Functional characterization of NCAM fibronectin type III domains: Demonstration of modulatory effects of the proline-rich sequence encoded by alternatively spliced exons a and AAG

Kasper, Christina; Stahlhut, Martin; Berezin, Vladimir; Maar, Thomas E.; Edvardsen, Klaus; Kiselyov, Vladislav V.; Soroka, Vladislav; Bock, Elisabeth

doi:10.1002/(sici)1097-4547(19961015)46:2<173::aid-jnr5>3.0.co;2-e

Cited by 37 publications

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“…Only very small differences were observed between the calculated and the actual molecular masses probably because of aberrant electrophoretic migration. Characterization of F3I,II-MBP has been described previously (22).…”

Section: Resultsmentioning

confidence: 99%

“…The recombinant clones were identified by small scale expression of the fusion proteins. Production of a fusion protein containing NCAM fibronectin type III domains I and II has been described previously (22). The fusion proteins were designated Ign-MBP (Ig-like domain number n produced in E. coli as a fusion protein with MBP as a fusion partner); Ex16,17,19-MBP (polypeptide encoded by NCAM exons 16, 17, and 19 produced in E. coli as a fusion protein with MBP as a fusion partner); and F3I,II-MBP (fibronectin type III domains I and II produced in E. coli as a fusion protein with MBP as a fusion partner).…”

Section: Production Of Fusion Proteins Of Ncam Fragments In a Bacterimentioning

confidence: 99%

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The First Immunoglobulin-like Neural Cell Adhesion Molecule (NCAM) Domain Is Involved in Double-reciprocal Interaction with the Second Immunoglobulin-like NCAM Domain and in Heparin Binding

Kiselyov

Berezin

Maar

et al. 1997

Journal of Biological Chemistry

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108

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To study the function of the first immunoglobulin (Ig)-like domain of the neural cell adhesion molecule (NCAM), it was produced as a recombinant fusion protein in a bacterial expression system and as a recombinant protein in a eukaryotic expression system of the yeast Pichia pastoris. For comparison, other NCAM domains were also produced as fusion proteins. By means of surface plasmon resonance analysis, it was shown that the first Ig-like NCAM domain binds the second Ig-like NCAM domain with a dissociation constant 5.5 +/- 1.6 x 10(-5) M. Furthermore, it was found that the first Ig-like domain binds heparin. It was also demonstrated that the second Ig-like NCAM domain binds heparin and that both domains bind collagen type I via heparin but not collagen type I directly.

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Section: Resultsmentioning

confidence: 99%

Section: Production Of Fusion Proteins Of Ncam Fragments In a Bacterimentioning

confidence: 99%

The First Immunoglobulin-like Neural Cell Adhesion Molecule (NCAM) Domain Is Involved in Double-reciprocal Interaction with the Second Immunoglobulin-like NCAM Domain and in Heparin Binding

Kiselyov

Berezin

Maar

et al. 1997

Journal of Biological Chemistry

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108

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“…The fibroblastoid mouse cell line L929 (L-cells) was obtained from the European Cell Culture Collection (Salisbury, UK). L-cells stably transfected with full-length cDNA encoding human 140 kDa NCAM were a gift from Dr Bock, Copenhagen [13]. The cells were routinely grown at 371C, 5% CO 2 in Dulbecco's modified Eagle's medium supplemented with 10% (v/v) fetal calf serum (Gibco BRL, Paisley, UK).…”

Section: Methodsmentioning

confidence: 99%

“…[13]. PC12 cells were stably transfected with the eukaryotic expression vector pJRERb2-AcGFP1 containing a cDNA construct encoding the entire sequence of CRMP-2.…”

Section: Methodsmentioning

confidence: 99%

Role of collapsin response mediator protein-2 in neurite outgrowth of PC12 cells

Bork

Karbe²,

Pollscheit³

et al. 2010

NeuroReport

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Collapsin response mediator proteins (CRMPs) are involved in cell differentiation and axonal growth. In this study, we investigated neurite outgrowth and the expression of CRMP-2 in PC12 cells. Nondifferentiated PC12 cells hardly express CRMP-2, but the expression of CRMP-2 increases with neurite outgrowth. We established a stable CRMP-2-overexpressing PC12 cell line and found that PC12 cells, which constitutively overexpress CRMP-2, were unable to extend neurites after stimulation with the nerve growth factor or the neural cell adhesion molecule, a procedure that promotes neurite outgrowth in untransfected cells. In contrast, a PC12 cell line deficient in CRMP-2 extends neurites after the stimulation of nerve growth factor or neural cell adhesion molecule.

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“…Rabbit antibodies against rat and chicken BASP1 and against human and rat NCAM were prepared as previously described (Kasper et al, 1996; Mosevitsky et al, 1997). Mouse antibodies against rat GAP‐43 were from Chemicon International/Millipore A/S (Copenhagen, Denmark).…”

Section: Methodsmentioning

confidence: 99%

Characterization of BASP1‐mediated neurite outgrowth

Korshunova

Caroni²,

Kolkova

et al. 2008

J of Neuroscience Research

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The brain acid-soluble protein BASP1 (CAP-23, NAP-22) belongs to the family of growth-associated proteins, which also includes GAP-43, a protein recently shown to regulate neural cell adhesion molecule (NCAM)-mediated neurite outgrowth. Here, the effects of BASP1 overexpression were investigated in PC12E2 cells and primary hippocampal neurons. BASP1 overexpression stimulated neurite outgrowth in both cell types. The effects of BASP1 and trans-homophilic NCAM interactions were additive, and BASP1-induced neurite outgrowth was not inhibited by ectopic expression of cytoplasmic NCAM domains. Furthermore, inhibition of signaling via the fibroblast growth factor receptor, Src-family nonreceptor tyrosine kinases, protein kinase C, or GSK3beta, and expression of constructs of the cytoskeletal proteins spectrin and tau inhibited NCAM- but not BASP1-induced neurite outgrowth. Expression of BASP1 mutated at the serine-5 phosphorylation site stimulated neurite outgrowth to a degree comparable to that observed in response to overexpression of wild-type BASP1, whereas expression of BASP1 mutated at the myristoylation site at glycine-1 completely abrogated the stimulatory effects of the protein on neurite outgrowth. Finally, coexpression experiments with dominant negative and wild-type versions of GAP-43 and BASP1 demonstrated that the two proteins could substitute for each other with respect to induction of NCAM-independent neurite outgrowth, whereas BASP1 was unable to replace the stimulatory effect of GAP-43 on NCAM-mediated neurite outgrowth. These observations demonstrate that BASP1 and GAP-43 have overlapping, but not identical, functions in relation to neurite outgrowth and indicate that the main function of BASP1 is to regulate the organization and morphology of the plasma membrane.

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Functional characterization of NCAM fibronectin type III domains: Demonstration of modulatory effects of the proline-rich sequence encoded by alternatively spliced exons a and AAG

Cited by 37 publications

References 0 publications

The First Immunoglobulin-like Neural Cell Adhesion Molecule (NCAM) Domain Is Involved in Double-reciprocal Interaction with the Second Immunoglobulin-like NCAM Domain and in Heparin Binding

The First Immunoglobulin-like Neural Cell Adhesion Molecule (NCAM) Domain Is Involved in Double-reciprocal Interaction with the Second Immunoglobulin-like NCAM Domain and in Heparin Binding

Role of collapsin response mediator protein-2 in neurite outgrowth of PC12 cells

Characterization of BASP1‐mediated neurite outgrowth

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