Identification and Regulation of Reticulon 4B (Nogo-B) in Renal Tubular Epithelial Cells

Marin, Ethan P.; Moeckel, Gilbert; Al‐Lamki, Rafia S.; Bradley, John R.; Yan, Qingshang; Wang, Tong; Wright, Paulette L.; Sessa, William C.

doi:10.2353/ajpath.2010.100199

Cited by 17 publications

(10 citation statements)

References 33 publications

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“…Marin et al have demonstrated a dramatic delay in the recruitment of macrophages in Nogo-B-disrupted mice in vivo , consistent with the findings of Schanda et al that Nogo-B deficiency is associated with reduced promotion of macrophage homing and functional recovery [17, 19]. Thus, it has been suggested that endogenous Nogo-B may be implicated in the control of macrophage activities and trafficking [20].…”

Section: Introductionsupporting

confidence: 61%

Nogo-B Facilitates LPS-Mediated Immune Responses by Up-Regulation of TLR4-Signaling in Macrophage RAW264.7

Zhu

Tong

Jia

et al. 2017

Cell Physiol Biochem

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Background/Aims: Nogo-B, a member of the reticulon family of proteins, is mainly located in the endoplasmic reticulum (ER). Here, we investigate the function and mechanism of Nogo-B in the regulation of TLR4-associated immune responses in the macrophage cell line of RAW264.7. Methods: Nogo-B was up- and down-regulated through the use of appropriate adenoviral vectors or siRNA, and the effects of Nogo-B on macrophages under liposaccharide (LPS) stimulation were evaluated via western blotting, immunofluorescence, enzyme-linked immunosorbent assay (ELISA), flow cytometric analysis, and transwell assay. Results: Our data indicates that the protein of Nogo-B was down-regulated in a time- and dose-dependent manner following LPS administration in the macrophage. Nogo-B overexpression increased the production of inflammatory cytokines (MCP-1, TNF-α, IL-1β, and TGF-β), enhanced macrophage migration activities, activated major histocompatibility complex II (MHC II), and elevated the expression of macrophage scavenger receptor 1(MSR1), all of which suggest that Nogo-B is necessary for immune responses and plays an important role in regulating macrophage recruitment. Mechanistically, Nogo-B may enhance TLR4 expression in macrophage surfaces, activate mitogen-activated protein kinase (MAPK) pathways, and initiate inflammatory responses. Conclusion: These findings illustrate the key regulatory functions of Nogo-B in facilitating LPS-mediated immune responses through promoting the phosphorylation of MAP kinase.

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Section: Introductionsupporting

confidence: 61%

Nogo-B Facilitates LPS-Mediated Immune Responses by Up-Regulation of TLR4-Signaling in Macrophage RAW264.7

Zhu

Tong

Jia

et al. 2017

Cell Physiol Biochem

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“…(Marin et al. ) reported that Nogo‐B mRNA and protein were dramatically upregulated in renal proximal tubule epithelial cells following unilateral ureteral obstruction. We found a similar large increase in Nogo‐B mRNA in the kidneys of mice treated with Urografin (Fig.…”

Section: Discussionmentioning

confidence: 99%

Pituitary adenylate cyclase-activating polypeptide prevents contrast-induced nephropathy in a novel mouse model

Khan

Maderdrut

et al. 2013

Physiol Rep

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We determined whether pituitary adenylate cyclase-activating polypeptide 38 (PACAP38) prevents contrast-induced nephropathy using human renal proximal tubule epithelial (HK-2) cells and homozygous endothelial nitric oxide synthase-deficient (eNOS−/−) mice as a novel in vivo model. Cultured HK-2 cells were pretreated with 10−9–10−6 mol/L PACAP or vasoactive intestinal peptide (VIP) for 1 h, and then exposed to ionic (Urografin) or nonionic (iohexol) contrast media at 50 mg iodine/mL for 24 h. Male eNOS−/− mice received Urografin (1.85 g iodine/kg) intravenously after water deprivation for 24 h, and PACAP38 (10 μg) intraperitoneally 1 h before and 12 h after Urografin injection. Urografin and iohexol increased lactate dehydrogenase and kidney injury molecule 1 in the culture medium, induced apoptosis, and inhibited cell proliferation in HK-2 cell cultures. PACAP38 and VIP reduced these changes in a dose-dependent manner. PACAP38 was more potent than VIP. In eNOS−/− mice, Urografin raised serum creatinine and cystatin C levels, caused renal tubule damage, induced apoptosis, and promoted neutrophil influx. Urografin also increased kidney protein levels of proinflammatory cytokines, and kidney mRNA levels of proinflammatory cytokines, kidney injury biomarkers, and enzymes responsible for reactive oxygen and nitrogen species. PACAP38 significantly reduced these Urografin-induced changes in eNOS−/− mice. This study shows that both Urografin and iohexol are toxic to HK-2 cells, but Urografin is more toxic than iohexol. Urografin causes acute kidney injury in eNOS−/− mice. PACAP38 protects HK-2 cells and mouse kidneys from contrast media and is a potential therapeutic agent for contrast-induced nephropathy.

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“…RNA isolation, reverse transcription, and quantitative PCR was performed as described 26 , except that GAPDH was used for normalization of transcript abundance. …”

Section: Methodsmentioning

confidence: 99%

Endothelial Cell Palmitoylproteomic Identifies Novel Lipid-Modified Targets and Potential Substrates for Protein Acyl Transferases

Marin

Derakhshan²,

Lam³

et al. 2012

Circulation Research

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Rationale Protein S-palmitoylation is the post-translational attachment of a saturated 16-carbon palmitic acid to a cysteine side chain via a thioester bond. Palmitoylation can affect protein localization, trafficking, stability, and function. The extent and roles of palmitoylation in endothelial cell (EC) biology is not well understood, in part due to technological limits on palmitoylprotein detection. Objective To develop a method using acyl-biotinyl exchange (ABE) technology coupled with mass spectrometry to globally isolate and identify palmitoylproteins in EC. Methods and Results More than 150 putative palmitoyl proteins were identified in EC using ABE and mass spectrometry. Among the novel palmitoylproteins identified is superoxide dismutase 1 (SOD1), an intensively studied enzyme that protects all cells from oxidative damage. Mutation of cysteine 6 prevents palmitoylation, leads to reduction in SOD1 activity in vivo and in vitro, and inhibits nuclear localization, thereby supporting a functional role for SOD1 palmitoylation. Moreover, we used ABE to search for substrates of particular protein acyl transferases in EC. We found that palmitoylation of the cell adhesion protein PECAM1 is dependent on the protein acyl transferase ZDHHC21. We show that knockdown of ZDHHC21 leads to reduced levels of PECAM1 at the cell surface. Conclusions Our data demonstrate the utility of EC palmitoylproteomics to reveal new insights into the role of this important post-translational lipid modification in EC biology.

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Identification and Regulation of Reticulon 4B (Nogo-B) in Renal Tubular Epithelial Cells

Cited by 17 publications

References 33 publications

Nogo-B Facilitates LPS-Mediated Immune Responses by Up-Regulation of TLR4-Signaling in Macrophage RAW264.7

Nogo-B Facilitates LPS-Mediated Immune Responses by Up-Regulation of TLR4-Signaling in Macrophage RAW264.7

Pituitary adenylate cyclase-activating polypeptide prevents contrast-induced nephropathy in a novel mouse model

Endothelial Cell Palmitoylproteomic Identifies Novel Lipid-Modified Targets and Potential Substrates for Protein Acyl Transferases

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