|
|
|
|
|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | ||||
Development, Vol 118, Issue 2 509-522, Copyright © 1993 by Company of Biologists
JOURNAL ARTICLES |
RO Karlstrom, LP Wilder and MJ Bastiani
Department of Biology, University of Utah, Salt Lake City 84112.
We describe the developmental expression in grasshopper (Schistocerca americana) and molecular characterization in grasshopper and fruit fly (Drosophila melanogaster) of Lachesin, a novel immunoglobulin superfamily protein. Lachesin is expressed on the surfaces of differentiating neuronal cells from the onset of neurogenesis in both the central and peripheral nervous systems. Lachesin expression begins in some cells of the neurogenic ectoderm immediately after engrailed expression begins in the posterior cells of each future segment. All neurogenic cells express Lachesin early, but only those cells that become neuroblasts continue to express Lachesin. Ectodermal cells in the neurogenic region that adopt non-neuronal fates lose Lachesin at the time that they diverge from a potentially neurogenic pathway. Neuroblasts, ganglion mother cells and neurons all express Lachesin early in their lives, but expression becomes restricted to a subset of neurons as development progresses. Sensory neurons express Lachesin as they delaminate from the body wall ectoderm. Lachesin is also present on growing axons of the CNS and PNS and becomes restricted to a subset of axons later in development. This expression is unique among known insect neurogenic genes and suggests a role for Lachesin in early neuronal differentiation and axon outgrowth. Grasshopper Lachesin is a 38 x 10(3) M(r) protein linked to cell membranes through a glycosyl phosphatidylinositol anchor. We have cloned the Lachesin gene from both grasshopper and fly. The proteins are highly conserved (70% identical) between the two species. Lachesin is similar to Drosophila amalgam, bovine OBCAM and the human poliovirus receptor, putting it into a subgroup of the immunoglobulin superfamily containing one V- and two C2-type immunoglobulin domains. Lachesin is also similar to several other vertebrate immunoglobulin superfamily proteins (TAG-1, F11, L1 and NgCAM) known to function in neurite outgrowth and other cell surface recognition events.
This article has been cited by other articles:
|
|
 |
|
  M. Cayre, S. Scotto-Lomassese, J. Malaterre, C. Strambi, and A. Strambi Understanding the Regulation and Function of Adult Neurogenesis: Contribution from an Insect Model, the House Cricket Chem Senses, May 1, 2007; 32(4): 385 - 395. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Llimargas, M. Strigini, M. Katidou, D. Karagogeos, and J. Casanova Lachesin is a component of a septate junction-based mechanism that controls tube size and epithelial integrity in the Drosophila tracheal system Development, January 1, 2004; 131(1): 181 - 190. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Nakamura, D. Baldwin, S. Hannaford, J. Palka, and C. Montell Defective Proboscis Extension Response (DPR), a Member of the Ig Superfamily Required for the Gustatory Response to Salt J. Neurosci., May 1, 2002; 22(9): 3463 - 3472. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Ashburner, S. Misra, J. Roote, S. E. Lewis, R. Blazej, T. Davis, C. Doyle, R. Galle, R. George, N. Harris, et al. An Exploration of the Sequence of a 2.9-Mb Region of the Genome of Drosophila melanogaster: The Adh Region Genetics, September 1, 1999; 153(1): 179 - 219. [Abstract] [Full Text]
|
|
|
|
 |
|
 A. Marg, P. Sirim, F. Spaltmann, A. Plagge, G. Kauselmann, F. Buck, F. G. Rathjen, and T. Brummendorf Neurotractin, A Novel Neurite Outgrowth-promoting Ig-like Protein that Interacts with CEPU-1 and LAMP J. Cell Biol., May 17, 1999; 145(4): 865 - 876. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Wright, M. Snyder, K. Schwinof, S Combes, and P. Copenhaver A role for fasciclin II in the guidance of neuronal migration Development, January 6, 1999; 126(14): 3217 - 3228. [Abstract] [PDF]
|
|
|
|
|
|
E. Seaver, E. Carpenter, and M. Bastiani REGA-1 is a GPI-linked member of the immunoglobulin superfamily present on restricted regions of sheath cell processes in grasshopper Development, January 2, 1996; 122(2): 567 - 578. [Abstract] [PDF]
|
|
|
|
|
|
J. C. Garbe, E. Yang, and J. W. Fristrom IMP-L2: an essential secreted immunoglobulin family member implicated in neural and ectodermal development in Drosophila Development, December 1, 1993; 119(4): 1237 - 1250. [Abstract] [PDF]
|
|
|
|
 |
|
 T. Angata and A. Varki Cloning, Characterization, and Phylogenetic Analysis of Siglec-9, a New Member of the CD33-related Group of Siglecs. EVIDENCE FOR CO-EVOLUTION WITH SIALIC ACID SYNTHESIS PATHWAYS J. Biol. Chem., July 14, 2000; 275(29): 22127 - 22135. [Abstract] [Full Text] [PDF]
|
|
