Murine platelets are not regulated by O-linked β-N-acetylglucosamine

Garland L. Crawford; Gerald W. Hart; Sidney W. Whiteheart

doi:10.1016/j.abb.2008.03.014

Murine platelets are not regulated by O-linked β-N-acetylglucosamine

Garland L. Crawford, Gerald W. Hart, Sidney W. Whiteheart

Molecular and Cellular Biochemistry

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

It is generally appreciated that platelets derived from diabetic patients display increased responsiveness to low levels of agonists. O-GlcNAcylation has been linked to hyperglycemia-related effects in other tissues; therefore we examined this modification in platelets to determine if O-GlcNAcylation affects platelet function. This post-translational modification consists of an N-acetylglucosamine attached to serine and/or threonine residues. We examined O-GlcNAc levels in platelets from a hyperglycemic murine model of Type I diabetes with known hypersensitivity to agonists and a Type II diabetes model (ob/ob) lacking detectable alterations in the aggregation profile. Neither model showed marked increases in protein O-GlcNAcylation. Treatment of platelets with multiple O-GlcNAcase inhibitors led to O-GlcNAc accumulation on multiple platelet proteins. However, the inhibitor-induced accumulation of this modification does not correlate with any gross alterations in platelet aggregation. These data suggest that while the modification occurs in platelets, their activity is not globally sensitive to O-GlcNAc levels.

Original language	English
Pages (from-to)	220-224
Number of pages	5
Journal	Archives of Biochemistry and Biophysics
Volume	474
Issue number	1
DOIs	https://doi.org/10.1016/j.abb.2008.03.014
State	Published - Jun 1 2008

Bibliographical note

Funding Information:
We thank the members of the Whiteheart laboratory: Dr. Elena A. Matveeva, Dr. Zubair A. Karim, Wangsun Choi, Qiansheng Ren, Chunxia Zhao, Shaojing Ye, and Rania Al Hawas for their helpful discussions and careful reading of this manuscript. This work was supported by grants from the National Institutes of Health (HL081614 and HL56652) (to S.W.W.) and from the Ohio Valley Affiliate of the American Heart Association (0415111B) (to G.L.C.).

Keywords

Aggregation
Diabetes
O-GlcNAc
Platelets
Protein modification

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.abb.2008.03.014

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title = "Murine platelets are not regulated by O-linked β-N-acetylglucosamine",

abstract = "It is generally appreciated that platelets derived from diabetic patients display increased responsiveness to low levels of agonists. O-GlcNAcylation has been linked to hyperglycemia-related effects in other tissues; therefore we examined this modification in platelets to determine if O-GlcNAcylation affects platelet function. This post-translational modification consists of an N-acetylglucosamine attached to serine and/or threonine residues. We examined O-GlcNAc levels in platelets from a hyperglycemic murine model of Type I diabetes with known hypersensitivity to agonists and a Type II diabetes model (ob/ob) lacking detectable alterations in the aggregation profile. Neither model showed marked increases in protein O-GlcNAcylation. Treatment of platelets with multiple O-GlcNAcase inhibitors led to O-GlcNAc accumulation on multiple platelet proteins. However, the inhibitor-induced accumulation of this modification does not correlate with any gross alterations in platelet aggregation. These data suggest that while the modification occurs in platelets, their activity is not globally sensitive to O-GlcNAc levels.",

keywords = "Aggregation, Diabetes, O-GlcNAc, Platelets, Protein modification",

author = "Crawford, {Garland L.} and Hart, {Gerald W.} and Whiteheart, {Sidney W.}",

note = "Funding Information: We thank the members of the Whiteheart laboratory: Dr. Elena A. Matveeva, Dr. Zubair A. Karim, Wangsun Choi, Qiansheng Ren, Chunxia Zhao, Shaojing Ye, and Rania Al Hawas for their helpful discussions and careful reading of this manuscript. This work was supported by grants from the National Institutes of Health (HL081614 and HL56652) (to S.W.W.) and from the Ohio Valley Affiliate of the American Heart Association (0415111B) (to G.L.C.). ",

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AU - Whiteheart, Sidney W.

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N2 - It is generally appreciated that platelets derived from diabetic patients display increased responsiveness to low levels of agonists. O-GlcNAcylation has been linked to hyperglycemia-related effects in other tissues; therefore we examined this modification in platelets to determine if O-GlcNAcylation affects platelet function. This post-translational modification consists of an N-acetylglucosamine attached to serine and/or threonine residues. We examined O-GlcNAc levels in platelets from a hyperglycemic murine model of Type I diabetes with known hypersensitivity to agonists and a Type II diabetes model (ob/ob) lacking detectable alterations in the aggregation profile. Neither model showed marked increases in protein O-GlcNAcylation. Treatment of platelets with multiple O-GlcNAcase inhibitors led to O-GlcNAc accumulation on multiple platelet proteins. However, the inhibitor-induced accumulation of this modification does not correlate with any gross alterations in platelet aggregation. These data suggest that while the modification occurs in platelets, their activity is not globally sensitive to O-GlcNAc levels.

AB - It is generally appreciated that platelets derived from diabetic patients display increased responsiveness to low levels of agonists. O-GlcNAcylation has been linked to hyperglycemia-related effects in other tissues; therefore we examined this modification in platelets to determine if O-GlcNAcylation affects platelet function. This post-translational modification consists of an N-acetylglucosamine attached to serine and/or threonine residues. We examined O-GlcNAc levels in platelets from a hyperglycemic murine model of Type I diabetes with known hypersensitivity to agonists and a Type II diabetes model (ob/ob) lacking detectable alterations in the aggregation profile. Neither model showed marked increases in protein O-GlcNAcylation. Treatment of platelets with multiple O-GlcNAcase inhibitors led to O-GlcNAc accumulation on multiple platelet proteins. However, the inhibitor-induced accumulation of this modification does not correlate with any gross alterations in platelet aggregation. These data suggest that while the modification occurs in platelets, their activity is not globally sensitive to O-GlcNAc levels.

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Murine platelets are not regulated by O-linked β-N-acetylglucosamine

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

UN SDGs

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