The Human Homologue of theninjurinGene Maps to the Candidate Region of Hereditary Sensory Neuropathy Type I (HSNI)

Chadwick, Brian P.; Heath, S; Williamson, Jon; Obermayr, Franz; Patel, Lisa; Sheer, Denise; Frischauf, Anna‐Maria

doi:10.1006/geno.1997.5084

Cited by 14 publications

(8 citation statements)

References 22 publications

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“…Chadwick et al [] reported that an N ‐glycosylation motif of Ninj1 is conserved in rodents and humans, and we further found that the N ‐glycosylation motif is highly conserved in vertebrates (Table ). To determine whether Ninj1 is N ‐glycosylated in situ, we cultured BMMs with tunicamycin, a GlcNAc transferase inhibitor that prevents N ‐glycosylation.…”

Section: Resultssupporting

confidence: 67%

Ninjurin1 Assembles Into a Homomeric Protein Complex Maintained byN-linked Glycosylation

et al. 2017

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Ninjurin1 (Ninj1) is a cell surface protein known as a homophilic adhesion molecule. Previous studies have shown a trans-interaction of Ninj1 between immune cells and endothelial cells; however, little is known about Ninj1 modification and structure in the cis-interaction. We showed that Ninj1 assembles into a homomeric complex via a cis-interaction mediated by the intracellular region and N-glycosylation at Asn . We identified cis-interaction between Ninj1 proteins using CFP- and YFP-tagged Ninj1 by Förster resonance energy transfer using a confocal microscope and fluorescence-activated cell sorter. We further observed the Ninj1 homomeric complexes composed of two to six monomeric Ninj1 molecules by a formaldehyde cross-linking assay. Co-immunoprecipitation assays with epitope-tagged truncated Ninj1 suggested that the intracellular region encompassing Leu -Ala participates in Ninj1 homomer assembly. Ninj1 N-glycosylation was characterized by treatment of tunicamycin and substitution of Asn to Gln or Ala. Fluorescence-activated cell sorting-based Förster resonance energy transfer assays further demonstrated that N-glycosylation is indispensable for the Ninj1 cis-interaction, and a formaldehyde cross-linking assay confirmed that interruption of N-glycosylation by Asn substitution disrupted Ninj1 homomeric complex formation. In silico analysis revealed that Ninj1 is highly conserved in vertebrates and that the conserved sequence contains an N-glycosylation motif and cis-interacting intracellular region, which participate in Ninj1 homomer assembly. Taken together, these data show that Ninj1 assembles into a homomeric protein complex and that N-glycosylation is a prerequisite for Ninj1 homomer assembly. J. Cell. Biochem. 118: 2219-2230, 2017. © 2017 Wiley Periodicals, Inc.

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Section: Resultssupporting

confidence: 67%

Ninjurin1 Assembles Into a Homomeric Protein Complex Maintained byN-linked Glycosylation

et al. 2017

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“…Ninj1 is located on the plasma membrane, can mediate homophilic adhesion and is involved in nerve regeneration . Ninj1 is also predominantly expressed in a number of other tissues originating from epithelial cells ( e.g ., lung, liver, kidney, brain, thymus and adrenal gland) . A recent study indicated that elevated Ninj1 level was associated with human cancer ( e.g ., liver, lung, colon and breast cancer cells) …”

Section: Discussionmentioning

confidence: 99%

Ninjurin1 suppresses metastatic property of lung cancer cells through inhibition of interleukin 6 signaling pathway

Jang

Kang

Woo

et al. 2016

Intl Journal of Cancer

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Nerve injury-induced protein 1 (Ninjurin1, Ninj1) is a cell surface molecule that can mediate homophilic adhesion and promote neurite outgrowth from cultured dorsal root ganglion (DRG) neurons. Interestingly, Ninj1 overexpressed in human cancer; however, its role in metastasis is not clear. This study showed that inhibition of Ninj1 promotes lung cancer metastasis through interleukin 6 (IL-6)/STAT3 signaling. Ninj1 levels were relatively low in highly motile lung cancer cells. While inhibition of Ninj1 enhanced cell migration in lung cancer cells, overexpression of Ninj1 significantly suppressed it. We found that inhibition of Ninj1 significantly increased expression and secretion of IL-6 in A549 cells. We also found that inhibition of IL-6 decreased intercellular adhesion molecule 1 (ICAM-1) expression. In addition, inhibition of Ninj1 significantly increased cell motility and invasiveness of lung cancer cells. In an in vivo model, we found that Ninj1 suppression did not affect tumor growth but induced significant increase in incidence of lung metastasis, and sizes and number of tumor nodules. Taken together, our data clearly demonstrate that Ninj1 suppresses migration, invasion and metastasis of lung cancer via inhibition of the IL-6 signaling pathway in vitro and in vivo.

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“…In addition, ninjurin1 is ubiquitously expressed in various human tissues originating from epithelial cells (e.g. liver, kidney, thymus, adrenal gland) [3]. However, the biological relevance of ninjurin1 on tissues other than the nervous system remains unknown.…”

Section: Introductionmentioning

confidence: 99%

Ninjurin1 increases p21 expression and induces cellular senescence in human hepatoma cells

Toyama

Sasaki

Horimoto

et al. 2004

Journal of Hepatology

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The Human Homologue of theninjurinGene Maps to the Candidate Region of Hereditary Sensory Neuropathy Type I (HSNI)

Cited by 14 publications

References 22 publications

Ninjurin1 Assembles Into a Homomeric Protein Complex Maintained byN-linked Glycosylation

Ninjurin1 Assembles Into a Homomeric Protein Complex Maintained byN-linked Glycosylation

Ninjurin1 suppresses metastatic property of lung cancer cells through inhibition of interleukin 6 signaling pathway

Ninjurin1 increases p21 expression and induces cellular senescence in human hepatoma cells

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