Role of neuropilin-2 in the immune system

Schellenburg, Samuel; Schulz, Alexander; Poitz, David M.; Muders, Michael H.

doi:10.1016/j.molimm.2017.08.010

Cited by 53 publications

(43 citation statements)

References 39 publications

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“…The other protein in this cluster, neuropilin-2, showed a significantly higher abundance at day 56 compared to days 14–21 ( Figure 4B ). Neuropilin-2 is a transmembrane glycoprotein that is abundantly expressed in immune cells, and supports multiple immune functions, including antigen presentation ( 52 , 53 ).…”

Section: Resultsmentioning

confidence: 99%

Plasma Proteome Responses in Salmonid Fish Following Immunization

et al. 2020

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Vaccination plays a critical role in the protection of humans and other animals from infectious diseases. However, the same vaccine often confers different protection levels among individuals due to variation in genetics and/or immunological histories. While this represents a well-recognized issue in humans, it has received little attention in fish. Here we address this knowledge gap in a proteomic study of rainbow trout ( Oncorhynchus mykiss , Walbaum), using non-lethal repeated blood sampling to establish the plasma protein response of individual fish following immunization. Six trout were immunized with adjuvanted hen egg-white lysozyme (HEL) and peripheral blood sampled at ten time points from day 0 to day 84 post-injection. We confirm that an antigen-specific antibody response to HEL was raised, showing differences in timing and magnitude among individuals. Using label-free liquid chromatography-mass spectrometry, we quantified the abundance of 278 plasma proteins across the timecourse. As part of the analysis, we show that this approach can distinguish many (but not all) duplicated plasma proteins encoded by paralogous genes retained from the salmonid-specific whole genome duplication event. Global variation in the plasma proteome was predominantly explained by individual differences among fish. However, sampling day explained a major component of variation in abundance for a statistically defined subset of 41 proteins, representing 15% of those detected. These proteins clustered into five groups showing distinct temporal responses to HEL immunization at the population level, and include classical immune (e.g. complement system members) and acute phase molecules (e.g. apolipoproteins, haptoglobins), several enzymes and other proteins supporting the immune response, in addition to evolutionarily conserved molecules that are as yet uncharacterized. Overall, this study improves our understanding of the fish plasma proteome, provides valuable marker proteins for different phases of the immune response, and has implications for vaccine development and the design of immune challenge experiments.

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Section: Resultsmentioning

confidence: 99%

Plasma Proteome Responses in Salmonid Fish Following Immunization

et al. 2020

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“…Since SEMA3s compete with VEGF for NRP binding, treatment with SEMA3s may enhance anti-tumor activity by impairing Treg infiltration induced by VEGF. However, the functions of NRP2 in immune systems are poorly understood ( Roy et al, 2017 ; Schellenburg et al, 2017 ). Further studies are needed to identify the effect of SEMA3F as an immune modulator.…”

Section: Introductionmentioning

confidence: 99%

Semaphorin 3F and Netrin-1: The Novel Function as a Regulator of Tumor Microenvironment

et al. 2018

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Axon guidance molecules play an important role in regulating proper neuronal networking during neuronal development. They also have non-neuronal properties, which include angiogenesis, inflammation, and tumor development. Semaphorin 3F (SEMA3F), a member of the class 3 semaphorins, was initially identified as an axon guidance factor, that repels axons and collapses growth cones. However, SEMA3F has similar effects on endothelial cells (ECs) and tumor cells. In this review, we discuss the novel molecular mechanisms underlying SEMA3F activity in vascular and tumor biology. Recent evidence suggests that SEMA3F functions as a PI3K-Akt-mTOR inhibitor in mammalian cells, including T cells, ECs, and tumor cells. Therefore, SEMA3F may have broad therapeutic implications. We also discuss the key role of axon guidance molecules as regulators of the tumor microenvironment. Netrin-1, a chemoattractant factor in the neuronal system, promotes tumor progression by enhancing angiogenesis and metastasis. Moreover, our recent studies demonstrate that netrin-1/neogenin interactions augment CD4+ T cell chemokinesis and elicit pro-inflammatory responses, suggesting that netrin-1 plays a key role in modulating the function of a tumor and its surrounding cells in the tumor microenvironment. Overall, this review focuses on SEMA3F and netrin-1 signaling mechanisms to understand the diverse biological functions of axon guidance molecules.

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“…The receptor of VEGF-C includes VEGF receptor-2 (VEGFR-2), VEGFR-3, and neuropilin (NRP-2). 14,16,17 Studies have confirmed that NRP-2 expression is associated with metastasis and a poor prognosis in a great majority of tumours. Besides lymphangiogenesis, VEGF-C is also involved in promoting cell survival under stress in many cell types.…”

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confidence: 97%

“…13 They are mainly expressed in neuronal tissues, several muscles, kidney, lung, some immune cells, various cancer tissue, and cancer cell lines. 14,16,17 Studies have confirmed that NRP-2 expression is associated with metastasis and a poor prognosis in a great majority of tumours. [18][19][20][21] In kidney, increased tubular and interstitial NRP-2 expression was observed in renal biopsy tissues from FSGS patients with various degrees of tubulointerstitial fibrosis.…”

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confidence: 97%

Roles for VEGF‐C/NRP–2 axis in regulating renal tubular epithelial cell survival and autophagy during serum deprivation

Chang

Yang

Zhang

et al. 2019

Cell Biochemistry & Function

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Vascular endothelial growth factor C (VEGF‐C) is an angiogenic and lymphangiogenic growth factor. Recent research has revealed the role for VEGF‐C in regulating autophagy by interacting with a nontyrosine kinase receptor, neuropilin‐2 (NRP–2). However, whether VEGF‐C participates in regulating cell survival and autophagy in renal proximal tubular cells is unknown. To address this question, we employed a cell modal of serum deprivation to verify the role of VEGF‐C and its receptor NRP–2 in regulating cell survival and autophagy in NRK52E cell lines. The results show that VEGF‐C rescued the loss of cell viability induced by serum deprivation in a concentration‐dependent manner. Furthermore, endogenous VEGF‐C was knocked down in NRK52E cells by using specific small‐interfering RNAs (siRNA), cells were more sensitive to serum deprivation–induced cell death. A similar increase in cell death rate was observed following NRP–2 depletion in serum‐starved NRK52E cells. Autophagy activity in serum‐starved NRK52E cells was confirmed by western blot analysis of microtubule‐associated protein‐1 chain 3 (LC3), immunofluorescence staining of endogenous LC3, and the formation of autophagosomes by electron microscopy. VEGF‐C or NRP–2 depletion further increased LC3 expression induced by serum deprivation, suggesting that VEGF‐C and NRP–2 were involved in controlling autophagy in NRK52E cells. We further performed autophagic flux experiments to identify that VEGF‐C promotes the activation of autophagy in serum‐starved NRK52E cells. Together, these results suggest for the first time that VEGF‐C/NRP–2 axis promotes survival and autophagy in NRK52E cells under serum deprivation condition. Significance of the study More researchers had focused on the regulation of autophagy in kidney disease. The effect of VEGF‐C on cell death and autophagy in renal epithelial cells has not been examined. We first identified the VEGF‐C as a regulator of cell survival and autophagy in NRK52E cell lines. And VEGF‐C/NRP–2 may mediate autophagy by regulating the phosphorylation of 4EBP1 and P70S6K. VEGF‐C treatment may be identified as a therapeutic target in renal injury repair due to its capacity to promote tubular cell survival in the future.

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Role of neuropilin-2 in the immune system

Cited by 53 publications

References 39 publications

Plasma Proteome Responses in Salmonid Fish Following Immunization

Plasma Proteome Responses in Salmonid Fish Following Immunization

Semaphorin 3F and Netrin-1: The Novel Function as a Regulator of Tumor Microenvironment

Roles for VEGF‐C/NRP–2 axis in regulating renal tubular epithelial cell survival and autophagy during serum deprivation

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