AMID: new insights on its intracellular localization and expression at apoptosis

AMID (apoptosis-inducing factor (AIF)-like mitochondrion-associated inducer of death) is a poorly studied member of the AIF family; despite the given name AMID, predicting its association with mitochondria, its real cellular localization, as well as its role and changes during apoptosis are currentl...

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Bibliographic Details
Published in:Apoptosis (London) 2008-05, Vol.13 (5), p.729-732
Main Authors: Bilyy, Rostyslav, Kit, Yuriy, Hellman, Ulf, Stoika, Rostyslav
Format: Article
Language:English
Subjects:
AIF
AMID
Animals
Antibodies, Monoclonal
Apoptosis
Apoptosis - physiology
Apoptosis Regulatory Proteins - immunology
Apoptosis Regulatory Proteins - isolation & purification
Apoptosis Regulatory Proteins - physiology
Biochemistry
Biomedical and Life Sciences
Biomedicine
Cancer Research
Cell Biology
Cell Membrane - chemistry
Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Glycosylation
Humans
Jurkat Cells
Lectin
Leukemia
Leukemia L1210
MALDI-TOF MS
Mass spectrometry
MEDICIN
MEDICINE
Mice
Mitochondrial Proteins - immunology
Mitochondrial Proteins - physiology
Oncology
Oxidoreductases
Plasma membrane
Short Communication
Silica
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Virology
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Summary:AMID (apoptosis-inducing factor (AIF)-like mitochondrion-associated inducer of death) is a poorly studied member of the AIF family; despite the given name AMID, predicting its association with mitochondria, its real cellular localization, as well as its role and changes during apoptosis are currently unclear. By means of MALDI-TOF mass spectrometry, we have identified as AMID (accession number AAH38129, sequence coverage 31%) the protein isolated by Pisum sativum lectin-affinity chromatography from the plasma membrane fraction of apoptotic murine leukemia L1210 cells, lacking in the intact cells. The obtained results suggest its possible glycosylation that was further suggested by finding N-glycosylation sequon in the signal peptide of AMID protein (in silica), and by predicting transmembrane localization of its N-terminal part. Using monoclonal antibodies to AMID, we demonstrated an increased expression of AMID in human leukemia Jurkat T-cells after apoptosis induction. Immunocytochemical study suggested its association to the plasma membrane.
ISSN:1360-8185
1573-675X
1573-675X
DOI:10.1007/s10495-008-0198-5