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Titolo:
An alternative amino-terminus expressed in the central nervous system converts agrin to a type II transmembrane protein
Autore:
Neumann, FR; Bittcher, G; Annies, M; Schumacher, B; Kroger, S; Ruegg, MA;
Indirizzi:
Univ Basel, Biozentrum, Dept Pharmacol Neurobiol, CH-4056 Basel, Switzerland Univ Basel Basel Switzerland CH-4056 urobiol, CH-4056 Basel, Switzerland Max Planck Inst Brain Res, D-60528 Frankfurt, Germany Max Planck Inst Brain Res Frankfurt Germany D-60528 8 Frankfurt, Germany
Titolo Testata:
MOLECULAR AND CELLULAR NEUROSCIENCE
fascicolo: 1, volume: 17, anno: 2001,
pagine: 208 - 225
SICI:
1044-7431(200101)17:1<208:AAAEIT>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEPARAN-SULFATE PROTEOGLYCAN; POSTSYNAPTIC-LIKE APPARATUS; RETINAL GANGLION-CELLS; ADULT-RAT BRAIN; ACETYLCHOLINE-RECEPTOR; BASAL LAMINA; MUSCLE-FIBERS; MESSENGER-RNA; NEUROMUSCULAR-JUNCTION; HIPPOCAMPAL-NEURONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Neumann, FR Swiss Inst Expt Canc Res, 155 Chemin Boveresses, CH-1066 Epalinges, Switzerland Swiss Inst Expt Canc Res 155 Chemin Boveresses EpalingesSwitzerland CH-1066
Citazione:
F.R. Neumann et al., "An alternative amino-terminus expressed in the central nervous system converts agrin to a type II transmembrane protein", MOL CELL NE, 17(1), 2001, pp. 208-225

Abstract

Agrin is a basal lamina-associated heparansulfate proteoglycan that is a key molecule in the formation of the vertebrate neuromuscular junction. The carboxy-terminal part of agrin is involved in its synaptogenic activity. The aminoterminal end of chick agrin consists of a signal sequence, required for the targeting of the protein to the secretory pathway, and the amino-terminal agrin (NtA) domain that binds to basal lamina-associated laminins. The cDNA encoding rat agrin lacks this NtA domain and instead codes for a shorter amino-terminal end. While the NtA domain is conserved in several species, including human, sequences homologous to the amino-terminus of rat agrin have not been described. In this work, we have characterized these aminoterminal sequences in mouse and chick. We show that they all serve as a noncleaved signal anchor that immobilizes the protein in a N-cyto/C-exo orientation in the plasma membrane. Like the secreted form, this transmembrane form of agrin is highly glycosylated indicative of a heparansulfate proteoglycan. The structure of the 5' end of the mouse agrin gene suggests that a distinct promoter drives expression of the transmembrane form. Agrin transcripts encoding this form are enriched in the embryonic brain, particularly inneurons. To our knowledge, this is the first example of a molecule that issynthesized both as a basal lamina and a plasma membrane protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 09:59:10