Novel cathelicidins in horse leukocytes(1).
Abstract: Cathelicidins are precursors of defense peptides of the innate immunity and are widespread in mammals. Their structure comprises a conserved prepropiece and an antimicrobial domain that is structurally varied both intra- and inter-species. We investigated the complexity of the cathelicidin family in horse by a reverse transcription-PCR-based cloning strategy of myeloid mRNA and by Southern and Western analyses. Three novel cathelicidin sequences were deduced from bone marrow mRNA and designated equine cathelicidins eCATH-1, eCATH-2 and eCATH-3. Putative antimicrobial domains of 26, 27 and 40 residues with no significant sequence homology to other peptides were inferred at the C-terminus of the sequences. Southern analysis of genomic DNA using a probe based on the cathelicidin-conserved propiece revealed a polymorphic DNA region with several hybridization-positive fragments and suggested the presence of additional genes. A null eCATH-1 allele was also demonstrated with a frequency of 0.71 in the horse population analyzed and low amounts of eCATH-1-specific mRNA were found in myeloid cells of gene-positive animals. A Western analysis using antibodies to synthetic eCATH peptides revealed the presence of eCATH-2 and eCATH-3 propeptides, but not of eCATH-1-related polypeptides, in horse neutrophil granules and in the secretions of phorbol myristate acetate-stimulated neutrophils. These results thus suggest that eCATH-2 and eCATH-3 are functional genes, whereas eCATH-1 is unable to encode a polypeptide.
Publication Date: 1999-09-03 PubMed ID: 10471829DOI: 10.1016/s0014-5793(99)01097-2Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Journal Article
- Research Support
- Non-U.S. Gov't
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.
The research article investigates the complexity of cathelicidin family in horses. The scientists identified three new cathelicidin sequences, eCATH-1, eCATH-2 and eCATH-3, from horse bone marrow mRNA, with findings suggesting eCATH-2 and eCATH-3 are functional genes, while eCATH-1 is unable to encode a polypeptide.
Understanding Cathelicidins
- Cathelicidins are precursors of defense peptides that play a significant role in innate immunity, which is the first line of defense in the immune system.
- These proteins are known to be widespread among mammals, including horses, possessing a structurally-conserved prepropiece and an antimicrobial domain that varies both within and across species.
Research Process
- The study used a reverse transcription-PCR-based cloning strategy on myeloid mRNA, accompanied by Southern and Western analyses, to investigate the variety within the Cathelicidin family in horses.
Discovery of Novel Cathelicidins
- From the horse bone marrow mRNA, the study identified three novel Cathelicidin sequences, which were named eCATH-1, eCATH-2, and eCATH-3.
- The research observed that these new sequences had 26, 27, and 40 residue antimicrobial domains with no significant sequence homology to other known peptides. These domains were located at the C-terminus of the sequences.
Evidence of Additional Genes and Variation within the Horse Population
- Using a probe based on the conserved propiece of cathelicidins, the team performed a Southern analysis of genomic DNA. They identified a polymorphic DNA region with several hybridization-positive fragments, suggesting the presence of additional genes.
- The study discovered a null eCATH-1 allele with a frequency of 0.71 within the horse population studied. This null allele was associated with low levels of eCATH-1 specific mRNA in the myeloid cells of gene-positive animals.
Functional Insights on the Novel Cathelicidins
- Western analyses using antibodies to synthetic eCATH peptides showed the presence of eCATH-2 and eCATH-3 propeptides, but not of eCATH-1-related polypeptides in horse neutrophil granules and in the secretions of phorbol myristate acetate-stimulated neutrophils.
- These findings suggest that eCATH-2 and eCATH-3 are functional genes, but eCATH-1 does not encode a polypeptide, thus is not functional in the same way.
Cite This Article
APA
Scocchi M, Bontempo D, Boscolo S, Tomasinsig L, Giulotto E, Zanetti M.
(1999).
Novel cathelicidins in horse leukocytes(1).
FEBS Lett, 457(3), 459-464.
https://doi.org/10.1016/s0014-5793(99)01097-2 Publication
Researcher Affiliations
- Laboratorio Nazionale Consorzio Interuniversitario Biotecnologie, AREA Science Park, Padriciano, I-34012, Trieste, Italy.
MeSH Terms
- Amino Acid Sequence
- Animals
- Antimicrobial Cationic Peptides / drug effects
- Antimicrobial Cationic Peptides / genetics
- Antimicrobial Cationic Peptides / metabolism
- Base Sequence
- Blood Proteins / genetics
- Blood Proteins / metabolism
- Blotting, Southern
- Blotting, Western
- Cathelicidins
- Cytoplasmic Granules / metabolism
- Horses / physiology
- Leukocytes / physiology
- Molecular Sequence Data
- Multigene Family / genetics
- Neutrophils / drug effects
- Neutrophils / metabolism
- Protein Precursors / genetics
- Protein Precursors / metabolism
- Reference Values
- Reverse Transcriptase Polymerase Chain Reaction
- Sequence Analysis
- Sequence Homology, Amino Acid
- Short Interspersed Nucleotide Elements / genetics
- Tetradecanoylphorbol Acetate / pharmacology
- Transcription, Genetic
Citations
This article has been cited 18 times.- Fingerhut L, Yücel L, Strutzberg-Minder K, von Köckritz-Blickwede M, Ohnesorge B, de Buhr N. Ex Vivo and In Vitro Analysis Identify a Detrimental Impact of Neutrophil Extracellular Traps on Eye Structures in Equine Recurrent Uveitis. Front Immunol 2022;13:830871.
- Zong X, Fu J, Xu B, Wang Y, Jin M. Interplay between gut microbiota and antimicrobial peptides. Anim Nutr 2020 Dec;6(4):389-396.
- Fingerhut L, Ohnesorge B, von Borstel M, Schumski A, Strutzberg-Minder K, Mörgelin M, Deeg CA, Haagsman HP, Beineke A, von Köckritz-Blickwede M, de Buhr N. Neutrophil Extracellular Traps in the Pathogenesis of Equine Recurrent Uveitis (ERU). Cells 2019 Nov 27;8(12).
- Grilz-Seger G, Druml T, Neuditschko M, Dobretsberger M, Horna M, Brem G. High-resolution population structure and runs of homozygosity reveal the genetic architecture of complex traits in the Lipizzan horse. BMC Genomics 2019 Mar 5;20(1):174.
- Cauchard S, Van Reet N, Büscher P, Goux D, Grötzinger J, Leippe M, Cattoir V, Laugier C, Cauchard J. Killing of Trypanozoon Parasites by the Equine Cathelicidin eCATH1. Antimicrob Agents Chemother 2016 May;60(5):2610-9.
- Dhaliwal KK, Arora JS, Mukhopadhyay CS, Dubey PP. In Silico Characterization of Functional Divergence of Two Cathelicidin Variants in Indian Sheep. Evol Bioinform Online 2015;11:189-96.
- Ferreira L, Pereira L, Faria R. Fluorescent dyes as a reliable tool in P2X7 receptor-associated pore studies. J Bioenerg Biomembr 2015 Aug;47(4):283-307.
- Wang G. Human antimicrobial peptides and proteins. Pharmaceuticals (Basel) 2014 May 13;7(5):545-94.
- Kościuczuk EM, Lisowski P, Jarczak J, Strzałkowska N, Jóźwik A, Horbańczuk J, Krzyżewski J, Zwierzchowski L, Bagnicka E. Cathelicidins: family of antimicrobial peptides. A review. Mol Biol Rep 2012 Dec;39(12):10957-70.
- Schlusselhuber M, Jung S, Bruhn O, Goux D, Leippe M, Leclercq R, Laugier C, Grötzinger J, Cauchard J. In vitro potential of equine DEFA1 and eCATH1 as alternative antimicrobial drugs in rhodococcosis treatment. Antimicrob Agents Chemother 2012 Apr;56(4):1749-55.
- Bruhn O, Grötzinger J, Cascorbi I, Jung S. Antimicrobial peptides and proteins of the horse--insights into a well-armed organism. Vet Res 2011 Sep 2;42(1):98.
- Leonard BC, Chu H, Johns JL, Gallo RL, Moore PF, Marks SL, Bevins CL. Expression and activity of a novel cathelicidin from domestic cats. PLoS One 2011 Apr 12;6(4):e18756.
- Di Nardo A, Yamasaki K, Dorschner RA, Lai Y, Gallo RL. Mast cell cathelicidin antimicrobial peptide prevents invasive group A Streptococcus infection of the skin. J Immunol 2008 Jun 1;180(11):7565-73.
- Chang CI, Zhang YA, Zou J, Nie P, Secombes CJ. Two cathelicidin genes are present in both rainbow trout (Oncorhynchus mykiss) and atlantic salmon (Salmo salar). Antimicrob Agents Chemother 2006 Jan;50(1):185-95.
- Skerlavaj B, Scocchi M, Gennaro R, Risso A, Zanetti M. Structural and functional analysis of horse cathelicidin peptides. Antimicrob Agents Chemother 2001 Mar;45(3):715-22.
- Wu H, Zhang G, Minton JE, Ross CR, Blecha F. Regulation of cathelicidin gene expression: induction by lipopolysaccharide, interleukin-6, retinoic acid, and Salmonella enterica serovar typhimurium infection. Infect Immun 2000 Oct;68(10):5552-8.
- Dzurová L, Holásková E, Pospíšilová H, Schneider Rauber G, Frébortová J. Cathelicidins: Opportunities and Challenges in Skin Therapeutics and Clinical Translation. Antibiotics (Basel) 2024 Dec 24;14(1).
- Zhang M, Liang W, Gong W, Yoshimura T, Chen K, Wang JM. The Critical Role of the Antimicrobial Peptide LL-37/ CRAMP in Protection of Colon Microbiota Balance, Mucosal Homeostasis, Anti-Inflammatory Responses, and Resistance to Carcinogenesis. Crit Rev Immunol 2019;39(2):83-92.
Use Nutrition Calculator
Check if your horse's diet meets their nutrition requirements with our easy-to-use tool Check your horse's diet with our easy-to-use tool
Talk to a Nutritionist
Discuss your horse's feeding plan with our experts over a free phone consultation Discuss your horse's diet over a phone consultation
Submit Diet Evaluation
Get a customized feeding plan for your horse formulated by our equine nutritionists Get a custom feeding plan formulated by our nutritionists
