Lactoferrin (Lf) is an iron-binding protein and belongs to the serum transferrin family. It has broad spectrum antimicrobial action, and it is found in exocrine secretions including milk. The sequence of the bovine lactoferrin gene promoter was analyzed in five different cattle breeds (Holstein Friesian, New Zealand Holstein, Montebéliard, Normande, and Norwegian Red) to determine the extent of polymorphic variation, which exists in this region both within and across cattle breeds. Fifteen different single nucleotide polymorphisms (SNPs) were identified throughout this region. Numerous polymorphisms were found throughout the Holstein Friesian, New Zealand Holstein, Montebéliard, and Normande populations. The most frequently encountered polymorphism found in all breeds was at position -28, which is immediately proximal to the TATA box of the promoter. The most variable base position was -131, which included three types of heterozygotes including a single base deletion in one allele, and three homozygote variants. This polymorphism occurs in a putative transcription factor binding site, for the nuclear factor of activated T cells (NF-ATc). A unique polymorphism was identified in one Normande animal, and three polymorphisms were found in one Montebéliard animal. In general, Norwegian Red cattle displayed fewer SNPs than other breeds. Most nucleotide changes in these animals were within the 190 base pairs of the transcription start point, with the exception of an insertion seen in three animals at position -478. In conclusion, SNPs were found in abundance throughout this regulatory region. Whether or not these polymorphisms have an effect on the regulation of the bovine lactoferrin gene is yet to be elucidated. However, the identification of lactoferrin promoter variants may serve as a marker for healthier animals, thereby accelerating the improvement of animals through breeding.
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http://dx.doi.org/10.1080/10495390500460965 | DOI Listing |
Life (Basel)
January 2025
College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot 010010, China.
Lactoferrin (LF), a member of the transferrin family, is widely present in mammalian milk and other secretions, exhibiting anti-inflammatory, antibacterial, and anti-infective properties. Although the biological functions of LF have been extensively studied, there are few reports on its effects and molecular mechanisms concerning bovine mastitis caused by bacterial infection. This study used bovine mammary epithelial cells (BMECs) cultured in vitro as the research model.
View Article and Find Full Text PDFAntioxidants (Basel)
December 2024
Department of Radiation Disaster Medicine, Research Institute for Radiation Biology and Medicine, Hiroshima University, Hiroshima 734-8553, Japan.
Lactoferrin (LF) is an iron-binding glycoprotein of the transferrin family and has been suggested to have a variety of biological functions, including anticancer activity. However, the effects of LF and its mechanisms in anticancer therapies, especially in radiotherapy against cancer cells under hypoxic conditions, are not well-determined. In this study, we focused on the molecular mechanisms of LF functions in cells under hypoxic conditions.
View Article and Find Full Text PDFToxicol Rep
June 2025
Therapeutic Chemistry Department, Pharmaceutical and Drug Industries Research Institute, National Research Centre, El Buhouth St., Dokki, Cairo 12622, Egypt.
Doxorubicin (DOX) is a powerful antineoplastic FDA-approved anthracycline-derived antibiotic and is considered as the most suitable intervention for solid tumors and hematological cancers therapy. However, its therapeutic application is highly limited due to acute and chronic renal, hematological and testicular toxicity. Oxidative stress, lipid peroxidation and apoptosis in germ cells as well as low sperm count, motility and disturbing steroidogenesis are the principal machineries of DOX-induced testicular toxicity.
View Article and Find Full Text PDFBiochem Cell Biol
January 2025
Department of Microbiology, Immunology, and Infectious Diseases, Snyder Institute, Cumming School of Medicine, University of Calgary, Calgary, AB, Canada.
Surface receptors in Gram-negative bacteria that bind and extract iron from the host glycoproteins transferrin (Tf) or lactoferrin (Lf) was discovered 35 years ago in pathogenic species and subsequently was discovered in other pathogens of humans and food production animals. These bacterial species reside exclusively on the mucosal surfaces of the respiratory or genitourinary tract of their mammalian host and rely on their host specific Tf and Lf receptors to acquire iron for survival. Since the specificity of the bacterial Tf receptors was shown to be due to selective pressures on the host Tf, their presence in bacteria that reside in both mammals and birds indicates that they arose over 320 million years ago.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Department of Molecular Pathophysiology, Wakayama Medical University, Wakayama 641-8509, Japan.
Plasmacytoid dendritic cells (pDCs) express Toll-like receptor 7 (TLR7) in the endosomes, recognize viral single-stranded RNA (ssRNA), and produce significant amounts of interferon (IFN)-α. Bovine lactoferrin (LF) enhances the response of IFN regulatory factors followed by the activation of IFN-sensitive response elements located in the promoter regions of the gene and IFN-stimulated genes in the TLR7 reporter THP-1 cells in the presence of R-848, a TLR7 agonist. In ex vivo experiments using human peripheral blood mononuclear cells, LF enhances IFN-α levels in the supernatant in the presence of R-848.
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