd, K. G. Bath, G. Fulgenzi, S. Yanpallewar, D. Jing, C. A. Barrick, J. Becker, H. Buckley, S. G. Dorsey, F. S. Lee, et al.
Endogenous Truncated TrkB.T1 Receptor Regulates Neuronal Complexity and TrkB Kinase Receptor Function In Vivo
J. Neurosci., January 21, 2009; 29(3): 678 - 685.
[Abstract] [Full Text] [PDF]
A. Caporali and C. Emanueli
Cardiovascular Actions of Neurotrophins
Physiol Rev, January 1, 2009; 89(1): 279 - 308.
[Abstract] [Full Text] [PDF]
P. F. Esteban, H.-Y. Yoon, J. Becker, S. G. Dorsey, P. Caprari, M. E. Palko, V. Coppola, H. U. Saragovi, P. A. Randazzo, and L. Tessarollo
A kinase-deficient TrkC receptor isoform activates Arf6-Rac1 signaling through the scaffold protein tamalin
J. Cell Biol., April 24, 2006; 173(2): 291 - 299.
[Abstract] [Full Text] [PDF]
W. Ma, L. Tessarollo, S.-B. Hong, M. Baba, E. Southon, T. C. Back, S. Spence, C. G. Lobe, N. Sharma, G. W. Maher, et al.
Hepatic Vascular Tumors, Angiectasis in Multiple Organs, and Impaired Spermatogenesis in Mice with Conditional Inactivation of the VHL Gene
Cancer Res., September 1, 2003; 63(17): 5320 - 5328.
[Abstract] [Full Text] [PDF]
K. Agerman, J. Hjerling-Leffler, M. P. Blanchard, E. Scarfone, B. Canlon, C. Nosrat, and P. Ernfors
BDNF gene replacement reveals multiple mechanisms for establishing neurotrophin specificity during sensory nervous system development
Development, April 15, 2003; 130(8): 1479 - 1491.
[Abstract] [Full Text] [PDF]
S. Wang, P. Bray, T. McCaffrey, K. March, B. L. Hempstead, and R. Kraemer
p75NTR Mediates Neurotrophin-Induced Apoptosis of Vascular Smooth Muscle Cells
Am. J. Pathol., October 1, 2000; 157(4): 1247 - 1258.
[Abstract] [Full Text] [PDF]
I. Das, J. R. Sparrow, M. I. Lin, E. Shih, T. Mikawa, and B. L. Hempstead
Trk C Signaling Is Required for Retinal Progenitor Cell Proliferation
J. Neurosci., April 15, 2000; 20(8): 2887 - 2895.
[Abstract] [Full Text] [PDF]
|
|
|
|
 |
|