Post-translational modification of osteopontin: Effects on in vitro hydroxyapatite formation and growth

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Post-translational modification of osteopontin: Effects on in vitro hydroxyapatite formation and growth. / Boskey, Adele L.; Christensen, Brian Søndergaard; Taleb, Hayat; Sørensen, Esben Skipper.

I: Biochemical and Biophysical Research Communications, Bind 419, Nr. 2, 09.03.2012, s. 333-338.

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

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Boskey, Adele L. o.a.. "Post-translational modification of osteopontin: Effects on in vitro hydroxyapatite formation and growth". Biochemical and Biophysical Research Communications. 2012, 419(2). 333-338. https://doi.org/10.1016/j.bbrc.2012.02.024

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Boskey, Adele L. ; Christensen, Brian Søndergaard ; Taleb, Hayat ; Sørensen, Esben Skipper. / Post-translational modification of osteopontin: Effects on in vitro hydroxyapatite formation and growth. I: Biochemical and Biophysical Research Communications. 2012 ; Bind 419, Nr. 2. s. 333-338.

Bibtex

@article{b93d8e475eaa48149a0bfeb3f7ba21a2,
title = "Post-translational modification of osteopontin: Effects on in vitro hydroxyapatite formation and growth",
abstract = "The manuscript tests the hypothesis that posttranslational modification of the SIBLING family of proteins in general and osteopontin in particular modify the abilities of these proteins to regulate in vitro hydroxyapatite (HA) formation. Osteopontin has diverse effects on hydroxyapatite (HA) mineral crystallite formation and growth depending on the extent of phosphorylation. We hypothesized that different regions of full-length OPN would also have distinct effects on the mineralization process. Thrombin fragmentation of milk OPN (mOPN) was used to test this hypothesis. Three fragments were tested in a de novo HA formation assay; an N-terminal fragment (aa 1–147), a central fragment (aa 148–204) denoted SKK-fragment and a C-terminal fragment (aa 205–262). Compared to intact mOPN the C- and N-terminal fragments behaved comparably, promoting HA formation and growth, but the central SKK-fragment acted as a mineralization inhibitor. In a seeded growth experiment all fragments inhibited mineral proliferation, but the SKK-fragment was the most effective inhibitor. These effects, seen in HA-formation and seeded growth assays in a gelatin gel system and in a pH-stat experiment were lost when the protein or fragments were dephosphorylated. Effects of the fully phosphorylated protein and fragments were also altered in the presence of fibrillar collagen. The diverse effects can be explained in terms of the intrinsically disordered nature of OPN and its fragments which enable them to interact with their multiple partners.",
keywords = "Osteopontin, Hydroxyapatite, SIBLING proteins, Mineralization mechanisms",
author = "Boskey, {Adele L.} and Christensen, {Brian S{\o}ndergaard} and Hayat Taleb and S{\o}rensen, {Esben Skipper}",
year = "2012",
month = "3",
day = "9",
doi = "10.1016/j.bbrc.2012.02.024",
language = "English",
volume = "419",
pages = "333--338",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier Inc",
number = "2",

}

RIS

TY - JOUR

T1 - Post-translational modification of osteopontin: Effects on in vitro hydroxyapatite formation and growth

AU - Boskey, Adele L.

AU - Christensen, Brian Søndergaard

AU - Taleb, Hayat

AU - Sørensen, Esben Skipper

PY - 2012/3/9

Y1 - 2012/3/9

N2 - The manuscript tests the hypothesis that posttranslational modification of the SIBLING family of proteins in general and osteopontin in particular modify the abilities of these proteins to regulate in vitro hydroxyapatite (HA) formation. Osteopontin has diverse effects on hydroxyapatite (HA) mineral crystallite formation and growth depending on the extent of phosphorylation. We hypothesized that different regions of full-length OPN would also have distinct effects on the mineralization process. Thrombin fragmentation of milk OPN (mOPN) was used to test this hypothesis. Three fragments were tested in a de novo HA formation assay; an N-terminal fragment (aa 1–147), a central fragment (aa 148–204) denoted SKK-fragment and a C-terminal fragment (aa 205–262). Compared to intact mOPN the C- and N-terminal fragments behaved comparably, promoting HA formation and growth, but the central SKK-fragment acted as a mineralization inhibitor. In a seeded growth experiment all fragments inhibited mineral proliferation, but the SKK-fragment was the most effective inhibitor. These effects, seen in HA-formation and seeded growth assays in a gelatin gel system and in a pH-stat experiment were lost when the protein or fragments were dephosphorylated. Effects of the fully phosphorylated protein and fragments were also altered in the presence of fibrillar collagen. The diverse effects can be explained in terms of the intrinsically disordered nature of OPN and its fragments which enable them to interact with their multiple partners.

AB - The manuscript tests the hypothesis that posttranslational modification of the SIBLING family of proteins in general and osteopontin in particular modify the abilities of these proteins to regulate in vitro hydroxyapatite (HA) formation. Osteopontin has diverse effects on hydroxyapatite (HA) mineral crystallite formation and growth depending on the extent of phosphorylation. We hypothesized that different regions of full-length OPN would also have distinct effects on the mineralization process. Thrombin fragmentation of milk OPN (mOPN) was used to test this hypothesis. Three fragments were tested in a de novo HA formation assay; an N-terminal fragment (aa 1–147), a central fragment (aa 148–204) denoted SKK-fragment and a C-terminal fragment (aa 205–262). Compared to intact mOPN the C- and N-terminal fragments behaved comparably, promoting HA formation and growth, but the central SKK-fragment acted as a mineralization inhibitor. In a seeded growth experiment all fragments inhibited mineral proliferation, but the SKK-fragment was the most effective inhibitor. These effects, seen in HA-formation and seeded growth assays in a gelatin gel system and in a pH-stat experiment were lost when the protein or fragments were dephosphorylated. Effects of the fully phosphorylated protein and fragments were also altered in the presence of fibrillar collagen. The diverse effects can be explained in terms of the intrinsically disordered nature of OPN and its fragments which enable them to interact with their multiple partners.

KW - Osteopontin

KW - Hydroxyapatite

KW - SIBLING proteins

KW - Mineralization mechanisms

U2 - 10.1016/j.bbrc.2012.02.024

DO - 10.1016/j.bbrc.2012.02.024

M3 - Journal article

C2 - 22342723

VL - 419

SP - 333

EP - 338

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -