Expression of the receptor for advanced glycation end products in acquired reactive perforating collagenosis

Gulsen Akoglu1, Nuran Sungu2, Eda Karaismailoglu3

  • 1Department of Dermatovenereology, Ataturk Training and Research Hospital, Ankara, Turkey.

Abstract

Insights

Acquired reactive perforating collagenosis (ARPC) shows increased expression of the receptor for advanced glycation end products (RAGE). This RAGE overexpression in ARPC skin lesions is independent of diabetes status.

Area of Science:

  • Dermatology
  • Pathology
  • Immunohistochemistry

Background:

  • Acquired reactive perforating collagenosis (ARPC) is a rare skin condition involving collagen elimination.
  • The pathogenesis of ARPC is not well understood.
  • The receptor for advanced glycation end products (RAGE) is implicated in inflammatory processes.

Purpose of the Study:

  • To investigate the expression levels of RAGE in patients with ARPC.
  • To determine if RAGE expression differs between ARPC patients and healthy controls.

Main Methods:

  • Immunohistochemical staining for RAGE was performed on skin biopsy specimens from 41 ARPC patients and 11 healthy controls.
  • RAGE expression intensity was semi-quantitatively assessed in epidermal cells, microvascular endothelium, dermal fibroblasts, and inflammatory cells.
  • Patients were analyzed based on diabetic and non-diabetic status.

Main Results:

  • RAGE expression was significantly more intense in the microvascular endothelium and inflammatory cells of ARPC patients compared to controls (p=0.005 and p=0.017, respectively).
  • Increased RAGE expression was also observed in dermal fibroblasts, though not statistically significant (p > 0.05).

Conclusions:

  • The study observed an overexpression of RAGE in lesional samples from ARPC patients.
  • This RAGE overexpression in ARPC is independent of the presence of diabetes.

Related Concept Videos

Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
5.0K
Rheumatic Heart Disease I: Introduction01:23

Rheumatic Heart Disease I: Introduction

Rheumatic heart disease or RHD is a chronic condition that results from rheumatic fever, causing permanent damage to the heart valves.Etiology and Risk FactorsIt primarily arises from rheumatic fever, an inflammatory disease that can develop after untreated or inadequately treated group A streptococcal (GAS) pharyngitis. Streptococcus spreads through direct contact with oral or respiratory secretions. While the bacteria are the causative agents, factors like malnutrition, overcrowding, poor...
656
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
3.2K
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
5.4K
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
3.5K