Ac2-26 peptide and serine protease of Bothrops atrox similarly induces angiogenesis without triggering local and systemic inflammation in a murine model of dorsal skinfold chamber

Molás, Rafaela Batista; Paula-Silva, Marina de; Masood, Rehana; Ullah, Anwar; Gimenes, Alexandre Dantas; Oliani, Sônia Maria

doi:10.1016/j.toxicon.2017.06.009

Cited by 7 publications

(5 citation statements)

References 38 publications

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“…Recent studies have investigated ANXA1 in different models of inflammation [13,[48][49][50][51], including placentas from high-risk pregnancies, such as those associated with Toxoplasma gondii [52] and Zika virus (ZIKV) infections [53] (Figure 1).…”

Section: Anxa1 In the Placentamentioning

confidence: 99%

ANNEXIN A1: Roles in Placenta, Cell Survival, and Nucleus

Sousa

Santos

Teixeira

et al. 2022

Cells

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The unbiased approaches of the last decade have enabled the collection of new data on the biology of annexin A1 (ANXA1) in a variety of scientific aspects, creating opportunities for new biomarkers and/or therapeutic purposes. ANXA1 is found in the plasma membrane, cytoplasm, and nucleus, being described at low levels in the nuclear and cytoplasmic compartments of placental cells related to gestational diabetic diseases, and its translocation from the cytoplasm to the nucleus has been associated with a response to DNA damage. The approaches presented here open pathways for reflection upon, and intrinsic clarification of, the modulating action of this protein in the response to genetic material damage, as well as its level of expression and cellular localization. The objective of this study is to arouse interest, with an emphasis on the mechanisms of nuclear translocation of ANXA1, which remain underexplored and may be beneficial in new inflammatory therapies.

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Section: Anxa1 In the Placentamentioning

confidence: 99%

ANNEXIN A1: Roles in Placenta, Cell Survival, and Nucleus

Sousa

Santos

Teixeira

et al. 2022

Cells

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“…The endogenous ANXA1 expression was analyzed (Axioskop 2-Mot Plus Zeiss microscope, Carl Zeiss, Jena, Germany), using Axio Vision software [26] and expressed as value of the mean optical density (MOD) in immunoreactive areas. The values were obtained as arbitrary units (a.u.)…”

Section: Densitometry Analysismentioning

confidence: 99%

“…Annexin A1 (ANXA1) is an endogenous anti-inflammatory molecule expressed by mast cells, neutrophils, eosinophils, monocytes, epithelial T cells that can modulate biological events in cancer progression and metastasis and in various models of inflammatory and autoimmune diseases [20][21][22][23][24][25][26]. ANXA1 is a member of the annexin superfamily of calcium-and phospholipid-binding proteins that participates in chronic inflammation, leukocyte migration, tissue growth and apoptosis [27,28].…”

Section: Introductionmentioning

confidence: 99%

Mast cell heterogeneity and anti-inflammatory annexin A1 expression in leprosy skin lesions

Costa

Mimura

Freitas

et al. 2018

Microbial Pathogenesis

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Mast cells (MCs) have important immunoregulatory roles in skin inflammation. Annexin A1 (ANXA1) is an endogenous anti-inflammatory protein that can be expressed by mast cells, neutrophils, eosinophils, monocytes, epithelial and T cells. This study investigated MCs heterogeneity and ANXA1 expression in human dermatoses with special emphasis in leprosy. Sixty one skin biopsies from 2 groups were investigated: 40 newly diagnosed untreated leprosy patients (18 reaction-free, 11 type 1 reaction/T1R, 11 type 2 reaction/T2R); 21 patients with other dermatoses. Tryptase/try+ and chymase/chy + phenotypic markers and toluidine blue stained intact/degranulated MC counts/mm were evaluated. Try/chy MCs and ANXA1 were identified by streptavidin-biotin-peroxidase immunostaining and density was reported. In leprosy, degranulated MCs outnumbered intact ones regardless of the leprosy form (from tuberculoid/TT to lepromatous/LL), leprosy reactions (reactional/reaction-free) and type of reaction (T1R/T2R). Compared to other dermatoses, leprosy skin lesions showed lower numbers of degranulated and intact MCs. Try MCs outnumbered chy in leprosy lesions (reaction-free/reactional, particularly in T2R), but not in other dermatoses. Compared to other dermatoses, ANXA1 expression, which is also expressed in mast cells, was higher in the epidermis of leprosy skin lesions, independently of reactional episode. In leprosy, higher MC degranulation and differential expression of try/chy subsets independent of leprosy type and reaction suggest that the Mycobacterium leprae infection itself dictates the inflammatory MCs activation in skin lesions. Higher expression of ANXA1 in leprosy suggests its potential anti-inflammatory role to maintain homeostasis preventing tissue and nerve damage.

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“…Several studies reported that Ac2‐26 could inhibit tumor necrosis factor alpha (TNF‐α) production in monocytes and promote phagocytosis of neutrophils by macrophages and transformation of macrophages from M1 to M2 phenotype 17‐21 . Ac2‐26 could also facilitate angiogenesis and stimulate fibroblast migration in high glucose conditions 22,23 . Hence, Ac2‐26 may regulate diabetic wound healing process.…”

Section: Introductionmentioning

confidence: 99%

Annexin A1‐derived peptide Ac2‐26 facilitates wound healing in diabetic mice

Huang

Xia

Wei

et al. 2020

Wound Repair Regeneration

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Impaired wound healing is a common complication of diabetes. In diabetic wounds, macrophages present dysfunctional efferocytosis and abnormal phenotypes, which could result in excessive neutrophil accumulation and prolonged inflammation, thereby eventually hindering wound repair. ANXA1 N‐terminal peptide Ac2‐26 exhibits a high potential in mitigating inflammation and improving repair; however, its efficacy in diabetic wound repair remains unclear. In this study, a cutaneous excisional wound model was built in genetically diabetic mice. Ac2‐26 or a vehicle solution was employed locally in wound sites. Subsequently, wound zones were measured and sampled at different time intervals post‐wounding. Using hematoxylin‐eosin and Masson's trichrome staining, we observed the histopathological variations and collagen deposition in wound samples. Based on immunohistochemistry and immunofluorescence, the numbers of neutrophils, macrophages, and CD206‐positive macrophages in the wound samples were determined. Cytokine expression in wound samples was studied by immunoblot assay. Results showed that Ac2‐26 treatment could facilitate diabetic wound closure, down‐regulate the number of neutrophils, and improve angiogenesis and collagen deposition. In addition, Ac2‐26 application expedited macrophage recruitment and up‐regulated the percentage of macrophages expressing CD206, which is a marker for M2 macrophages. Moreover, Ac2‐26 inhibited the expressions of TNF‐α and IL‐6 and up‐regulated the expressions of IL‐10, TGF‐β, and VEGFA during diabetic wound healing. Hence, based on the aforementioned findings, Ac2‐26 application in diabetic wounds could exert anti‐inflammatory and pro‐repair effects by reducing neutrophil accumulation and facilitating M2 macrophage development.

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Ac2-26 peptide and serine protease of Bothrops atrox similarly induces angiogenesis without triggering local and systemic inflammation in a murine model of dorsal skinfold chamber

Cited by 7 publications

References 38 publications

ANNEXIN A1: Roles in Placenta, Cell Survival, and Nucleus

ANNEXIN A1: Roles in Placenta, Cell Survival, and Nucleus

Mast cell heterogeneity and anti-inflammatory annexin A1 expression in leprosy skin lesions

Annexin A1‐derived peptide Ac2‐26 facilitates wound healing in diabetic mice

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