Link of a new type of apoptosis-inducing gene ASY/Nogo-B to human cancer

Li, Qin; Qi, Bing; Oka, Kiyomasa; Shimakage, Misuzu; Yoshioka, Naohisa; Inoue, Hirokazu; Hakura, Akira; Kodama, Ken; Stanbridge, Eric J.; Yutsudo, Masuo

doi:10.1038/sj.onc.1204536

Cited by 101 publications

(116 citation statements)

References 31 publications

Supporting

Mentioning

111

Contrasting

Unclassified

Order By: Relevance

“…Finally, it should be noted that the splice isoform Nogo-B recently has been shown to have proapoptotic activity, particularly in cancer cells, that is modulated by means of interactions with bcl-2 and bcl-xL (Tagami et al, 2000;Li et al, 2001). Mutant analysis has indicated that the apoptotic region resides in the second hydrophobic region and includes part of Nogo-66 (see Fig.…”

Section: What Is Nogo's Role In Development?mentioning

confidence: 99%

See 1 more Smart Citation

Nogo and Nogo‐66 receptor in human and chick: Implications for development and regeneration

O’Neill¹,

Whalley²,

Ferretti³

2004

Developmental Dynamics

View full text Add to dashboard Cite

Antibodies to the myelin protein Nogo increase axonal regrowth after central nervous system injury. We have investigated whether Nogo expression contributes to loss of regenerative potential during development by using chick embryos, which regenerate their spinal cord until embryonic day (E) 13, when myelination begins. We show that Nogo-A and the Nogo receptor (NgR) are developmentally regulated both in chick and human embryos, are first detected at developmental stages when the chick spinal cord regenerates, and are not down-regulated after injury at permissive stages for regeneration. Therefore, expression of Nogo-A and NgR in pre-E13 chick spinal cords is not sufficient to inhibit regeneration. Nogo-A expression in the chick early embryo is primarily observed in axons, whereas NgR is mainly located on neuronal cell bodies, both in spinal cord and eye, and in striated muscle including the heart. With the onset of myelination, there is down-regulation of Nogo-A expression in neurons. Therefore, loss of regenerative potential might be linked to changes in its cellular localization. The possibility that only Nogo expressed in mature oligodendrocytes can exercise inhibitory effects would reconcile the lack of inhibition we observe in developing chick spinal cords before the onset of myelination with evidence from other laboratories on the inhibitory effects of Nogo in mature central nervous system. The distinctive and complementary patterns of Nogo-A and NgR expression and their conservation throughout evolution support the view that Nogo signaling represents a key pathway in nervous system and striated muscle development. Its putative role in target innervation and establishment of neural circuitry is discussed.

show abstract

Section: What Is Nogo's Role In Development?mentioning

confidence: 99%

“…Schematic representation of the three Nogo isoforms. Location of the common Nogo-66 region is labeled, as is the region associated with promoting apoptosis in tumors (Li et al, 2001). The location of antigens recognized by the antibodies used in this study are indicated.…”

Section: Introductionmentioning

confidence: 99%

Nogo and Nogo‐66 receptor in human and chick: Implications for development and regeneration

O’Neill¹,

Whalley²,

Ferretti³

2004

Developmental Dynamics

View full text Add to dashboard Cite

show abstract

“…It is noteworthy that the second hydrophobic domain at NogoB C-terminus is important for apoptotic function of this protein [35]. As described above the different RTN isoforms share a C-terminal reticulon homology domain containing two hydrophobic segments and a 66-amino acid hydrophilic loop.…”

Section: Reticulons In Cell Deathmentioning

confidence: 90%

“…However, the ectopic expression of this RTN family member triggers extensive apoptosis in CGL4 and SaOS-2 cancer cell lines. Moreover, NogoB mRNA expression is abrogated in small cell lung cancer, suggesting a potential involvement in cancer development [35]. Additional studies indicate that NogoB overexpression causes ER stressmediated apoptosis accompanied by ER lumenal Ca 2+ depletion [36].…”

Section: Reticulons In Cell Deathmentioning

confidence: 97%

The reticulons: Guardians of the structure and function of the endoplasmic reticulum

Sano

Bernardoni

Piacentini

2012

Experimental Cell Research

View full text Add to dashboard Cite

The endoplasmic reticulum (ER) consists of the nuclear envelope and a peripheral network of tubules and membrane sheets. The tubules are shaped by a specific class of curvature stabilizing proteins, the reticulons and DP1; however it is still unclear how the sheets are assembled. The ER is the cellular compartment responsible for secretory and membrane protein synthesis. The reducing conditions of ER lead to the intra/inter-chain formation of new disulphide bonds into polypeptides during protein folding assessed by enzymatic or spontaneous reactions. Moreover, ER represents the main intracellular calcium storage site and it plays an important role in calcium signaling that impacts many cellular processes. Accordingly, the maintenance of ER function represents an essential condition for the cell, and ER morphology constitutes an important prerogative of it. Furthermore, it is well known that ER undergoes prominent shape transitions during events such as cell division and differentiation. Thus, maintaining the correct ER structure is an essential feature for cellular physiology. Now, it is known that proper ER-associated proteins play a fundamental role in ER tubules formation. Among these ER-shaping proteins are the reticulons (RTN), which are acquiring a relevant position. In fact, beyond the structural role of reticulons, in very recent years new and deeper functional implications of these proteins are emerging in relation to their involvement in several cellular processes.

show abstract

“…Domain analysis indicates that deletion of the Nogo-66 region results in a loss of ability to induce apoptosis. The transcription of Nogo-B was suppressed in lung carcinoma cell lines, indicating a possible role for Nogo-B in antitumorigenic activities (Li et al, 2001). …”

Section: Nogo-mediated Growth Inhibitionmentioning

confidence: 99%

Nogos and the Nogo‐66 receptor: Factors inhibiting CNS neuron regeneration

Tang

2002

J of Neuroscience Research

View full text Add to dashboard Cite

The recently cloned gene Nogo, whose alternative splice products correspond to the antigenic target of the central nervous system (CNS) regeneration enhancing monoclonal antibody IN-1, codes for membrane proteins enriched in brain, particularly in oligodendrocytes. The 66-amino acid extracellular domain of Nogo (Nogo-66) interacts with a high-affinity receptor (NgR), a glycosylphosphatidylinositol (GPI)-linked protein with multiple leucine-rich repeats. The amino terminal cytoplasmic domain of Nogo appears to have a general cellular growth inhibitory effect. Nogo-66, on the other hand, specifically retards neurite outgrowth and induces growth cone collapse, possibly through its interaction with NgR and as yet unidentified transmembrane coreceptors. Recent results also suggest that Nogo expression may induce apoptosis in tumor cells. Together, these proteins provide new molecular handles for the design of therapeutic interventions for CNS injuries and neurodegenerative diseases, as well as possible leads to anticancer strategies.

show abstract

Link of a new type of apoptosis-inducing gene ASY/Nogo-B to human cancer

Cited by 101 publications

References 31 publications

Nogo and Nogo‐66 receptor in human and chick: Implications for development and regeneration

Nogo and Nogo‐66 receptor in human and chick: Implications for development and regeneration

The reticulons: Guardians of the structure and function of the endoplasmic reticulum

Nogos and the Nogo‐66 receptor: Factors inhibiting CNS neuron regeneration

Contact Info

Product

Resources

About