Pathophysiological functions of semaphorins in the sympathetic nervous system

Mizuno, Yumiko; Nakanishi, Yoshimitsu; Kumanogoh, Atsushi

doi:10.1186/s41232-023-00281-7

Cited by 6 publications

(2 citation statements)

References 80 publications

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“… 6 Semaphorins are a family of membrane-bound and secreted proteins that are divided, in vertebrates, into five subfamilies from Sema3 to Sema7. 7 Semaphorins signal predominantly through receptor proteins of the plexin and neuropilin families and are implicated in numerous neuronal wiring events in the central and peripheral nervous system, 6 , 7 but little is known on their potential roles in the regulation of ENS neuronal network in health and disease.…”

Section: Introductionmentioning

confidence: 99%

The regulation of enteric neuron connectivity by semaphorin 5A is affected by the autism-associated S956G missense mutation

Le Dréan,

Le Berre-Scoul,

Paillé

et al. 2024

iScience

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Section: Introductionmentioning

confidence: 99%

The regulation of enteric neuron connectivity by semaphorin 5A is affected by the autism-associated S956G missense mutation

Le Dréan,

Le Berre-Scoul,

Paillé

et al. 2024

iScience

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“…As science and medicine start exploring the immune-muscle system interface, the Ig-domains appear central, with skeletal muscles expressing immunomodulatory molecules such as ICAM-1, ICOSL, CD80 or PD-L1 (Afzali et al 2018; Nelke et al 2019). It is also the case in the immune-nervous systems interface (Steinman 2004; Morimoto and Nakajima 2019; Dantzer 2018; Ren and Dubner 2010; Elenkov et al 2000; Salvador, de Lima, and Kipnis 2021; Mancusi and Monje 2023) and the neuroimmune cardiovascular interface where, for example, the parallel role of semaphorins in neurons and immune cells has become an intense field of research (Mohanta et al 2022; Yin et al 2022; Mizuno, Nakanishi, and Kumanogoh 2023).…”

Section: Introductionmentioning

confidence: 99%

A universal residue numbering scheme for the Immunoglobulin-fold (Ig-fold) to study Ig-Proteomes and Ig-Interactomes

Tawfeeq,

Wang,

Khaniya

et al. 2024

Preprint

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The Immunoglobulin fold (Ig-fold) is found in proteins from all domains of life and represents the most populous fold in the human genome, with current estimates ranging from 2 to 3% of protein coding regions. That proportion is much higher in the surfaceome where Ig and Ig-like domains orchestrate cell-cell recognition, adhesion and signaling. The ability of Ig-domains to reliably fold and self-assemble through highly specific interfaces represents a remarkable property of these domains, making them key elements of molecular interaction systems: the immune system, the nervous system, the vascular system and the muscular system. We define a universal residue numbering scheme, common to all domains sharing the Ig-fold in order to study the wide spectrum of Ig-domain variants constituting the Ig-proteome and Ig-Ig interactomes at the heart of thesesystems. The “IgStrand numbering scheme” enables the identification of Ig structural proteomes and interactomes in and between any species, and comparative structural, functional, and evolutionary analyses. We review how Ig-domains are classified today as topological and structural variants and highlight the“Ig-fold irreducible structural signature”shared by all of them. The IgStrand numbering scheme lays the foundation for the systematic annotation of structural proteomes by detecting and accurately labeling Ig-, Ig-like and Ig-extended domains in proteins, which are poorly annotated in current databases and opens the door to accurate machine learning. Importantly it sheds light on the robustIg protein folding algorithmused by nature to form beta sandwich supersecondary structures. The numbering scheme powers an algorithm implemented in the interactive structural analysis software iCn3D to systematically recognize Ig-domains, annotate them and perform detailed analyses comparing any domain sharing the Ig-fold in sequence, topology and structure, regardless of their diverse topologies. The scheme provides a robust fold detection and labeling mechanism that reveals unsuspected structural homologies among protein structures beyond currently identified Ig- and Ig-like domain variants. Indeed, multiple folds classified independently contain a common structural signature, in particular jelly-rolls. Examples of folds that harbor an “Ig-extended” architecture are given. Applications in protein engineering should be straightforward.

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Immune response to cold exposure: Role of γδ T cells and TLR2‐mediated inflammation

Vasek,

Holicek,

Galatik

et al. 2024

Eur J Immunol

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The mammalian body possesses remarkable adaptability to cold exposure, involving intricate adjustments in cellular metabolism, ultimately leading to thermogenesis. However, cold‐induced stress can impact immune response, primarily through noradrenaline‐mediated pathways. In our study, we utilized a rat model subjected to short‐term or long‐term mild cold exposure to investigate systemic immune response during the cold acclimation. To provide human relevance, we included a group of regular cold swimmers in our study. Our research revealed complex relationship between cold exposure, neural signaling, immune response, and thermogenic regulation. One‐day cold exposure triggered stress response, including cytokine production in white adipose tissue, subsequently activating brown adipose tissue, and inducing thermogenesis. We further studied systemic immune response, including the proportion of leukocytes and cytokines production. Interestingly, γδ T cells emerged as possible regulators in the broader systemic response, suggesting their possible contribution in the dynamic process of cold adaptation. We employed RNA‐seq to gain further insights into the mechanisms by which γδ T cells participate in the response to cold. Additionally, we challenged rats exposed to cold with the Toll‐like receptor 2 agonist, showing significant modulation of immune response. These findings significantly contribute to understanding of the physiological acclimation that occur in response to cold exposure.

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Pathophysiological functions of semaphorins in the sympathetic nervous system

Cited by 6 publications

References 80 publications

The regulation of enteric neuron connectivity by semaphorin 5A is affected by the autism-associated S956G missense mutation

The regulation of enteric neuron connectivity by semaphorin 5A is affected by the autism-associated S956G missense mutation

A universal residue numbering scheme for the Immunoglobulin-fold (Ig-fold) to study Ig-Proteomes and Ig-Interactomes

Immune response to cold exposure: Role of γδ T cells and TLR2‐mediated inflammation

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