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The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2026; 221554261474565; doi: 10.1369/00221554261474565

Ortholog-specific Spatial Expression of Vanins in the Respiratory Tract of Horses.

Abstract: Equine asthma (EA) is the most prevalent chronic respiratory disease in horses, but molecules thought to be relevant in its pathogenesis are not yet fully understood. Recently, increased Vanin-1 (VNN1) levels were found in bronchoalveolar lavage fluid from horses with severe EA. Human VNN1 is known as a pantetheinase, which is associated with respiratory diseases such as asthma, but the equine vanins (eVNNs) are uncharacterized. We identified the domain architecture of eVNN in silico and analyzed its tissue expression in healthy horses using RT-PCR (=5) and in situ hybridization (=3). Recombinant eVNNs were expressed in HEK293 cells to assess cellular transport and glycosylation via Endo H and PNGase F treatment. Three putative functional were identified on chromosome 10, each containing canonical Nitrilase superfamily domains. All genes showed a broad tissue expression, but distinct airway localization: and were predominantly expressed in respiratory epithelium, whereas was localized in submucosal glands. eVNN1 and eVNN3 were secreted, while eVNN2 remained cell associated. Pantetheinase activity of recombinant eVNN1 was confirmed by mass spectrometry. The three eVNNs appear to cover different functional niches in equine airways, enabling future research into their putative role in EA.
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Publication Date: 2026-08-31 PubMed ID: 42670687PubMed Central: PMC13530036DOI: 10.1369/00221554261474565Google Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

Plain Language Overview

  • This research investigates the expression and characteristics of vanin proteins in the respiratory tract of healthy horses, focusing on their potential role in equine asthma, a common chronic lung disease in horses.

Introduction and Background

  • Equine asthma (EA) is the most widespread chronic respiratory condition affecting horses, yet the molecular mechanisms driving its development are not fully understood.
  • Vanin-1 (VNN1), a pantetheinase enzyme, has been associated with human respiratory diseases such as asthma and was found at elevated levels in the lung fluid of horses suffering from severe EA.
  • Despite its significance in humans, the equine counterparts of vanins (eVNNs) have not been characterized prior to this study.

Objective and Methods

  • The study aimed to characterize the domain structure and spatial expression of equine vanins (eVNNs) and to understand their biochemical properties.
  • In silico analyses were conducted to identify the domain architecture of the eVNN proteins.
  • Tissue expression of the identified eVNN genes was examined in healthy horses using:
    • Reverse transcription polymerase chain reaction (RT-PCR) on samples from five horses.
    • In situ hybridization on samples from three horses to localize the expression within airway tissues.
  • Recombinant forms of eVNN proteins were produced in HEK293 cells to analyze:
    • Cellular transport mechanisms.
    • Protein glycosylation status using Endoglycosidase H (Endo H) and Peptide-N-Glycosidase F (PNGase F) treatments.
  • Pantetheinase enzyme activity was validated for recombinant eVNN1 using mass spectrometry.

Key Findings

  • Three putative functional vanin genes were identified on equine chromosome 10.
  • Each gene contained canonical domains characteristic of the Nitrilase superfamily, indicating conserved enzymatic capabilities.
  • Tissue expression analysis revealed:
    • All three genes exhibited broad expression across multiple tissues.
    • Distinct localization patterns within airway tissue:
      • eVNN1 and eVNN3 were primarily expressed in the respiratory epithelium.
      • eVNN2 expression was predominant in the submucosal glands of the airway.
  • Protein characterization showed:
    • Both eVNN1 and eVNN3 proteins were secreted from cells, suggesting roles in extracellular processes.
    • eVNN2 remained associated with the cell, implying a potentially different functional role.
    • Successful confirmation of pantetheinase activity for recombinant eVNN1 enzyme.

Significance and Future Directions

  • The three eVNN proteins likely fulfill distinct functional roles in the equine respiratory system based on their spatial expression and secretion profiles.
  • Understanding these differences enhances the foundation for investigating their involvement in the development or progression of equine asthma.
  • This work opens pathways for future research focusing on the specific contributions of each eVNN to airway health and disease, potentially leading to novel therapeutic targets or biomarkers for equine asthma.

Cite This Article

APA
Landmann K, Bartenschlager F, Meierhofer D, Spree A, Pisch C, Zeyner A, Schnabel CL, Mundhenk L. (2026). Ortholog-specific Spatial Expression of Vanins in the Respiratory Tract of Horses. J Histochem Cytochem, 221554261474565. https://doi.org/10.1369/00221554261474565

Publication

The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
ISSN: 1551-5044
NlmUniqueID: 9815334
Country: United States
Language: English
Pages: 221554261474565
PII: 00221554261474565

Researcher Affiliations

Landmann, Katharina
  • Institute of Veterinary Pathology, Faculty of Veterinary Medicine, Freie Universität Berlin, Berlin, Germany.
Bartenschlager, Florian
  • Institute of Veterinary Pathology, Faculty of Veterinary Medicine, Freie Universität Berlin, Berlin, Germany.
Meierhofer, David
  • Max Planck Institute for Molecular Genetics, Berlin, Germany.
Spree, Andreas
  • Institute of Veterinary Pathology, Faculty of Veterinary Medicine, Freie Universität Berlin, Berlin, Germany.
Pisch, Caroline
  • Institute of Agricultural and Nutritional Sciences, Martin Luther University Halle-Wittenberg, Halle, Germany.
Zeyner, Annette
  • Institute of Agricultural and Nutritional Sciences, Martin Luther University Halle-Wittenberg, Halle, Germany.
Schnabel, Christiane L
  • Institute of Immunology, Faculty of Veterinary Medicine, Leipzig University, Leipzig, Germany.
Mundhenk, Lars
  • Institute of Veterinary Pathology, Faculty of Veterinary Medicine, Freie Universität Berlin, Berlin, Germany.

Conflict of Interest Statement

The authors declared no potential conflicts of interest with respect to the research, authorship, and/or publication of this article.

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