A simple skin blister technique for the study of in vivo transmigration of human leukocytes

Davidsson, Lisa; Björkman, Lena; Christenson, Karin; Alsterholm, Mikael; Movitz, Charlotta; Thorén, Fredrik B.; Karlsson, Anna; Welin, Amanda; Bylund, Johan

doi:10.1016/j.jim.2013.03.013

Cited by 16 publications

(25 citation statements)

References 20 publications

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“…This makes sense, given that neutrophils are short lived and terminally differentiated; they do not divide after leaving the bone marrow. We confirmed these findings [11] and also demonstrated that the relative proportion of OLFM4-expressing neutrophils is not altered by in vivo transmigration to tissues but reflects the relative abundance in circulation, i.e., roughly 10-50% [11,12]. Among the subtype markers described so far is CD177 (also known as HNA-2a), a membraneanchored glycoprotein that is expressed at the surface and in granules of a varying proportion (0-100%) of neutrophils [8] and the granule protein OLFM4.…”

Section: Introductionsupporting

confidence: 78%

Olfactomedin-4 autoantibodies give unusual c-ANCA staining patterns with reactivity to a subpopulation of neutrophils

Amirbeagi

Thulin

Pullerits

et al. 2014

Journal of Leukocyte Biology

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Section: Introductionsupporting

confidence: 78%

Olfactomedin-4 autoantibodies give unusual c-ANCA staining patterns with reactivity to a subpopulation of neutrophils

Amirbeagi

Thulin

Pullerits

et al. 2014

Journal of Leukocyte Biology

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“…; Davidsson et al. ). Since blister induction may cause local skin hyperpigmentation, we induced blisters on the medial upper arm (5 cm proximal to the elbow).…”

Section: Methodsmentioning

confidence: 98%

“…; Davidsson et al. ). Two identical (same LOT number) human cytokine 17‐plex assays where purchased (Bio‐Plex Pro TM Human Magnetic Cytokine, Bio‐Rad Laboratories Inc., Copenhagen, Denmark) for measurement of concentrations of interleukin‐1 β (IL‐1 β ), IL‐2, IL‐4, IL‐5, IL‐6, IL‐7, IL‐8, IL‐10, IL‐12, IL‐13, IL‐17, Granulocyte Colony Stimulating Factor (G‐CSF), Granulocyte‐Monocyte Colony Stimulating Factor (GM‐CSF), Interferon‐ γ (IFN‐ γ ), Monocyte Chemotactic Protein‐1 (MCP‐1), Macrophage Inflammatory Protein‐1 (MIP‐1), and Tumor Necrosis Factor‐ α (TNF‐ α ) in plasma and suction blister fluid samples.…”

Section: Methodsmentioning

confidence: 98%

Higher vascular endothelial growth factor-C concentration in plasma is associated with increased forearm capillary filtration capacity in breast cancer-related lymphedema

et al. 2015

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Breast cancer-related lymphedema (BCRL) is a frequent, chronic and debilitating swelling that mainly affects the ipsilateral arm and develops as a complication to breast cancer treatment. The pathophysiology is elusive opposing development of means for prediction and treatment. We have earlier shown that the forearm capillary filtration coefficient (CFC) is increased bilaterally in BCRL. In this study, we aimed to elucidate if increased CFC is associated with low-grade inflammation and/or vascular endothelial growth factor-c (VEGF-C) signaling. Fourteen patients with unilateral BCRL and nine matched breast cancer controls without BCRL participated. Forearm CFC was measured by venous congestion strain gauge plethysmography, and suction blisters were induced medially on the upper arms. Concentrations of 17 selected cytokines, VEGF-C, and total protein were measured in blister fluid and in plasma. Forearm CFC was higher bilaterally in BCRL subjects (P ≤ 0.036). No differences between forearms were found in either group. Plasma VEGF-C concentrations were significantly higher in the BCRL subjects (P < 0.001). In BCRL subjects, monocyte chemotactic protein 1 (MCP-1) (P = 0.009) and total protein (P = 0.035) concentrations were higher in blister fluid from edematous arms compared with nonedematous arms. No differences were found in interstitial cytokine or total protein concentrations between arms in control subjects. Higher plasma concentration of VEGF-C is a possible cause of bilaterally increased forearm CFC in BCRL subjects. Interstitially increased MCP-1 levels may augment local microvascular protein permeability in BCRL.

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“…The priming state of neutrophils was investigated as CD11b exposure by staining with PE‐labeled anti‐CD11b monoclonal antibody (1:20 dilution). To ensure proper identification of neutrophils, monocytes, and lymphocytes during flow cytometry analysis, the cells were colabeled with mouse anti‐human CD45 antibody conjugated with APC (for anti‐galectin‐3 or anti‐CD11b stained cells) or FITC (for anti‐CRD stained cells) . The CD45 staining allows for clear gating between the different white blood cells as demonstrated in Supplemental Figure 2.…”

Section: Methodsmentioning

confidence: 99%

Galectin-3 type-C self-association on neutrophil surfaces; The carbohydrate recognition domain regulates cell function

Sundqvist

Welin

Elmwall

et al. 2018

Journal of Leukocyte Biology

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Summary sentence: Galectin-3 is cleaved by both neutrophils and bacteria and the residual galectin-3C inhibits galectin-3-induced neutrophil activity but potentiates galectin-3 cell-surface binding. AbstractGalectin-3 is an endogenous -galactoside-binding lectin comprising a carbohydrate recognition domain (CRD) linked to a collagen-like N-domain. Both domains are required for galectin-3 to induce cellular effects; a C-terminal fragment of galectin-3, galectin-3C, containing the CRD but lacking the N-domain, binds cell surface glycoconjugates but does not induce cellular effects since cross-linking promoted by the N-domain is thought to be required. Instead, galectin-3C is proposed to antagonize the effects of galectin-3 by competing for binding sites. The aim of this study was to investigate the effects of galectin-3C on galectin-3 interactions with human neutrophils.Recombinant galectin-3C inhibited galectin-3-induced production of reactive oxygen species in primed neutrophils. Surprisingly, this inhibition was not due to competitive inhibition of galectin-3 binding to the cells. In contrast, galectin-3C potentiated galectin-3 binding, in line with emerging evidence that galectin-3 can aggregate not only through the N-domain but also through the CRD. The cell surface interaction between galectin-3C and galectin-3 was corroborated by colocalization of fluorescently labeled galectin-3 and galectin-3C. Galectin-3C can be generated in vivo through cleavage of galectin-3 by proteases. Indeed, in circulation, galectin-3 and galectin-3C were both attached to the cell surface of neutrophils, which displayed great capacity to bind additional galectin-3 and galectin-3C. In conclusion, galectin-3C enhances galectin-3 binding to neutrophils by nonactivating type-C self-association, in parallel to inhibiting neutrophil activation by galectin-3 (induced by type-N self-association). This implicates type-C self-association as a termination system for galectin-3-induced cell activation, with the purpose of avoiding oxidantdependent tissue damage.

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A simple skin blister technique for the study of in vivo transmigration of human leukocytes

Cited by 16 publications

References 20 publications

Olfactomedin-4 autoantibodies give unusual c-ANCA staining patterns with reactivity to a subpopulation of neutrophils

Olfactomedin-4 autoantibodies give unusual c-ANCA staining patterns with reactivity to a subpopulation of neutrophils

Higher vascular endothelial growth factor-C concentration in plasma is associated with increased forearm capillary filtration capacity in breast cancer-related lymphedema

Galectin-3 type-C self-association on neutrophil surfaces; The carbohydrate recognition domain regulates cell function

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