Skin Injury Activates TRPV1+ Nociceptive Fibers to Stimulate a Rapid Innate Antiviral Protein Response

2020 ◽  
Author(s):  
Chelsea Handfield ◽  
Jeffery Kwock ◽  
Vivian Lei ◽  
Min Jin Lee ◽  
Margaret Coates ◽  
...  
Keyword(s):  
Antiviral Protein ◽  
Skin Injury ◽  
Nociceptive Fibers ◽  
Protein Response

Skin Injury Activates A Rapid TRPV1-dependent Antiviral Protein Response

2022 ◽  
Author(s):  
Vivian Lei ◽  
Chelsea Handfield ◽  
Jeffery T. Kwock ◽  
Stephen J. Kirchner ◽  
Min Jin Lee ◽  
...  
Keyword(s):  
Antiviral Protein ◽  
Skin Injury ◽  
Protein Response

scholarly journals Inhibition of protein glycosylation is a novel pro-angiogenic strategy that acts via activation of stress pathways

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Cuiling Zhong ◽  
Pin Li ◽  
Sulabha Argade ◽  
Lixian Liu ◽  
Anastasia Chilla’ ◽  
...  
Keyword(s):  
Therapeutic Strategy ◽  
Driving Forces ◽  
Mouse Skin ◽  
Protein Glycosylation ◽  
Skin Injury ◽  
Unfolded Protein ◽  
Injury Model ◽  
The Unfolded Protein Response ◽  
Protein Response ◽  
Jnk Activation

AbstractEndothelial cell (EC) metabolism is thought to be one of the driving forces for angiogenesis. Here we report the identification of the hexosamine D-mannosamine (ManN) as an EC mitogen and survival factor for bovine and human microvascular EC, with an additivity with VEGF. ManN inhibits glycosylation in ECs and induces significant changes in N-glycan and O-glycan profiles. We further demonstrate that ManN and two N-glycosylation inhibitors stimulate EC proliferation via both JNK activation and the unfolded protein response caused by ER stress. ManN results in enhanced angiogenesis in a mouse skin injury model. ManN also promotes angiogenesis in a mouse hindlimb ischemia model, with accelerated limb blood flow recovery compared to controls. In addition, intraocular injection of ManN induces retinal neovascularization. Therefore, activation of stress pathways following inhibition of protein glycosylation can promote EC proliferation and angiogenesis and may represent a therapeutic strategy for treatment of ischemic disorders.

scholarly journals 1401 Activation of nociceptive fibers following acute skin injury triggers innate antiviral immunity

2018 ◽  
Vol 138 (5) ◽  
pp. S238
Author(s):  
C. Handfield ◽  
J. Kwock ◽  
P. Hoang ◽  
J. Suwanpradid ◽  
Q. Han ◽  
...  
Keyword(s):  
Antiviral Immunity ◽  
Skin Injury ◽  
Nociceptive Fibers ◽  
Innate Antiviral Immunity

scholarly journals 663 Activation of Trpv1+ nociceptive fibers stimulates an innate antiviral immune response following skin injury

2019 ◽  
Vol 139 (5) ◽  
pp. S114
Author(s):  
C. Handfield ◽  
J. Kwock ◽  
P. Hoang ◽  
A.S. MacLeod
Keyword(s):  
Immune Response ◽  
Skin Injury ◽  
Antiviral Immune Response ◽  
Nociceptive Fibers

Stability of papain – pectin system under high pressure and its application for treatment of skin injury

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
KM Gregorio-Jáuregui ◽  
JC Cano-Cabrera ◽  
EP Segura-Ceniceros ◽  
JL Martínez-Hernández ◽  
A Ilyina
Keyword(s):  
High Pressure ◽  
Skin Injury

Unfolded protein response pathway, IRE1[alpha]-XBP1 is altered during adipogenesis in obese human adipocytes

2013 ◽  
pp. 1-1
Author(s):  
Philip Voyias ◽  
Ciara McCarthy ◽  
Adaikala Antonysunil ◽  
Warunee Kumsaiyai ◽  
Alison Harte ◽  
...  
Keyword(s):  
Unfolded Protein Response ◽  
Human Adipocytes ◽  
Unfolded Protein ◽  
Obese Human ◽  
Protein Response

Oestrogen-driven changes in the bovine uterus are associated with activation of the unfolded protein response

2014 ◽  
Author(s):  
Mohammed A Alfattah ◽  
Paul Anthony McGettigan ◽  
John Arthur Browne ◽  
Khalid M Alkhodair ◽  
Katarzyna Pluta ◽  
...  
Keyword(s):  
Unfolded Protein Response ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

Native Ubiquitin Structural Changes Resulting from Complexation with β-methylamino-L-alanine (BMAA)

2020 ◽  
Author(s):  
Katie Mae Wilson ◽  
Aurora Burkus-Matesevac ◽  
Samuel Maddox ◽  
Christopher Chouinard
Keyword(s):  
Structural Changes ◽  
Noncovalent Complex ◽  
Unfolded Protein ◽  
Protein Size ◽  
High Concentrations ◽  
The Unfolded Protein Response ◽  
Critical Binding ◽  
Protein Response ◽  
The Brain ◽  
Lateral Sclerosis

β-methylamino-L-alanine (BMAA) has been linked to the development of neurodegenerative (ND) symptoms following chronic environmental exposure through water and dietary sources. The brains of those affected by this condition, often referred to as amyotrophic lateral sclerosis-parkinsonism-dementia complex (ALS-PDC), have exhibited the presence of plaques and neurofibrillary tangles (NFTs) from protein aggregation. Although numerous studies have sought to better understand the correlation between BMAA exposure and onset of ND symptoms, no definitive link has been identified. One prevailing hypothesis is that BMAA acts a small molecule ligand, complexing with critical proteins in the brain and reducing their function. The objective of this research was to investigate the effects of BMAA exposure on the native structure of ubiquitin. We hypothesized that formation of a Ubiquitin+BMAA noncovalent complex would alter the protein’s structure and folding and ultimately affect the ubiquitinproteasome system (UPS) and the unfolded protein response (UPR). Ion mobility-mass spectrometry revealed that at sufficiently high concentrations BMAA did in fact form a noncovalent complex with ubiquitin, however similar complexes were identified for a range of additional amino acids. Collision induced unfolding (CIU) was used to interrogate the unfolding dynamics of native ubiquitin and these Ubq-amino acid complexes and it was determined that complexation with BMAA led to a significant alteration in native protein size and conformation, and this complex required considerably more energy to unfold. This indicates that the complex remains more stable under native conditions and this may indicate that BMAA has attached to a critical binding location.

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