Transient and reversible reduction of stratum corneum filaggrin degradation products after allergen challenge in experimentally mite‐sensitised atopic dogs

2021 ◽  
Author(s):  
Thierry Olivry ◽  
Judy S. Paps ◽  
Nicolas Amalric
Keyword(s):  
Stratum Corneum ◽  
Degradation Products ◽  
Allergen Challenge ◽  
Reversible Reduction

scholarly journals Stratum Corneum Biomarkers in Atopic Dermatitis: Biological and Spatial Variability

2020 ◽  
Vol 10 (1) ◽  
pp. 47-54
Author(s):  
Ruzica Jurakic Toncic ◽  
Sanja Kezic ◽  
Suzana Ljubojevic Hadzavdic ◽  
Branka Marinovic ◽  
Ivone Jakasa
Keyword(s):  
Atopic Dermatitis ◽  
Stratum Corneum ◽  
Degradation Products ◽  
Biological Variability ◽  
Lesional Skin ◽  
Skin Site ◽  
Multiplex Immunoassay ◽  
Non Invasive ◽  
Subject Variability ◽  
Highly Correlated

Background: Atopic dermatitis is a highly heterogeneous skin disease, mainly affecting children. Introduction of biological therapies has urged the development of biomarkers to facilitate personalized therapy. Stratum corneum biomarkers emerged as a promising non-invasive alternative to skin biopsy, yet validation of spatial and biological variability is essential for their application in clinical research. Objective: To assess spatial and biological variability of stratum corneum biomarkers for atopic dermatitis. Methods: Stratum corneum was collected from 17 atopic dermatitis patients by consecutive application of eight adhesive tapes to a lesional skin site and 2 cm and 4 cm from the lesion. Two non-lesional sites at a 2 cm distance from the same lesion were collected to determine biological variability. Filaggrin degradation products (NMF) were determined by liquid chromatography and thirteen cytokines (IL-4, IL-13, IL-18, IL-31, IL-33, CCL17, CCL22, CCL27, CXCL8, IL-1α, IL-RA, IL-18, IL-22) by multiplex immunoassay. Results: Biomarker levels showed gradual changes from lesional to non-lesional skin sites at 2 cm and 4 cm; magnitude and direction of change were biomarker-specific. Intra-subject variability ranged from 17.3% (NMF) to 85.1% (CXCL8). Biomarker levels from two stratum corneum depths were highly correlated; several biomarkers showed significant depth dependence. Conclusion: Stratum corneum enables non-invasive collection of relevant immune and epidermal biomarkers, but biomarker-specific spatial and biological variability emphasizes the importance of standardized procedures for stratum corneum collection.

Changes in corneocyte element concentrations occur in skin inner stratum corneum

1990 ◽  
Vol 48 (2) ◽  
pp. 146-147
Author(s):  
R. R. Warner
Keyword(s):  
Stratum Corneum ◽  
Human Skin ◽  
Element Concentration ◽  
Skin Barrier ◽  
Barrier Properties ◽  
Brick Wall ◽  
Inorganic Elements ◽  
Dry Skin ◽  
Skin Biopsies ◽  
Intercellular Lipid

Keratinocytes undergo maturation during their transit through the viable layers of skin, and then abruptly transform into flattened, anuclear corneocytes that constitute the cellular component of the skin barrier, the stratum corneum (SC). The SC is generally considered to be homogeneous in its structure and barrier properties, and is often shown schematically as a featureless brick wall, the “bricks” being the corneocytes, the “mortar” being intercellular lipid. Previously we showed the outer SC was not homogeneous in its composition, but contained steep gradients of the physiological inorganic elements Na, K and Cl, likely originating from sweat salts. Here we show the innermost corneocytes in human skin are also heterogeneous in composition, undergoing systematic changes in intracellular element concentration during transit into the interior of the SC.Human skin biopsies were taken from the lower leg of individuals with both “good” and “dry” skin and plunge-frozen in a stirred, cooled isopentane/propane mixture.

Paracrystalline Aggregates of Psoriatic Keratin and Their Relation to Normal Keratin Structure

1985 ◽  
Vol 43 ◽  
pp. 680-681
Author(s):  
S. Trachtenberg ◽  
P.M. Steinert ◽  
B.L. Trus ◽  
A.C. Steven
Keyword(s):  
Cell Death ◽  
Stratum Corneum ◽  
Intermediate Filament ◽  
Skin Disease ◽  
Amorphous Matrix ◽  
Terminal Differentiation ◽  
Proteolytic Degradation ◽  
Horny Layer ◽  
Chronic Skin ◽  
Chronic Skin Disease

During terminal differentiation of vertebrate epidermis, certain specific keratin intermediate filament (KIF) proteins are produced. Keratinization of the epidermis involves cell death and disruption of the cytoplasm, leaving a network of KIF embedded in an amorphous matrix which forms the outer horny layer known as the stratum corneum. Eventually these cells are shed (desquamation). Normally, the processes of differentiation, keratinization, and desquamation are regulated in an orderly manner. In psoriasis, a chronic skin disease, a hyperkeratotic stratum corneum is produced, resulting in abnormal desquamation of unusually large scales. In this disease, the normal KIF proteins are diminished in amount or absent, and other proteins more typical of proliferative epidermal cells are present. There is also evidence of proteolytic degradation of the KIF.

Unilateral nasal allergen challenge leads to bilateral release of prostaglandin D2

1996 ◽  
Vol 26 (4) ◽  
pp. 371-378 ◽  
Author(s):  
M. WAGENMANN ◽  
F. M. BAROODY ◽  
M. DESROSIERS ◽  
W. C. HUBBARD ◽  
S. FORD ◽  
...  
Keyword(s):  
Allergen Challenge ◽  
Prostaglandin D2 ◽  
Nasal Allergen Challenge

Collagen degradation products modulate matrix metalloproteinase expression in cultured articular chondrocytes

2005 ◽  
Vol 24 (1) ◽  
pp. 63-70 ◽  
Author(s):  
M. Fichter ◽  
U. Körner ◽  
J. Schömburg ◽  
L. Jennings ◽  
A. A. Cole ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Articular Chondrocytes ◽  
Degradation Products ◽  
Collagen Degradation ◽  
Collagen Degradation Products

Structural Studies of Fibrinolysis by Electron and Light Microscopy

1999 ◽  
Vol 82 (08) ◽  
pp. 277-282 ◽  
Author(s):  
Yuri Veklich ◽  
Jean-Philippe Collet ◽  
Charles Francis ◽  
John W. Weisel
Keyword(s):  
Electron Microscopy ◽  
Light Microscopy ◽  
Plasminogen Activator ◽  
Structural Changes ◽  
Molecular Mechanisms ◽  
Degradation Products ◽  
Molecular Model ◽  
Three Dimensional ◽  
Tissue Type ◽  
Type Plasminogen Activator

IntroductionMuch is known about the fibrinolytic system that converts fibrin-bound plasminogen to the active protease, plasmin, using plasminogen activators, such as tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator. Plasmin then cleaves fibrin at specific sites and generates soluble fragments, many of which have been characterized, providing the basis for a molecular model of the polypeptide chain degradation.1-3 Soluble degradation products of fibrin have also been characterized by transmission electron microscopy, yielding a model for their structure.4 Moreover, high resolution, three-dimensional structures of certain fibrinogen fragments has provided a wealth of information that may be useful in understanding how various proteins bind to fibrin and the overall process of fibrinolysis (Doolittle, this volume).5,6 Both the rate of fibrinolysis and the structures of soluble derivatives are determined in part by the fibrin network structure itself. Furthermore, the activation of plasminogen by t-PA is accelerated by the conversion of fibrinogen to fibrin, and this reaction is also affected by the structure of the fibrin. For example, clots made of thin fibers have a decreased rate of conversion of plasminogen to plasmin by t-PA, and they generally are lysed more slowly than clots composed of thick fibers.7-9 Under other conditions, however, clots made of thin fibers may be lysed more rapidly.10 In addition, fibrin clots composed of abnormally thin fibers formed from certain dysfibrinogens display decreased plasminogen binding and a lower rate of fibrinolysis.11-13 Therefore, our increasing knowledge of various dysfibrinogenemias will aid our understanding of mechanisms of fibrinolysis (Matsuda, this volume).14,15 To account for these diverse observations and more fully understand the molecular basis of fibrinolysis, more knowledge of the physical changes in the fibrin matrix that precede solubilization is required. In this report, we summarize recent experiments utilizing transmission and scanning electron microscopy and confocal light microscopy to provide information about the structural changes occurring in polymerized fibrin during fibrinolysis. Many of the results of these experiments were unexpected and suggest some aspects of potential molecular mechanisms of fibrinolysis, which will also be described here.

Fibrinogen Bastia (γ 318 Asp → Tyr) a Novel Abnormal Fibrinogen Characterized by Defective Fibrin Polymerization

1999 ◽  
Vol 82 (12) ◽  
pp. 1639-1643 ◽  
Author(s):  
Karim Chabane Lounes ◽  
Claudine Soria ◽  
Antoine Valognes ◽  
Marie France Turchini ◽  
Jaap Koopman ◽  
...  
Keyword(s):  
Calcium Ions ◽  
Clinical Symptoms ◽  
Degradation Products ◽  
Base Substitution ◽  
Chain Gene ◽  
Fibrinogen Concentration ◽  
Clotting Time ◽  
Terminal Part ◽  
Fibrin Polymerization ◽  
Chain Sequence

SummaryA new congenital dysfibrinogen, Fibrinogen Bastia, was discovered in a 20-year-old woman with no clinical symptoms. The plasma thrombin-clotting time was severely prolonged. The functional plasma fibrinogen concentration was low (0.2 mg/ml), whereas the immunological concentration was normal (2.9 mg/ml). Purified fibrinogen Bastia displayed a markedly prolonged thrombin-clotting time related to a delayed thrombin-induced fibrin polymerization. Both the thrombin-clotting time and the fibrin polymerization were partially corrected by the addition of calcium ions. The anomaly of fibrinogen Bastia was found to be located in the γ-chain since by SDS-PAGE performed according to the method of Laemmli two γ-chains were detected, one normal and one with an apparently lower molecular weight. Furthermore, analysis of plasmin degradation products demonstrated that calcium ions only partially protect fibrinogen Bastia γ-chain against plasmin digestion, suggesting that the anomaly is located in the C-terminal part of the γ-chain. Sequence analysis of PCR-amplified genomic DNA fragments of the propositus demonstrated a single base substitution (G → T) in the exon VIII of the γ chain gene, resulting in the amino acid substitution 318 Asp (GAC) → Tyr (TAC). The PCR clones were recloned and 50% of them contained the mutation, indicating that the patient was heterozygous. These data indicate that residue Asp 318 is important for normal fibrin polymerization and the protective effect of calcium ions against plasmin degradation of the C-terminal part of the γ-chain.

Rätselhafte Bläschen an Händen und Mundschleimhaut bei einem 15 Monate alten Mädchen: Intoxikation durch Dieselöl

2005 ◽  
Vol 5 (03) ◽  
pp. 141-143
Author(s):  
Andreas Merkenschlager ◽  
Matthias Bernhard
Keyword(s):  
Stratum Corneum

ZusammenfassungAkzidentelle Vergiftungen ereignen sich am häufigsten im Kleinkindesalter. Der weit verbreitete Gebrauch von aliphatischen Hydrokarbonen wie Dieselöl begünstigt Intoxikationen. Die Ingestion von Dieseltreibstoff birgt insbesondere die Gefahr einer Aspirationspneumonie. Akute Hauttoxizität ist hingegen selten.Ein 15 Monate altes Mädchen entwickelte nach vorausgegangenem Erbrechen und einer mehrere Stunden andauernden Lethargie innerhalb von 24 Stunden zahlreiche bläschenartige Hautläsionen, die teilweise ulzeriert waren, an den Fingern, der Handinnenfläche sowie perioral. Die Wangen- und Gaumensegelschleimhaut zeigten mehrere kleine Ulzera, die weißlich belegt und hämorrhagisch waren. Zunächst wurde eine Hand-Fuß-Mund-Krankheit vermutet. Durch ausführliche Anamnese konnte jedoch festgestellt werden, dass das Kind am Tag zuvor in einem Sandkasten gespielt hatte, der durch ein Leck in einem daneben stehenden Dieselöltank kontaminiert gewesen war. Eine pulmonale oder hepatische Beteiligung konnte nicht nachgewiesen werden. Die Läsionen heilten vollständig unter antiseptischen Verbänden innerhalb einer Woche ab.Man nimmt an, dass Dieselöl primär das Stratum corneum der Haut schädigt. Kinder sind aufgrund ihrer gegenüber Erwachsenen dünneren Hornhaut gefährdeter. In seltenen Fällen können sich Vesikel, Ulzera und Hämorrhagien entwickeln, die mit Infektionskrankheiten verwechselt werden können.Unstimmigkeiten bei klinischen Befunden sollten insbesondere bei Kleinkindern immer an mögliche Intoxikationen denken lassen.

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