Incubation of unfixed and unfrozen slices of skin in diaminobenzidine allows visualization of peroxidatic activity in the perinuclear envelope and endoplasmic reticulum of normal human Langerhans cells. A similar peroxidatic activity is observed in supra-basal keratinocytes undergoing orthokeratotic differentiation. Basal keratinocytes and melanocytes are always negative. This enzyme is absent in mucous and parakeratotic (psoriatic) differentiation. A peroxidatic activity was also found in the endoplasmic reticulum of normal resident skin macrophages. Mitochondria are also strongly stained by this technique and it was shown that the number of epidermal mitochondria is greatly increased in psoriatic lesions.

Download full-text PDF

Source
http://dx.doi.org/10.1111/j.1365-2133.1982.tb01039.xDOI Listing

Publication Analysis

Top Keywords

peroxidatic activity
12
langerhans cells
8
macrophages mitochondria
8
endoplasmic reticulum
8
reticulum normal
8
cytochemical marker
4
marker epidermal
4
epidermal differentiation
4
differentiation langerhans
4
cells skin
4

Similar Publications

Molecular characterization, cytoprotective, DNA protective, and immunological assessment of peroxiredoxin-1 (Prdx1) from yellowtail clownfish (Amphiprion clarkii).

Dev Comp Immunol

July 2024

Department of Marine Life Sciences & Center for Genomic Selection in Korean Aquaculture, Jeju National University, Jeju, 63243, Republic of Korea; Marine Life Research Institute, Jeju National University, Jeju, 63333, Republic of Korea. Electronic address:

Peroxiredoxin-1 (Prdx1) is a thiol-specific antioxidant enzyme that detoxifies reactive oxygen species (ROS) and regulates the redox status of cells. In this study, the Prdx1 cDNA sequence was isolated from the pre-established Amphiprion clarkii (A. clarkii) (AcPrdx1) transcriptome database and characterized structurally and functionally.

View Article and Find Full Text PDF

Peroxiredoxin1(Prx1), also known as natural killer enhancing factor A (NKEF-A), is a crucial antioxidant involving in various cellular activities and immune response against bacterial and viral infection in fish. In the present study, a full-length Prx1 cDNA sequence (TfPrx1) was firstly cloned from roughskin sculpin (Trachidermus fasciatus), which was composed of 1044 bp nucleotides encoding a peptide of 199 amino acids with a molecular weight of 22.35 kDa and a theoretical pI of 6.

View Article and Find Full Text PDF

Sleeve Gastrectomy Provides Cardioprotection from Oxidative Stress In Vitro Due to Reduction of Circulating Myeloperoxidase.

Nutrients

November 2023

Department of Surgery, Division of Gastrointestinal and Minimally Invasive Surgery, Medical College of Wisconsin, 8900 W. Doyne Avenue, Milwaukee, WI 53226, USA.

Bariatric surgery, including sleeve gastrectomy (SG), improves systolic and diastolic function, which is independent of weight loss in rodent models. The cause of weight loss-independent improvements in cardiac function are unknown but may originate from the gastrointestinal tract. In this study, we investigated whether a circulating blood factor is a mechanism for acute cardioprotection after SG by testing the utility of rodent SG plasma to reduce metabolic stress in vitro.

View Article and Find Full Text PDF

12-oxo-phytodienoic acid (OPDA) is a primary precursor of jasmonates, able to trigger autonomous signaling cascades that activate and fine-tune plant defense responses, as well as growth and development. However, its mechanism of actions remains largely elusive. Here we describe a dual-function messenger of OPDA signaling, reduced glutathione (GSH), that cross-regulates photosynthesis machinery and stress protection/adaptation in concert, optimizing plant plasticity and survival potential.

View Article and Find Full Text PDF

Biophysical tools to study the oligomerization dynamics of Prx1-class peroxiredoxins.

Biophys Rev

August 2023

Laboratorio Fisicoquímica Biológica, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay.

Peroxiredoxins (Prx) are ubiquitous, highly conserved peroxidases whose activity depends on catalytic cysteine residues. The Prx1-class of the peroxiredoxin family, also called typical 2-Cys Prx, organize as head-to-tail homodimers containing two active sites. The peroxidatic cysteine C of one monomer reacts with the peroxide substrate to form sulfenic acid that reacts with the resolving cysteine (C) of the adjacent subunit to form an intermolecular disulfide, that is reduced back by the thioredoxin/thioredoxin reductase/NADPH system.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!