Increase in phosphotidylinositide-3 kinase activity by nitrotyrosylation of lysates of platelets from patients with systemic sclerosis

Thomas M. Chiang, Arnold Postlethwaite

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4 Citations (Scopus)

Abstract

We have observed that the platelet non-integrin collagen receptor (65 kDa) and another protein (Mr 185 kDa) are altered in the posttranslational modification by nitrotyrosylation in platelets from patients with systemic sclerosis (SSc). We reported the identification of nitrotyrosylated 65-kDa proteins in a previous study. In the present investigation, using Western blots, one- and two-dimensional gel electrophoreses and matrix assisted ionization/desorption-time of flight (MALDI-TOF) we have identified the 185-kDa protein as phosphoinositide kinase C2β (PI 3-K). There is a positive correlation between the nitrotyrosylation of PI 3-K and activity of the enzyme, i.e., the nitrotyrosylation of PI 3-K increases its enzymatic activity. In addition, the activity of PI 3-K increases in nitrotyrosylated platelet lystaes from patients with SSc compared to normal volunteer controls, suggesting that this is an alteration in the posttranslational modification of PI 3-K in platelets from patients with SSc. The increased nitrotyrosylation of PI 3-K may contribute to the impairment of platelet function in patients with SSc by increasing platelet reactivity to matrix components within the vascular walls of patients with this disease.

Original languageEnglish (US)
Pages (from-to)32-37
Number of pages6
JournalBiochimica et Biophysica Acta - General Subjects
Volume1760
Issue number1
DOIs
StatePublished - Jan 1 2006

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Systemic Scleroderma
Platelets
Phosphotransferases
Blood Platelets
Post Translational Protein Processing
Collagen Receptors
Proteins
1-Phosphatidylinositol 4-Kinase
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Ionization
Blood Vessels
Desorption
Healthy Volunteers
Western Blotting
Gels
Enzymes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

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title = "Increase in phosphotidylinositide-3 kinase activity by nitrotyrosylation of lysates of platelets from patients with systemic sclerosis",
abstract = "We have observed that the platelet non-integrin collagen receptor (65 kDa) and another protein (Mr 185 kDa) are altered in the posttranslational modification by nitrotyrosylation in platelets from patients with systemic sclerosis (SSc). We reported the identification of nitrotyrosylated 65-kDa proteins in a previous study. In the present investigation, using Western blots, one- and two-dimensional gel electrophoreses and matrix assisted ionization/desorption-time of flight (MALDI-TOF) we have identified the 185-kDa protein as phosphoinositide kinase C2β (PI 3-K). There is a positive correlation between the nitrotyrosylation of PI 3-K and activity of the enzyme, i.e., the nitrotyrosylation of PI 3-K increases its enzymatic activity. In addition, the activity of PI 3-K increases in nitrotyrosylated platelet lystaes from patients with SSc compared to normal volunteer controls, suggesting that this is an alteration in the posttranslational modification of PI 3-K in platelets from patients with SSc. The increased nitrotyrosylation of PI 3-K may contribute to the impairment of platelet function in patients with SSc by increasing platelet reactivity to matrix components within the vascular walls of patients with this disease.",
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AU - Postlethwaite, Arnold

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N2 - We have observed that the platelet non-integrin collagen receptor (65 kDa) and another protein (Mr 185 kDa) are altered in the posttranslational modification by nitrotyrosylation in platelets from patients with systemic sclerosis (SSc). We reported the identification of nitrotyrosylated 65-kDa proteins in a previous study. In the present investigation, using Western blots, one- and two-dimensional gel electrophoreses and matrix assisted ionization/desorption-time of flight (MALDI-TOF) we have identified the 185-kDa protein as phosphoinositide kinase C2β (PI 3-K). There is a positive correlation between the nitrotyrosylation of PI 3-K and activity of the enzyme, i.e., the nitrotyrosylation of PI 3-K increases its enzymatic activity. In addition, the activity of PI 3-K increases in nitrotyrosylated platelet lystaes from patients with SSc compared to normal volunteer controls, suggesting that this is an alteration in the posttranslational modification of PI 3-K in platelets from patients with SSc. The increased nitrotyrosylation of PI 3-K may contribute to the impairment of platelet function in patients with SSc by increasing platelet reactivity to matrix components within the vascular walls of patients with this disease.

AB - We have observed that the platelet non-integrin collagen receptor (65 kDa) and another protein (Mr 185 kDa) are altered in the posttranslational modification by nitrotyrosylation in platelets from patients with systemic sclerosis (SSc). We reported the identification of nitrotyrosylated 65-kDa proteins in a previous study. In the present investigation, using Western blots, one- and two-dimensional gel electrophoreses and matrix assisted ionization/desorption-time of flight (MALDI-TOF) we have identified the 185-kDa protein as phosphoinositide kinase C2β (PI 3-K). There is a positive correlation between the nitrotyrosylation of PI 3-K and activity of the enzyme, i.e., the nitrotyrosylation of PI 3-K increases its enzymatic activity. In addition, the activity of PI 3-K increases in nitrotyrosylated platelet lystaes from patients with SSc compared to normal volunteer controls, suggesting that this is an alteration in the posttranslational modification of PI 3-K in platelets from patients with SSc. The increased nitrotyrosylation of PI 3-K may contribute to the impairment of platelet function in patients with SSc by increasing platelet reactivity to matrix components within the vascular walls of patients with this disease.

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