Role of group-specific component (vitamin D binding protein) in clearance of actin from the circulation in the rabbit.

Goldschmidt‐Clermont, Pascal J.; Baelen, Hugo Van; Bouillon, Roger; Shook, Thomas E.; Williams, Merfyn H.; Nel, André E.; Galbraith, Robert M.

doi:10.1172/jci113484

Cited by 49 publications

(25 citation statements)

References 62 publications

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“…The concomitant decrease in Gc total to a nadir on day one could be caused by the clearance of Gc-globulin-actin complexes from the circulation. Since the plasma half life of Gc-globulin unbound to actin is in the magnitude of 12 to 24 h and the half life of Gc-globulin complexed to actin is around 30 min, an increase in Gc complexed would lead to a more rapid turnover of Gc total [18,19]. This could explain why the nadir level for Gc total is seen on day one, whereas the maximum level of Gc complexed is seen on day three.…”

Section: Discussionmentioning

confidence: 99%

Gc-globulin is an acute phase reactant and an indicator of muscle injury after spinal surgery

Dahl

Schiødt

Gehrchen

et al. 2001

Inflammation Research

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The initial changes in Gc-globulin can be explained by increased release of actin from injured muscle tissue. Subsequently Gc-globulin displays characteristics of a so-called positive acute phase reactant, supporting previous in vitro studies, and clinical studies after minor surgery. In spite of genetic linkage and structural homology Gc-globulin and albumin are regulated differently after surgical trauma.

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Section: Discussionmentioning

confidence: 99%

Gc-globulin is an acute phase reactant and an indicator of muscle injury after spinal surgery

Dahl

Schiødt

Gehrchen

et al. 2001

Inflammation Research

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“…In contrast to our expectations, few hemoglobin-derived peptides and no actin-derived peptides were identified. In fact, both hemoglobin and actin are actively sequestered and cleared from the serum via the abundant serum proteins haptoglobin and vitamin D-binding protein, respectively (42)(43)(44)(45). Another example of unexpected results are the identification of immunoglobulin-derived peptides, although depletion was complete when evaluated by SDS-PAGE.…”

Section: Table II Proteins Found Comparing a Single Ms/ms Analysis Tomentioning

confidence: 99%

Toward a Human Blood Serum Proteome

Adkins

Varnum

Auberry

et al. 2002

Molecular & Cellular Proteomics

720

375

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Blood serum is a complex body fluid that contains various proteins ranging in concentration over at least 9 orders of magnitude. Using a combination of mass spectrometry technologies with improvements in sample preparation, we have performed a proteomic analysis with submilliliter quantities of serum and increased the measurable concentration range for proteins in blood serum beyond previous reports. We have detected 490 proteins in serum by on-line reversed-phase microcapillary liquid chromatography coupled with ion trap mass spectrometry. To perform this analysis, immunoglobulins were removed from serum using protein A/G, and the remaining proteins were digested with trypsin. Resulting peptides were separated by strong cation exchange chromatography into distinct fractions prior to analysis. This separation resulted in a 3-5-fold increase in the number of proteins detected in an individual serum sample. With this increase in the number of proteins identified we have detected some lower abundance serum proteins (ng/ml range) including human growth hormone, interleukin-12, and prostate-specific antigen. We also used SEQUEST to compare different protein databases with and without filtering. This comparison is plotted to allow for a quick visual assessment of different databases as a subjective measure of analytical quality. With this study, we have performed the most extensive analysis of serum proteins to date and laid the foundation for future refinements in the identification of novel protein biomarkers of disease.Molecular & Cellular Proteomics 1:947-955, 2002.

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“…In human (19)(20)(21)(22) and experimental (23) conditions characterized by extensive tissue injury, actin-DBP and actin-gelsolin complexes have been found in plasma. The intravenous injection of small amounts of actin into animals results in its association with these two plasma proteins (24)(25)(26), further suggesting their roles in a putative mechanism for protection against the formation, growth, and perseverance of circulating microfilaments. In the present studies, we tested the hypothesis that a plasma actin-scavenger system would protect animals from increasing amounts of infused G-actin until the actin-binding capacity was saturated.…”

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confidence: 99%

Angiopathic consequences of saturating the plasma scavenger system for actin.

Haddad

Harper

Guoth

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

168

107

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Two plasma proteins, vitamin D-binding protein (actin monomer sequestrant) and gelsolin (actin polymer severing), have been found in association with actin in plasma from ill humans and during experimental injury. In vitro, these are the only plasma proteins that display a high affinity for actin. We infused increasing amounts of globular actin intravenously to rats to evaluate its disposition in plasma and tissues. Intravascular filament formation, microthrombi, and endothelial injury were observed, especially in the pulmonary circulation. These pathological changes were not observed when the globular actin in the infusate had been preincubated with the vitamin D-binding protein in vitro. Complexes of actin with both proteins were found in the plasma, suggesting a saturable, plasma actin-binding system in vivo. Our findings suggest that in vivo saturation of these proteins' actin-binding capacities may serve as a paradigm for pulmonary vascular disorders seen during widespread tissue trauma and cell lysis.

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Role of group-specific component (vitamin D binding protein) in clearance of actin from the circulation in the rabbit.

Cited by 49 publications

References 62 publications

Gc-globulin is an acute phase reactant and an indicator of muscle injury after spinal surgery

Gc-globulin is an acute phase reactant and an indicator of muscle injury after spinal surgery

Toward a Human Blood Serum Proteome

Angiopathic consequences of saturating the plasma scavenger system for actin.

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