Netrin Family: Role for Protein Isoforms in Cancer

Bruikman, Caroline S.; Zhang, Huayu; Kemper, Anneli Maite; Gils, Janine M. van

doi:10.1155/2019/3947123

Cited by 31 publications

(26 citation statements)

References 92 publications

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“…The V2 domain of netrin-1 binds to the Ig1/Ig2 domain of Unc5B, which can bind and compete with FLRT proteins (other Unc5 ligands; Figure 1B ) ( Shirakawa et al, 2019 ). The different patterns of binding to receptors likely contribute to the variety of netrin functions, such as cell migration, axon branching, synaptogenesis, oligodendrocyte differentiation, angiogenesis, lymphangiogenesis, immune function, and tumor progression ( Rajasekharan and Kennedy, 2009 ; Larrieu-Lahargue et al, 2011 ; Finci et al, 2015 ; Feinstein and Ramkhelawon, 2017 ; Bruikman et al, 2019 ; Meijers et al, 2020 ).…”

Section: Netrin Family Proteinsmentioning

confidence: 99%

Involvement of Netrins and Their Receptors in Neuronal Migration in the Cerebral Cortex

Yamagishi

Bandô

Sato

2021

Front. Cell Dev. Biol.

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In mammals, excitatory cortical neurons develop from the proliferative epithelium and progenitor cells in the ventricular zone and subventricular zone, and migrate radially to the cortical plate, whereas inhibitory GABAergic interneurons are born in the ganglionic eminence and migrate tangentially. The migration of newly born cortical neurons is tightly regulated by both extracellular and intracellular signaling to ensure proper positioning and projections. Non-cell-autonomous extracellular molecules, such as growth factors, axon guidance molecules, extracellular matrix, and other ligands, play a role in cortical migration, either by acting as attractants or repellents. In this article, we review the guidance molecules that act as cell–cell recognition molecules for the regulation of neuronal migration, with a focus on netrin family proteins, their receptors, and related molecules, including neogenin, repulsive guidance molecules (RGMs), Down syndrome cell adhesion molecule (DSCAM), fibronectin leucine-rich repeat transmembrane proteins (FLRTs), and draxin. Netrin proteins induce attractive and repulsive signals depending on their receptors. For example, binding of netrin-1 to deleted in colorectal cancer (DCC), possibly together with Unc5, repels migrating GABAergic neurons from the ventricular zone of the ganglionic eminence, whereas binding to α3β1 integrin promotes cortical interneuron migration. Human genetic disorders associated with these and related guidance molecules, such as congenital mirror movements, schizophrenia, and bipolar disorder, are also discussed.

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Section: Netrin Family Proteinsmentioning

confidence: 99%

Involvement of Netrins and Their Receptors in Neuronal Migration in the Cerebral Cortex

Yamagishi

Bandô

Sato

2021

Front. Cell Dev. Biol.

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“…[23][24] Moreover, netrin domains are involved in diverse processes from axonal guidance, morphogenesis and angiogenesis by regulating cell migration and survival. 25 Recombinant Ac-AIP-2 was demonstrated to bind to mesenteric CD103+ dendritic cells and drive expansion of regulatory T cells (Tregs) that suppressed inducible asthma in mice and down regulated the expression of co-stimulatory markers on human peripheral blood dendritic cells from asthmatic subjects. 13 The homologous Ac-AIP-1 protein was subsequently shown in recombinant form to suppress proinflammatory responses in the TNBS model of chemically-induced murine colitis.…”

Section: Introductionmentioning

confidence: 99%

A netrin domain-containing protein secreted by the human hookworm Necator americanus protects against CD4 T cell transfer colitis

Buitrago

Pickering

Ruscher

et al. 2021

Translational Research

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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“…Netrin-4, in contrast, which arose independently from β laminin ancestors [ 23 , 25 ], appears to be functionally distinct in that it can disrupt LM networks via competition of LM ternary nodes [ 28 ], with implications for directed cell migration during angiogenesis and neurogenesis [ 29 – 35 ]. LMs and netrins are known to play context-specific roles across a range of tissues types, with local expression patterns and abundance providing valuable clues to functionality, as reviewed in [ 2 – 4 , 13 , 22 , 24 , 26 , 36 – 41 ]. However, the equivalent expression and distribution of LaNt α31 protein have not been determined.…”

Section: Introductionmentioning

confidence: 99%

Laminin N-terminus α31 protein distribution in adult human tissues

et al. 2020

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Laminin N-terminus α31 (LaNt α31) is a netrin-like protein derived from alternative splicing of the laminin α3 gene. Although LaNt α31 has been demonstrated to influence corneal and skin epithelial cell function, its expression has not been investigated beyond these tissues. In this study, we used immunohistochemistry to characterise the distribution of this protein in a wide-array of human tissue sections in comparison to laminin α3. The data revealed widespread LaNt α31 expression. In epithelial tissue, LaNt α31 was present in the basal layer of the epidermis, throughout the epithelium of the digestive tract, and in much of the epithelium of the reproductive system. LaNt α31 was also found throughout the vasculature of most tissues, with enrichment in reticular-like fibres in the extracellular matrix surrounding large vessels. A similar matrix pattern was observed around the terminal ducts in the breast and around the alveolar epithelium in the lung, where basement membrane staining was also evident. Specific enrichment of LaNt α31 was identified in sub-populations of cells of the kidney, liver, pancreas, and spleen, with variations in intensity between different cell types in the collecting ducts and glomeruli of the kidney. Intriguingly, LaNt α31 immunoreactivity was also evident in neurons of the central nervous system, in the cerebellum, cerebral cortex, and spinal cord. Together these findings suggest that LaNt α31 may be functionally relevant in a wider range of tissue contexts than previously anticipated, and the data provides a valuable basis for investigation into this interesting protein.

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Netrin Family: Role for Protein Isoforms in Cancer

Cited by 31 publications

References 92 publications

Involvement of Netrins and Their Receptors in Neuronal Migration in the Cerebral Cortex

Involvement of Netrins and Their Receptors in Neuronal Migration in the Cerebral Cortex

A netrin domain-containing protein secreted by the human hookworm Necator americanus protects against CD4 T cell transfer colitis

Laminin N-terminus α31 protein distribution in adult human tissues

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