Differential expression of glycans in the urothelial layers of horse urinary bladder.
Abstract: Urothelium is a multilayer epithelium covering the inner surface of the urinary bladder that acts as a blood-urine barrier and is involved in maintaining the wellbeing of the whole organism. Glycans serve in the maturation and differentiation of cells and thus play a key role in the morphology and function of the multilayered epithelium. The aim of the present study was to examine the glycoprotein pattern of the horse urinary bladder urothelium by lectin histochemistry. Methods: The study involved urinary bladders from four horse stallions. Tissue sections were stained with a panel of eleven lectins, in combination with saponification and sialidase digestion (Ks). Results: Basal cells displayed high-mannose N-glycans (Con A), α2,6-linked sialic acid (SNA), and O-linked sialoglycans with sialic acids linked to Galβl,3GalNAc (T antigen) (KsPNA) and terminal N-acetylgalactosamine (Tn antigen) (KsSBA). The young intermediate cells expressed terminal N-acetylglucosamine (GlcNAc) (GSA II), galactose (GSA I-B), T- and Tn antigens (PNA, SBA). The mature intermediate cells showed additional high-mannose N-glycans, O-linked sialoglycans (sialyl-T antigen, sialyl-Tn antigen), α2,6- and α2,3-linked sialic acid (MAL II), α1,2-linked fucose (UEA I), and GlcNAc (KsWGA). The latter residue marked the boundary with the overlying surface layer. Few Con A positive intermediate cells were seen to cross the entire urothelium thickness. The surface cells showed additional glycans such as T antigen and sialic acids linked to GalNAc binding DBA (KsDBA). Few surface cells contained α1,3-linked fucose (LTA), whereas some other cells displayed intraluminal secretion of mucin-type glycans terminating with GalNAcα1,3(LFucα1,2)Galβ1,3/4GlcNAcβ1 (DBA). The luminal surface expressed the most complex glycan pattern in the urothelium because only α1,3-linked fucose lacked among the demonstrated glycans. Conclusions: This study showed that the glycan pattern becomes more complex from the basal to surface layer of the urothelium and that surface cells could modify the composition of urine via the secretion of glycoproteins.
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Publication Date: 2022-08-17 PubMed ID: 35987426DOI: 10.1016/j.aanat.2022.151988Google Scholar: Lookup
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Summary
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The research explores the presence and variations of sugar chains (glycans) in the cell layers (urothelium) that line the inside of a horse’s urinary bladder. The study investigates how these glycans contribute to the structure and function of the bladder, revealing that the complexity of the glycans increases from the base to the surface layers and that the surface cells might be able to alter the composition of urine through the release of glycoproteins.
Objective of Research
- The main aim of this study was to investigate the pattern of glycoproteins, proteins with attached sugar chains, in the urothelium of a horse’s urinary bladder through a process called lectin histochemistry. This method allows researchers to identify and visualize specific carbohydrate compounds in cells and tissues, thus revealing the patterns and variations of glycans in the urothelium.
Methodology of Research
- The study involved the examination of urinary bladder tissues from four horse stallions.
- Sections of these tissues were stained with a group of proteins called lectins, which can bind to specific sugar compounds. In combination with processes called saponification and sialidase digestion, the researchers were able to isolate and identify the specific glycans present in the cells of the urothelium.
Results and Discoveries
- Different types of glycans were found in the different layers of cells within the urothelium. For instance, basal cells exhibited high-mannose N-glycans, α2,6-linked sialic acid, and a specific type of O-linked sugars.
- The young intermediate cells expressed another set of glycans, such as terminal N-acetylglucosamine and galactose.
- The complexity of the glycans increased as the layers of cells matured, with the mature intermediate cells showing additional high-mannose N-glycans, α2,6- and α2,3-linked sialic acid, among others.
- The surface layer of cells displayed the most complex pattern of glycans, indicating that the complexity of glycan patterns increased from the base to the surface layer of the urothelium.
- Some surface cells were found to contain α1,3-linked fucose, while others were seen to secrete mucin-type glycans into the bladder’s internal cavity, suggesting that the composition of urine could be altered by the secretion of glycoproteins from these cells.
Conclusions
- The research concluded that glycans play a significant role in determining the morphology and functionality of the urothelium in horse urinary bladders.
- It also emphasized the likelihood of urinary composition being modified by the surface cells of the urothelium via secretion of glycoproteins.
Cite This Article
APA
Desantis S, Santamaria N, Zizza S, Accogli G, Mastrodonato M, Scillitani G, Mentino D.
(2022).
Differential expression of glycans in the urothelial layers of horse urinary bladder.
Ann Anat, 244, 151988.
https://doi.org/10.1016/j.aanat.2022.151988 Publication
Researcher Affiliations
- Department of Emergency and Organ Transplantation (DETO), University of Bari Aldo Moro, Bari, Italy. Electronic address: salvatore.desantis@uniba.it.
- Department of Emergency and Organ Transplantation (DETO), University of Bari Aldo Moro, Bari, Italy.
- Department of Emergency and Organ Transplantation (DETO), University of Bari Aldo Moro, Bari, Italy.
- Department of Emergency and Organ Transplantation (DETO), University of Bari Aldo Moro, Bari, Italy.
- Department of Biology, University of Bari Aldo Moro, Bari, Italy.
- Department of Biology, University of Bari Aldo Moro, Bari, Italy.
- Department of Biosciences, Biotechnology, and Biopharmaceutics, University of Bari Aldo Moro, Bari, Italy.
MeSH Terms
- Horses
- Male
- Animals
- Urothelium
- Urinary Bladder
- Mannose
- N-Acetylneuraminic Acid
- Neuraminidase
- Fucose
- Galactose
- Acetylgalactosamine
- Acetylglucosamine
- Polysaccharides / metabolism
- Lectins / chemistry
- Lectins / metabolism
- Glycoproteins
- Mucins
- Antigens, Viral, Tumor
Conflict of Interest Statement
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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