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Inflammatory effect of cleaved bovine lactoferrin by elastase on staphylococcal mastitis
Yumiko Komine1, Toshinobu Kuroishi, Jin Kobayashi
1Intelligent Cosmos Research Institute Corporation, Sendia, Japan.
Bovine lactoferrin (bLf) cleavage by elastase during staphylococcal mastitis generates low-affinity bLf molecules. This process contributes to inflammation by activating immune responses in mammary epithelial cells.
Area of Science:
- Veterinary Immunology
- Biochemistry
- Molecular Biology
Background:
- Staphylococcal mastitis is a significant challenge in bovine health.
- Bovine lactoferrin (bLf) is an important immune-modulating protein in milk.
- The role of bLf modifications during mastitis requires further elucidation.
Purpose of the Study:
- To investigate the effect of elastase on bLf during bovine staphylococcal mastitis.
- To determine the inflammatory potential of elastase-modified bLf.
Main Methods:
- Detection of elastase activity and Concanavalin A (Con A) low-affinity bLf in mammary secretions.
- Treatment of bLf with elastase and analysis via Con A two-dimensional immunoelectrophoresis.
- Confirmation and synthesis of specific bLf peptides.
- Assessment of inflammatory gene expression (IL-6, TNFα, IL-8, MCP-1) in bovine mammary epithelial cells.
Main Results:
- Elastase activity and low Con A affinity bLf correlated with clinical mastitis severity.
- Elastase treatment of bLf produced smaller molecules with similar immunoelectrophoresis profiles to mastitic bLf.
- Four common bLf peptides were identified in elastase-treated and mastitic bLf.
- Low Con A affinity bLf and a specific synthetic peptide (GQRDLLFKDSAL) induced strong expression of inflammatory genes.
Conclusions:
- Elastase cleaves bLf in mastitic mammary glands, altering its physical properties and function.
- Elastase-induced low Con A affinity bLf, including the GQRDLLFKDSAL peptide, contributes to the inflammatory process in staphylococcal mastitis.
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