VASE-encoded peptide modifies NCAM- and L1-mediated neurite outgrowth

Lahrtz, Fritz; Horstkorte, Rüdiger; Cremer, Harold; Schachner, Melitta; Montag, Dirk

doi:10.1002/(sici)1097-4547(19971001)50:1<62::aid-jnr7>3.0.co;2-j

Cited by 16 publications

(4 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Ncam1 contains five Ig-like domains involved in homophilic binding of Ncam1 either in cis or trans, which in turn controls cellcell interactions and the induction of neurite outgrowth (Walsh and Doherty 1997). The AS of VASE determines the inclusion or exclusion of the fourth Ig domain and alters the homophilic binding of NCAM-140 (Lahrtz et al 1997). The VASE À isoform of NCAM-140 stimulateswhile VASE + inhibits-neurite outgrowth (Doherty et al 1992;Liu et al 1993;Saffell et al 1994).…”

Section: Pqbp1 Affects the As Of Mrnas In Neuronsmentioning

confidence: 99%

PQBP1, a factor linked to intellectual disability, affects alternative splicing associated with neurite outgrowth

et al. 2013

View full text Add to dashboard Cite

Polyglutamine-binding protein 1 (PQBP1) is a highly conserved protein associated with neurodegenerative disorders. Here, we identify PQBP1 as an alternative messenger RNA (mRNA) splicing (AS) effector capable of influencing splicing of multiple mRNA targets. PQBP1 is associated with many splicing factors, including the key U2 small nuclear ribonucleoprotein (snRNP) component SF3B1 (subunit 1 of the splicing factor 3B [SF3B] protein complex). Loss of functional PQBP1 reduced SF3B1 substrate mRNA association and led to significant changes in AS patterns. Depletion of PQBP1 in primary mouse neurons reduced dendritic outgrowth and altered AS of mRNAs enriched for functions in neuron projection development. Disease-linked PQBP1 mutants were deficient in splicing factor associations and could not complement neurite outgrowth defects. Our results indicate that PQBP1 can affect the AS of multiple mRNAs and indicate specific affected targets whose splice site determination may contribute to the disease phenotype in PQBP1-linked neurological disorders.

show abstract

Section: Pqbp1 Affects the As Of Mrnas In Neuronsmentioning

confidence: 99%

PQBP1, a factor linked to intellectual disability, affects alternative splicing associated with neurite outgrowth

et al. 2013

View full text Add to dashboard Cite

show abstract

“…This prolonged maintenance of p75 expression may contribute to the enhanced migration of OEC s compared with Schwann cells. The transplanted OEC s also express high levels of molecules such as laminin (Liesi, 1985) and L1, which may contribute to both the cell migration and the induction of axon growth (Burden-Gulley et al, 1997;Lahrtz et al, 1997).…”

Section: The Composition and Behavior Of The Transplanted Oecsmentioning

confidence: 99%

Regeneration of Adult Rat Corticospinal Axons Induced by Transplanted Olfactory Ensheathing Cells

1998

View full text Add to dashboard Cite

Precisely localized focal stereotaxic electrolytic lesions were made in the corticospinal tract at the level of the first to second cervical segments in the adult rat. This consistently destroyed all central nervous tissue elements (axons, astrocytes, oligodendrocytes, microglia, and microvessels) in a highly circumscribed area.In a group of these rats immediately after lesioning, a suspension of cultured adult olfactory ensheathing cells was transplanted into the lesion site. Within the first week after transplantation, the cut corticospinal axons (identified by anterograde transport of biotin dextran) extended caudally along the axis of the corticospinal tract as single, fine, minimally branched sprouts that ended in a simple tip, often preceded by a small varicosity. By 3 weeks, the regenerating axons, ensheathed by P0-positive peripheral myelin had accumulated into parallel bundles, which now extended across the full length of the lesioned area and reentered the caudal part of the host corticospinal tract.The transplants contained two main types of cells: (1) p75-expressing S cells, which later formed typical peripheral one-to-one myelin sheaths around individual ensheathed axons, and (2) fibronectin-expressing A cells, which aggregated into tubular sheaths enclosing bundles of myelinated axons. The point of reentry of the axons into the central nervous territory of the caudal host corticospinal tract was marked by the resumption of oligodendrocytic myelination. Thus the effect of the transplant was to form a "patch" of peripheral-type tissue across which the cut central axons regenerated and then continued to grow along their original central pathway.

show abstract

“…The third Ig domain seems to bind to itself and is also capable of stimulating neurite outgrowth (Rao et al, 1992Sandig et al, 1994;Ranheim et al, 1996). The fourth Ig domain is involved in interaction with another NCAM, L1, and contains an alternatively spliced 10 amino acidlong sequence termed VASE, which when expressed abrogates the neurite outgrowth-promoting activity of NCAM (Small and Akeson, 1990;Saffell et al, 1994;Lahritz et al, 1997). In contrast, relatively little is known about the functions of the cytoplasmic domains of NCAM.…”

mentioning

confidence: 99%

Identification of an Amino Acid Sequence Motif in the Cytoplasmic Domain of the NCAM‐140 kDa Isoform Essential for Its Neuritogenic Activity

Kolkova

Pedersen

Berezin

et al. 2000

Journal of Neurochemistry

View full text Add to dashboard Cite

Abstract:The functions of the extracellular domains of neural cell adhesion molecule (NCAM) have been studied extensively, whereas the roles of the cytoplasmic domains of the transmembrane forms of NCAM are less elucidated. We investigated the importance of the cytoplasmic domain of the 140-kDa NCAM isoform (cyt-NCAM-140) and of the 180-kDa NCAM isoform (cyt-NCAM-180) in NCAM-induced neurite extension by estimating NCAM-dependent neurite outgrowth from PC12-E2 cells grown in coculture with NCAM-negative or NCAM-positive fibroblasts. PC12-E2 cells were transiently transfected with expression plasmids encoding cytNCAM-140, cytNCAM-180, the constitutively active form of the mitogen-activated protein (MAP) kinase/extracellular signal-regulated kinase kinase (MEK2), and the enhanced variant of the green fluorescent protein (EGFP). EGFP expression was used for identification of transfected cells. We found that expression of cytNCAM-180 had no effect on NCAM-stimulated neuritogenesis, whereas expression of cytNCAM-140 strongly inhibited this process. However, if MEK2 was expressed concomitantly with cytNCAM-140, neurite outgrowth was rescued, indicating that cytNCAM-140 is involved in signaling via the Ras-MAP kinase pathway. PC12-E2 cells were subsequently transiently transfected with constructs encoding a series of fragments of cytNCAM-140 and various full-length cytNCAM-140 mutants, and the residues Thr-Glu-Val-Lys-Thr (839 -843) were identified as essential in NCAM-stimulated neuritogenesis. The combined substitution of Glu 840 and Lys 842 with Ala abrogated the effect of the construct, assigning a critical role to these two residues. Key Words: NCAM-Cytoplasmic domain-Fibroblasts-Neurite outgrowth.

show abstract

VASE-encoded peptide modifies NCAM- and L1-mediated neurite outgrowth

Cited by 16 publications

References 47 publications

PQBP1, a factor linked to intellectual disability, affects alternative splicing associated with neurite outgrowth

PQBP1, a factor linked to intellectual disability, affects alternative splicing associated with neurite outgrowth

Regeneration of Adult Rat Corticospinal Axons Induced by Transplanted Olfactory Ensheathing Cells

Identification of an Amino Acid Sequence Motif in the Cytoplasmic Domain of the NCAM‐140 kDa Isoform Essential for Its Neuritogenic Activity

Contact Info

Product

Resources

About