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15:06
Synthesis of an Intein-mediated Artificial Protein Hydrogel
Published on: January 27, 2014
Recombinant human intelectin binds bovine lactoferrin and its peptides
Kouichirou Shin1, Hiroyuki Wakabayashi, Koji Yamauchi
1Food Science & Technology Institute, Morinaga Milk Industry Co., Ltd, Kanagawa, Japan. k_shin@morniagamilk.co.jp
Biological & Pharmaceutical Bulletin
|August 2, 2008
Summary
Human intelectin (hIntL), a small intestine protein, binds bovine lactoferrin (bLF) more effectively than human lactoferrin (hLF). This suggests hIntL acts as a receptor for bLF and its breakdown products.
Area of Science:
- Biochemistry
- Immunology
- Gastroenterology
Background:
- Intelectin (IntL) is a small intestine lectin involved in innate immunity.
- IntL functions as a receptor for lactoferrin (LF), an iron-binding glycoprotein.
- Both human LF (hLF) and bovine LF (bLF) influence human enterocyte proliferation, differentiation, and cytokine production.
Purpose of the Study:
- To investigate the interaction and binding affinity between human intelectin (hIntL) and bovine lactoferrin (bLF).
Main Methods:
- Recombinant hIntL (rhIntL) was produced with a tag sequence.
- Ligand-binding assays were performed using microtiter plates coated with bLF, hLF, and other proteins.
- Binding capacity of rhIntL to coated ligands was quantified.
Main Results:
- rhIntL exhibited higher binding affinity for bLF compared to hLF.
- rhIntL also bound to pepsin hydrolysate of bLF, though to a lesser extent than native bLF.
- Minimal binding of rhIntL was observed for bovine serum albumin and transferrin.
Conclusions:
- Human intelectin (hIntL) functions as a receptor for bovine lactoferrin (bLF).
- hIntL can also bind to digested fragments of bLF.
- These findings elucidate a specific molecular interaction in the gastrointestinal tract.
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