Serum leucine-rich alpha-2-glycoprotein-1 binds cytochrome c and inhibits antibody detection of this apoptotic marker in enzyme-linked immunosorbent assay

@article{Cummings2006SerumLA,
  title={Serum leucine-rich alpha-2-glycoprotein-1 binds cytochrome c and inhibits antibody detection of this apoptotic marker in enzyme-linked immunosorbent assay},
  author={C. Cummings and Jennifer Walder and A. Treeful and R. Jemmerson},
  journal={Apoptosis},
  year={2006},
  volume={11},
  pages={1121-1129}
}
Cytochrome c (Cyt c) has been implicated as a serum marker for aberrant apoptosis and, thus, has considerable clinical potential. Using a sandwich enzyme-linked immunosorbent assay (ELISA) we found that the sensitivity of Cyt c detection is reduced in the presence of serum. The inhibitory factor responsible was purified from both fetal bovine serum and human serum employing standard chromatography procedures followed by affinity chromatography on Affi-Gel 10-bound Cyt c. In SDS-PAGE, bands at… Expand
ELISA for human serum leucine-rich alpha-2-glycoprotein-1 employing cytochrome c as the capturing ligand
TLDR
An indirect enzyme-linked immunosorbent assay (ELISA) for quantifying LRG in human serum is described in which cytochrome c is employed as the capturing ligand and a monoclonal antibody specific for LRG is used to detect the captured glycoprotein. Expand
Autologous extracellular cytochrome c is an endogenous ligand for leucine-rich alpha2-glycoprotein and beta-type phospholipase A2 inhibitor.
TLDR
The results suggest that autologous Cyt c is an endogeneous ligand for LRG and PLIbeta and that these serum proteins neutralize the autologueous CyT c released from the dead cells. Expand
Cytochrome c-induced lymphocyte death from the outside in: inhibition by serum leucine-rich alpha-2-glycoprotein-1
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It is found that serum LRG when bound to extracellular Cyt c that is released from apoptotic cells acts as a survival factor for lymphocytes and possibly other cells that are susceptible to the toxic effect ofextracellularCyt c. Expand
Intracellular leucine-rich alpha-2-glycoprotein-1 competes with Apaf-1 for binding cytochrome c in protecting MCF-7 breast cancer cells from apoptosis
TLDR
It is proposed that intracellular LRG1 raises the threshold of cytoplasmic Cyt c required to induce apoptosis and, thus, prevents onset of the intrinsic pathway in cells whereCyt c release from mitochondria does not result from committed apoptotic signaling. Expand
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TLDR
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Peroxidase activity of cytochrome c in its compact state depends on dynamics of the heme region.
TLDR
The results suggest that dynamic equilibrium among the denaturant-induced non-native coordination states of cyt c, very likely due to reversible unfolding of the least stable foldons, is pre-requisite for enhanced peroxidase-like activity of cytc in its compact state. Expand
Heightened Dynamics of the Oxidized Y48H Variant of Human Cytochrome c Increases Its Peroxidatic Activity.
TLDR
A dynamic picture associated with this disease relative to cy tochrome c is emerging whereby increasing dynamics in substructures of the cytochrome c fold serve to facilitate an increased population of the peroxidatic pentacoordinate heme state. Expand
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