Proteomics

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Human Angiogenin Cytoplasmic Interactomics

ABSTRACT: Human Angiogenin (hAng) is a member of the ribonuclease A superfamily and a potent inducer of neovascularization. Herein, protein interactions of hAng in the nucleus and cytoplasm of the human umbilical vein cell line EA.hy926, have been investigated by mass spectroscopy. The first gel-free analysis of hAng immunoprecipitates from the cytoplasmic and nuclear extracts from EA.hy926 cancer human cell line, revealed many statistically significant potential hAng-interacting proteins. The majority of the proteins identified by the mass spectrometry analysis are parts of multiprotein complexes, and some of them are common in nucleus and cytoplasm, including spliceosome, proteasome, and molecular chaperone TRiC/CCT. These complexes are involved in crucial biological pathways, implicating thus the key role of hAng in many vital cellular processes.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Endothelial Cell

SUBMITTER: Martina Samiotaki  

LAB HEAD: Maria Kontou

PROVIDER: PXD006583 | Pride | 2017-08-11

REPOSITORIES: Pride

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Publications

Proteomic Analysis of Human Angiogenin Interactions Reveals Cytoplasmic PCNA as a Putative Binding Partner.

Chatzileontiadou Demetra S M DSM   Samiotaki Martina M   Alexopoulou Annika N AN   Cotsiki Marina M   Panayotou George G   Stamatiadi Melina M   Balatsos Nikolaos A A NAA   Leonidas Demetres D DD   Kontou Maria M  

Journal of proteome research 20170908 10

Human Angiogenin (hAng) is a member of the ribonuclease A superfamily and a potent inducer of neovascularization. Protein interactions of hAng in the nucleus and cytoplasm of the human umbilical vein cell line EA.hy926 have been investigated by mass spectroscopy. Data are available via ProteomeXchange with identifiers PXD006583 and PXD006584. The first gel-free analysis of hAng immunoprecipitates revealed many statistically significant potential hAng-interacting proteins involved in crucial biol  ...[more]

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