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dc.contributor.authorHolm, J.
dc.contributor.authorHillenbrand, R.
dc.contributor.authorSteuber, Volker
dc.contributor.authorBartsch, U.
dc.contributor.authorMoos, M.
dc.contributor.authorLübbert, H.
dc.contributor.authorMontag, D.
dc.contributor.authorSchachner, M.
dc.date.accessioned2011-10-06T08:01:08Z
dc.date.available2011-10-06T08:01:08Z
dc.date.issued1996
dc.identifier.citationHolm , J , Hillenbrand , R , Steuber , V , Bartsch , U , Moos , M , Lübbert , H , Montag , D & Schachner , M 1996 , ' Structural features of a close homologue of L1 (CHL1) in the mouse: a new member of the L1 family of neural recognition molecules ' , European Journal of Neuroscience , vol. 8 , no. 8 , pp. 1613-29 . https://doi.org/10.1111/j.1460-9568.1996.tb01306.x
dc.identifier.issn0953-816X
dc.identifier.otherPURE: 381238
dc.identifier.otherPURE UUID: b96bda62-909d-4775-9f11-cd5c9f4aeddd
dc.identifier.otherPubMed: 8921253
dc.identifier.otherScopus: 0029739225
dc.identifier.urihttp://hdl.handle.net/2299/6586
dc.descriptionFull text of this article is not available in the UHRA
dc.description.abstractWe have identified a close homologue of L1 (CHL1) in the mouse. CHL1 comprises an N-terminal signal sequence, six immunoglobulin (Ig)-like domains, 4.5 fibronectin type III (FN)-like repeats, a transmembrane domain and a C-terminal, most likely intracellular domain of approximately 100 amino acids. CHL1 is most similar in its extracellular domain to chicken Ng-CAM (approximately 40% amino acid identity), followed by mouse L1, chicken neurofascin, chicken Nr-CAM, Drosophila neuroglian and zebrafish L1.1 (37-28% amino acid identity), and mouse F3, rat TAG-1 and rat BIG-1 (approximately 27% amino acid identity). The similarity with other members of the Ig superfamily [e.g. neural cell adhesion molecule (N-CAM), DCC, HLAR, rse] is 16-11%. The intracellular domain is most similar to mouse and chicken Nr-CAM, mouse and rat neurofascin (approximately 60% amino acid identity) followed by chicken neurofascin and Ng-CAM, Drosophila neuroglian and zebrafish L1.1 and L1.2 (approximately 40% amino acid identity). Besides the high overall homology and conserved modular structure among previously recognized members of the L1 family (mouse/human L1/rat NILE; chicken Ng-CAM; chicken/mouse Nr-CAM; Drosophila neuroglian; zebrafish L1.1 and L1.2; chicken/mouse neurofascin/rat ankyrin-binding glycoprotein), criteria characteristic of L1 were identified with regard to the number of amino acids between positions of conserved amino acid residues defining distances within and between two adjacent Ig-like domains and FN-like repeats. These show a collinearity in the six Ig-like domains and four adjacent FN-like repeats that is remarkably conserved between L1 and molecules containing these modules (designated the L1 family cassette), including the GPI-linked forms of the F3 subgroup (mouse F3/chicken F11/human CNTN1; rat BIG-1/mouse PANG; rat TAG-1/mouse TAX-1/chicken axonin-1). The colorectal cancer molecule (DCC), previously introduced as an N-CAM-like molecule, conforms to the L1 family cassette. Other structural features of CHL 1 shared between members of the L1 family are a high degree of N-glycosidically linked carbohydrates (approximately 20% of its molecular mass), which include the HNK-1 carbohydrate structure, and a pattern of protein fragments comprising a major 185 kDa band and smaller fragments of 165 and 125 kDa. As for the other L1 family members, predominant expression of CHL1 is observed in the nervous system and at later developmental stages. In the central nervous system CHL1 is expressed by neurons, but, in contrast to L1, also by glial cells. Our findings suggest a common ancestral L1-like molecule which evolved via gene duplication to generate a diversity of structurally and functionally distinct yet similar molecules.en
dc.format.extent17
dc.language.isoeng
dc.relation.ispartofEuropean Journal of Neuroscience
dc.subjectAnimals
dc.subjectBase Sequence
dc.subjectCOS Cells
dc.subjectCell Adhesion Molecules
dc.subjectFibronectins
dc.subjectImmunoglobulin G
dc.subjectLeukocyte L1 Antigen Complex
dc.subjectMembrane Proteins
dc.subjectMice
dc.subjectMice, Inbred ICR
dc.subjectMolecular Sequence Data
dc.subjectMultigene Family
dc.subjectNeural Cell Adhesion Molecule L1
dc.subjectNeural Cell Adhesion Molecules
dc.subjectPC12 Cells
dc.subjectProtein Sorting Signals
dc.subjectProtein Structure, Tertiary
dc.subjectProteins
dc.subjectRats
dc.subjectRats, Wistar
dc.subjectRepetitive Sequences, Nucleic Acid
dc.subjectSequence Homology, Amino Acid
dc.titleStructural features of a close homologue of L1 (CHL1) in the mouse: a new member of the L1 family of neural recognition moleculesen
dc.contributor.institutionCentre for Computer Science and Informatics Research
dc.contributor.institutionDepartment of Computer Science
dc.contributor.institutionSchool of Engineering and Computer Science
dc.contributor.institutionCentre of Data Innovation Research
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Engineering and Computer Science
dcterms.dateAccepted1996
rioxxterms.versionofrecordhttps://doi.org/10.1111/j.1460-9568.1996.tb01306.x
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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