Milk osteopontin retains integrin-binding activity after in vitro gastrointestinal transit

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

Milk osteopontin retains integrin-binding activity after in vitro gastrointestinal transit. / Christensen, B; Karlsen, N J; Jørgensen, S D S; Jacobsen, L N; Ostenfeld, M S; Petersen, S V; Müllertz, A; Sørensen, E S.

I: Journal of Dairy Science, Bind 103, Nr. 1, 01.2020, s. 42-51.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Christensen, B, Karlsen, NJ, Jørgensen, SDS, Jacobsen, LN, Ostenfeld, MS, Petersen, SV, Müllertz, A & Sørensen, ES 2020, 'Milk osteopontin retains integrin-binding activity after in vitro gastrointestinal transit', Journal of Dairy Science, bind 103, nr. 1, s. 42-51. https://doi.org/10.3168/jds.2019-17212

APA

Christensen, B., Karlsen, N. J., Jørgensen, S. D. S., Jacobsen, L. N., Ostenfeld, M. S., Petersen, S. V., Müllertz, A., & Sørensen, E. S. (2020). Milk osteopontin retains integrin-binding activity after in vitro gastrointestinal transit. Journal of Dairy Science, 103(1), 42-51. https://doi.org/10.3168/jds.2019-17212

CBE

Christensen B, Karlsen NJ, Jørgensen SDS, Jacobsen LN, Ostenfeld MS, Petersen SV, Müllertz A, Sørensen ES. 2020. Milk osteopontin retains integrin-binding activity after in vitro gastrointestinal transit. Journal of Dairy Science. 103(1):42-51. https://doi.org/10.3168/jds.2019-17212

MLA

Vancouver

Christensen B, Karlsen NJ, Jørgensen SDS, Jacobsen LN, Ostenfeld MS, Petersen SV o.a. Milk osteopontin retains integrin-binding activity after in vitro gastrointestinal transit. Journal of Dairy Science. 2020 jan;103(1):42-51. https://doi.org/10.3168/jds.2019-17212

Author

Christensen, B ; Karlsen, N J ; Jørgensen, S D S ; Jacobsen, L N ; Ostenfeld, M S ; Petersen, S V ; Müllertz, A ; Sørensen, E S. / Milk osteopontin retains integrin-binding activity after in vitro gastrointestinal transit. I: Journal of Dairy Science. 2020 ; Bind 103, Nr. 1. s. 42-51.

Bibtex

@article{985d57dd93214f73b30ec8160bde53c0,
title = "Milk osteopontin retains integrin-binding activity after in vitro gastrointestinal transit",
abstract = "Osteopontin (OPN) is a multifunctional protein highly expressed in milk, where it is hypothesized to be involved in immunological signaling via the conserved Arg-Gly-Asp (RGD) integrin-binding sequence. Intervention studies have indicated beneficial effects of orally administered OPN in animal and human infants, but the mechanisms underlying these effects are not well described. To induce physiological effects, OPN must resist gastrointestinal transit in a bioactive form. In this study, we subjected bovine milk OPN to in vitro gastrointestinal transit, and characterized the generated fragments using monoclonal antibody and mass spectrometric analyses. We found that the fragment Trp27-Phe151 containing the integrin-binding RGD sequence resisted in vitro gastric digestion. This resistance was dependent on glycosylation of threonine residues near the integrin-binding sequence in both human and bovine milk OPN. Furthermore, the fragment Trp27-Phe151 retained the ability to interact with integrins in an RGD-dependent process. These results suggest a mechanism for how ingested milk OPN can induce physiological effects via integrin signaling in the intestine.",
keywords = "bioactive milk proteins, gastrointestinal digestion, infant formula, osteopontin",
author = "B Christensen and Karlsen, {N J} and J{\o}rgensen, {S D S} and Jacobsen, {L N} and Ostenfeld, {M S} and Petersen, {S V} and A M{\"u}llertz and S{\o}rensen, {E S}",
note = "Copyright {\textcopyright} 2020 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.",
year = "2020",
month = jan,
doi = "10.3168/jds.2019-17212",
language = "English",
volume = "103",
pages = "42--51",
journal = "Journal of Dairy Science",
issn = "0022-0302",
publisher = "Elsevier Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Milk osteopontin retains integrin-binding activity after in vitro gastrointestinal transit

AU - Christensen, B

AU - Karlsen, N J

AU - Jørgensen, S D S

AU - Jacobsen, L N

AU - Ostenfeld, M S

AU - Petersen, S V

AU - Müllertz, A

AU - Sørensen, E S

N1 - Copyright © 2020 American Dairy Science Association. Published by Elsevier Inc. All rights reserved.

PY - 2020/1

Y1 - 2020/1

N2 - Osteopontin (OPN) is a multifunctional protein highly expressed in milk, where it is hypothesized to be involved in immunological signaling via the conserved Arg-Gly-Asp (RGD) integrin-binding sequence. Intervention studies have indicated beneficial effects of orally administered OPN in animal and human infants, but the mechanisms underlying these effects are not well described. To induce physiological effects, OPN must resist gastrointestinal transit in a bioactive form. In this study, we subjected bovine milk OPN to in vitro gastrointestinal transit, and characterized the generated fragments using monoclonal antibody and mass spectrometric analyses. We found that the fragment Trp27-Phe151 containing the integrin-binding RGD sequence resisted in vitro gastric digestion. This resistance was dependent on glycosylation of threonine residues near the integrin-binding sequence in both human and bovine milk OPN. Furthermore, the fragment Trp27-Phe151 retained the ability to interact with integrins in an RGD-dependent process. These results suggest a mechanism for how ingested milk OPN can induce physiological effects via integrin signaling in the intestine.

AB - Osteopontin (OPN) is a multifunctional protein highly expressed in milk, where it is hypothesized to be involved in immunological signaling via the conserved Arg-Gly-Asp (RGD) integrin-binding sequence. Intervention studies have indicated beneficial effects of orally administered OPN in animal and human infants, but the mechanisms underlying these effects are not well described. To induce physiological effects, OPN must resist gastrointestinal transit in a bioactive form. In this study, we subjected bovine milk OPN to in vitro gastrointestinal transit, and characterized the generated fragments using monoclonal antibody and mass spectrometric analyses. We found that the fragment Trp27-Phe151 containing the integrin-binding RGD sequence resisted in vitro gastric digestion. This resistance was dependent on glycosylation of threonine residues near the integrin-binding sequence in both human and bovine milk OPN. Furthermore, the fragment Trp27-Phe151 retained the ability to interact with integrins in an RGD-dependent process. These results suggest a mechanism for how ingested milk OPN can induce physiological effects via integrin signaling in the intestine.

KW - bioactive milk proteins

KW - gastrointestinal digestion

KW - infant formula

KW - osteopontin

U2 - 10.3168/jds.2019-17212

DO - 10.3168/jds.2019-17212

M3 - Journal article

C2 - 31733850

VL - 103

SP - 42

EP - 51

JO - Journal of Dairy Science

JF - Journal of Dairy Science

SN - 0022-0302

IS - 1

ER -