Structure of a new nervous system glycoprotein, Nr-CAM, and its relationship to subgroups of neural cell adhesion molecules.

Grumet, Martin; Mauro, Vincent P.; Burgoon, Mark P.; Edelman, Gerald M.; Cunningham, Bruce A.

doi:10.1083/jcb.113.6.1399

Cited by 178 publications

(149 citation statements)

References 96 publications

(156 reference statements)

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“…This is in marked contrast to the group of the L1-like glycoproteins, which appear to be closely related by both structural and functional features, yet exhibit a substantially lower amino acid sequence identity between the avian and the mammalian representatives, viz. Ng-CAM/L1 or Nr-CAM/Ll, of 44% and 39%, respectively (Burgoon et al, 1991;Grumet et al, 1991).…”

Section: Discussionmentioning

confidence: 99%

“…The deduced amino acid sequence of axonin-1 was compared with the NBRF-PIR protein database (release 25,1990), and especially to all the sequences of neural cell adhesion molecules of the Ig/FNIII subfamily available to date, including rat TAG-1 (Furley et al, 1990), chicken F11 (Bruemmendorf et al, 1989) and contactin (Ranscht, 1988), mouse F3 (Gennarini et al, 1989), chicken Ng-CAM (Burgoon et al, 1991), chicken Nr-CAM (Grumet et al, 1991), mouse L1 (Moos et al, 1988), and chicken N-CAM (Cunningham et al, 1987). The highest degree of similarity was found to the sequence of rat TAG-I.…”

Section: Similarity Of Axonin-1 With Other Axcamsmentioning

confidence: 99%

“…Based on comparisons of their deduced amino acid sequence and their presumed structural organisation, they may be subdivided into two groups. One group includes glycoproteins with six Ig and five FNIII domains, such as mouse L1 (Rathjen and Schachner, 1984), rat NILE (Prince et al, 1989), chicken Ng-CAM (Burgoon et al, 1991), chicken Nr-CAM (Grumet et al, 1991) and Drosophilu neuroglian (Bieber et al, 1989). Information derived from N-terminal sequencing and immunological comparisons indicate that chicken G4 (Rathjen et al, 1987), 8D9 (Lemmon and McLoon, 1986) and Bravo (de la Rosa et al, 1990) are further members of this subgroup.…”

mentioning

confidence: 99%

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The axonally secreted cell adhesion molecule, axonin‐1

Zuellig

Rader

Schroeder

et al. 1992

European Journal of Biochemistry

120

111

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Axonin-I is an axon-associated cell adhesion molecule (AxCAM) of the chicken, which promotes neurite outgrowth by interaction with the AxCAM Ll(G4) of the neuritic membrane. Here we report the cloning and sequence determination of a cDNA encoding axonin-I, Peptides generated by enzymatic cleavage showed similarity to the AxCAM F11. Degenerated polymerase chain reaction (PCR) primers were designed and an axonin-I fragment was amplified from mRNA of embryonic retina. Screening of a cDNA library from embryonic brain resulted in the isolation of a 4.0-kb cDNA insert with an open reading frame of 3108 nucleotides. The deduced polypeptide of 1036 amino acids includes a putative hydrophobic N-terminal signal sequence of 23 or 25 amino acids and a C-terminal hydrophobic sequence of 29 amino acids which is suggestive of sequences serving as signal for the attachment of a glycosyl-phosphatidylinositol (glycosyl-PtdIns) anchor. The putative mature form of axonin-1 comprises six immunoglobulin-like repeats, followed by four fibronectin-type I11 repeats.Axonin-1 exhibits 75% amino acid identity with the AxCAM TAG-1 of the rat, suggesting that it is the chicken homologue of TAG-1. Like TAG-1, axonin-I is glycosyl-PtdIns-anchored to the neuronal membrane; in contrast to TAG-1, it does not exhibit an Arg-Gly-Asp sequence.The interconnection of neurons by processes forming synaptic contacts is one of the crucial developmental stages of neurogenesis. In order to span long distances, bundles of axons are formed in a process which is thought to be driven by the tendency of growing axons to adhere specifically to and elongate along preexisting axons. The consistency with which

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Section: Discussionmentioning

confidence: 99%

Section: Similarity Of Axonin-1 With Other Axcamsmentioning

confidence: 99%

mentioning

confidence: 99%

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The axonally secreted cell adhesion molecule, axonin‐1

Zuellig

Rader

Schroeder

et al. 1992

European Journal of Biochemistry

120

111

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“…So far, Nr-CAM and neurofascin have only been found in the chick. goon et al, 1991;Grumet et al, 1991;Volkmer et al, 1992). Axonin-1/TAG-1 and Fll/F3 also exist as secreted forms, probably derived from an intracellular pool rather than released from the cell surface (Ruegg et al, 1989).…”

Section: Structural Features Of Ig/fniii-like Proteins Concentrated Omentioning

confidence: 99%

Regulation of axonal growth in the vertebrate nervous system by interactions between glycoproteins belonging to two subgroups of the immunoglobulin superfamily.

Sonderegger

Rathjen

1992

The Journal of Cell Biology

152

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“…These proteins contain multiple C2-type immunoglobulin (Ig)-like extracellular domains and multiple fibronectin type III (FnIII) repeats, which are connected with the cell membrane via a transmembrane domain or lipid anchor (Williams and Barclay, 1988;Gumbiner, 1996;Hortsch, 2000). The NrCAM (neuron-glia-related cell-adhesion molecule) is a 200 -220 kDa transmembrane protein composed of six Ig-like domains and five FnIII repeats in the extracellular region, plus a highly conserved cytoplasmic tail (Grumet et al, 1991;Kayyem et al, 1992;Lane et al, 1996). In addition to the nervous system, expression of the NrCAM gene (chromosome 7q31.1 -q31.2) has also been demonstrated in a variety of healthy or neoplastic tissues and cell lines including pancreatic cancer, melanoma, renal and colon carcinoma, adrenal gland, placenta, thyroid, and testis (Wang et al, 1998;Dhodapkar et al, 2001;Conacci-Sorrell et al, 2002a).…”

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confidence: 99%

NrCAM, a neuronal system cell-adhesion molecule, is induced in papillary thyroid carcinomas

et al. 2007

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NrCAM (neuron-glia-related cell-adhesion molecule) is primarily, although not solely, expressed in the nervous system. In the present study, NrCAM expression was analysed in a series (46) of papillary thyroid carcinomas (PTCs) and paired normal tissues (NT). Quantitative reverse transcriptase (QRT)-PCR revealed that NrCAM expression was upregulated in all PTCs compared to normal thyroid, whatever the stage or size of the primary tumour. NrCAM transcript levels were 1.3-to 30.7-fold higher in PTCs than in NT. Immunohistochemistry (IHC) confirmed that the expression of NrCAM was considerably higher in tumours (score 2 þ /3 þ ) than in adjacent normal paratumoural thyroid tissue. The NrCAM protein was detected in all but three (93.3%) PTC samples, and it was mainly cytoplasmic; in some cases there was additional membranous localisation -basolateral and partly apical. In the normal thyroid and tissues surrounding tumours, focal NrCAM immunolabelling was seen only in follicles containing tall cells, where staining was restricted to the apical pole of thyrocytes. Western blot analysis corroborated the QRT -PCR and IHC results, showing higher NrCAM protein levels in PTCs than in paired NT. The level of overexpression of the NrCAM mRNA in tumourous tissue appeared to be independent of the primary tumour stage (pT) or the size of the PTC. These data provide the first evidence that NrCAM is overexpressed in human PTCs at the mRNA and protein levels, whatever the tumour stage. Thus, the induction and upregulation of NrCAM expression could be implicated in the pathogenesis and behaviour of papillary thyroid cancers.

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Structure of a new nervous system glycoprotein, Nr-CAM, and its relationship to subgroups of neural cell adhesion molecules.

Abstract: Abstract. We have identified and characterized a new

Cited by 178 publications

References 96 publications

The axonally secreted cell adhesion molecule, axonin‐1

The axonally secreted cell adhesion molecule, axonin‐1

Regulation of axonal growth in the vertebrate nervous system by interactions between glycoproteins belonging to two subgroups of the immunoglobulin superfamily.

NrCAM, a neuronal system cell-adhesion molecule, is induced in papillary thyroid carcinomas

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