Characterization of soluble forms of NCAM

Bock, Elisabeth; Edvardsen, Klaus; Gibson, Ann; Linnemann, Dorte; Lyles, Joan M.; Nybroe, Ole

doi:10.1016/0014-5793(87)81126-2

Cited by 53 publications

(19 citation statements)

References 15 publications

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“…The sizes of the soluble 115 kD NCAM ectodomain and 30 kD membraneassociated (Buttner et al, 2004) fragments resulting from PV-induced shedding were in accord with NCAM fragments identified in brain (Bock et al, 1987(Bock et al, , 1988Nybroe et al, 1989;Krog et al, 1992) and cerebrospinal fluid (Krog et al, 1992). The size of the soluble fragment suggested that proteolytic cleavage occurred at a juxtamembrane site of NCAM140 located between the fifth Ig-like domain and the transmembrane segment.…”

Section: Discussionsupporting

confidence: 56%

“…Moreover, a %115 kD band representing the soluble NCAM140 ectodomain appeared on blots of the conditioned media from pervanadate-stimulated cells using -NCAM-ECD antibodies ( Fig. 1, PV lower panel), and is the reported size of the NCAM ectodomain (Bock et al, 1987;Nybroe et al, 1989;Krog et al, 1992;Todaro et al, 2004). The 115 kD NCAM fragment was not present in conditioned media from untreated or PMA-treated cells.…”

Section: Cleavage Of the Ncam140 Ectodomain Is Induced By Pervanadatementioning

confidence: 88%

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Metalloprotease‐induced ectodomain shedding of neural cell adhesion molecule (NCAM)

Hinkle¹,

Diestel²,

Lieberman³

et al. 2006

J. Neurobiol.

102

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Transmembrane forms of neural cell adhesion molecule (NCAM140, NCAM180(1)) are key regulators of neuronal development. The extracellular domain of NCAM can occur as a soluble protein in normal brain, and its levels are elevated in neuropsychiatric disorders, such as schizophrenia; however the mechanism of ectodomain release is obscure. Ectodomain shedding of NCAM140, releasing a fragment of 115 kD, was found to be induced in NCAM-transfected L-fibroblasts by the tyrosine phosphatase inhibitor pervanadate, but not phorbol esters. Pervanadate-induced shedding was mediated by a disintegrin metalloprotease (ADAM), regulated by ERK1/2 MAP kinase. In primary cortical neurons, NCAM was shed at high levels, and the metalloprotease inhibitor GM6001 significantly increased NCAM-dependent neurite branching and outgrowth. Moreover, NCAM-dependent neurite outgrowth and branching were inhibited in neurons isolated from a transgenic mouse model of NCAM shedding. These results suggest that regulated metalloprotease-induced ectodomain shedding of NCAM down-regulates neurite branching and neurite outgrowth. Thus, increased levels of soluble NCAM in schizophrenic brain have the potential to impair neuronal connectivity.

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Section: Discussionsupporting

confidence: 56%

Section: Cleavage Of the Ncam140 Ectodomain Is Induced By Pervanadatementioning

confidence: 88%

Metalloprotease‐induced ectodomain shedding of neural cell adhesion molecule (NCAM)

Hinkle¹,

Diestel²,

Lieberman³

et al. 2006

J. Neurobiol.

102

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“…1). This exon contains a stop-codon thereby producing a truncated form of the extracellular part of NCAM with a M r around 115 kD (14,15). Soluble NCAM also exists in a ''shedded'' form.…”

Section: Isoforms Of Ncammentioning

confidence: 99%

Zippers Make Signals: NCAM-mediated Molecular Interactions and Signal Transduction

et al. 2004

Self Cite

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The neural cell adhesion molecule, NCAM, is involved in multiple cis- and trans-homophilic interactions (NCAM binding to NCAM) thereby facilitating cell-cell adhesion through the formation of zipper-like NCAM-complexes. NCAM is also involved in heterophilic interactions with a number of proteins and extracellular matrix molecules. Some of these heterophilic interactions are mutually exclusive, and some interfere with or are dependent on homophilic NCAM interactions. Furthermore, both homo- and heterophilic interactions are modulated by posttranslational modifications of NCAM. Heterophilic NCAM-interactions initiate several intracellular signal transduction pathways ultimately leading to biological responses involving cellular differentiation, proliferation, migration and survival. Both homo- and heterophilic NCAM-interactions can be mimicked by synthetic peptides, which can induce NCAM-like signalling, and in vitro and in vivo studies suggest that such NCAM mimetics may be used for the treatment of neurodegenerative disorders.

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“…Although NCAM is expressed transiently in various embryonic structures, the H-or Lform of NCAM is found predominantly in neurons and glial cells,4 in muscle," in the adrenal medulla," pheochromocytoma,'3 neuroblastoma cell^,'^,'^ anterior pituitary," pancreatic islets,17 developing kidney,18,19 Wilms tumor," and small cell lung cancer (SCLC) cell line^. '^,^^ The a- (2,8)-PSA-rich NCAM (NCAM-H) is recognized by a monoclonal antibody Mab 735," which also detects the SCLC cluster 1 (SC-1) antigens on SCLC cells, as shown recently by Moolenaar et alI5 In this study, we took a newly developed enzyme immunoassay that includes, aside from another NCAM-specific antibody, the monoclonal antibody Mab 735. To assess the value of NCAM as a possible tumor marker for patients with SCLC, we examined the sera of 221 patients with histologically confirmed SCLC in two prospective multicenter trials and compared the results with the expression of neuron-specific enolase (NSE), a rather specific and sensitive tumor marker for SCLC.…”

mentioning

confidence: 99%

Evaluation of serum neural cell adhesion molecule as a new tumor marker in small cell lung cancer

Jaques

Auerbach

Pritsch

et al. 1993

Cancer

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Background. Small cell lung cancer (SCLC) is distinguished from other histologic types of lung cancer by possessing a variety of neuroendocrine properties. Neuron‐specific enolase (NSE) is the most frequently elevated tumor marker for patients with SCLC at diagnosis. To assess the value of neural cell adhesion molecules (NCAM), another possible tumor marker for small cell lung cancer, NCAM was evaluated in the sera of patients with histologically confirmed SCLC in two prospective multicenter trials. Methods. The study includes 221 patients with SCLC, normal human blood donors (n = 34), patients with benign lung disease (n = 53), and patients with non‐small cell lung cancer (n = 28). NCAM was determined by means of an enzyme immunoassay, NSE by a radioimmunoassay. Results. The data show the following: (1) 51% (113 of 221) of all patients with SCLC had NCAM levels higher than 20 U/ml, 34% (75 of 221) had NSE levels higher than 25 ng/ml; (2) levels of both markers significantly differ between limited and extensive disease patients; (3) patients with pathologic NCAM and NSE levels have significantly shorter survival times; (4) a positive correlation between pretreatment NSE and NCAM levels was found (n = 221, r = 0.60); and (5) a correlation between serum marker levels and clinical status was found in follow‐up studies of 19 patients. Conclusions. From these data, it is concluded that NCAM is, along with NSE, a potential tumor marker for SCLC.

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Characterization of soluble forms of NCAM

Cited by 53 publications

References 15 publications

Metalloprotease‐induced ectodomain shedding of neural cell adhesion molecule (NCAM)

Metalloprotease‐induced ectodomain shedding of neural cell adhesion molecule (NCAM)

Zippers Make Signals: NCAM-mediated Molecular Interactions and Signal Transduction

Evaluation of serum neural cell adhesion molecule as a new tumor marker in small cell lung cancer

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