Deep coverage mouse red blood cell proteome: a first comparison with the human red blood cell

Erica M Pasini, Morten Kirkegaard, Doris Salerno, Peter V. Mortensen, Matthias Mann, Alan W Thomas

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 2008-Jul
OriginalsprogEngelsk
TidsskriftMolecular and Cellular Proteomics
Vol/bind7
Udgave nummer7
Sider (fra-til)1317-1330
Antal sider13
ISSN1535-9476
DOI
StatusUdgivet - 1. jul. 2008

Fingeraftryk

Proteome
Blood
Cells
Cytology
Membranes
Proteins
Mammals
Malaria
Cell Biology
Vertebrates
Biomedical Research
Protein Isoforms
Parasites
Molecular Weight
Gases
Molecular weight
Cell Membrane
Peptides
Research

Citer dette

Pasini, E. M., Kirkegaard, M., Salerno, D., Mortensen, P. V., Mann, M., & Thomas, A. W. (2008). Deep coverage mouse red blood cell proteome: a first comparison with the human red blood cell. Molecular and Cellular Proteomics, 7(7), 1317-1330. https://doi.org/10.1074/mcp.M700458-MCP200
Pasini, Erica M ; Kirkegaard, Morten ; Salerno, Doris ; Mortensen, Peter V. ; Mann, Matthias ; Thomas, Alan W. / Deep coverage mouse red blood cell proteome: a first comparison with the human red blood cell. I: Molecular and Cellular Proteomics. 2008 ; Bind 7, Nr. 7. s. 1317-1330.
@article{1bbe6590ee2b11dd84b0000ea68e967b,
title = "Deep coverage mouse red blood cell proteome: a first comparison with the human red blood cell",
abstract = "Mice have close genetic/physiological relationships to humans, breed rapidly, and can be genetically modified, making them the most used mammal in biomedical research. Because the red blood cell (RBC) is the sole gas transporter in vertebrates, diseases of the RBC are frequently severe; much research has therefore focused on RBC and cardiovascular disorders of mouse and humans. RBCs also host malaria parasites. Recently we presented an in-depth proteome for the human RBC. Here we present directly comparable data for the mouse RBC as membrane-only, soluble-only, and combined membrane-bound/soluble proteomes (comprising, respectively, 247, 232, and 165 proteins). All proteins were identified, validated, and categorized in terms of subcellular localization, protein family, and function, and in comparison with the human RBC, were classified as orthologs, family-related, or unique. Splice isoforms were identified, and polypeptides migrating with anomalous apparent molecular weights were grouped into putatively ubiquitinated or partially degraded complexes. Overall there was close concordance between mouse and human proteomes, confirming the unexpected RBC complexity. Several novel findings in the human proteome have been confirmed here. This comparison sheds light on several open issues in RBC biology and provides a departure point for more comprehensive understanding of RBC function.",
keywords = "Amino Acid Sequence, Animals, Cluster Analysis, Cytosol, Databases, Protein, Erythrocytes, Humans, Membrane Proteins, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Protein Isoforms, Proteome, Sequence Homology, Amino Acid",
author = "Pasini, {Erica M} and Morten Kirkegaard and Doris Salerno and Mortensen, {Peter V.} and Matthias Mann and Thomas, {Alan W}",
year = "2008",
month = "7",
day = "1",
doi = "10.1074/mcp.M700458-MCP200",
language = "English",
volume = "7",
pages = "1317--1330",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology",
number = "7",

}

Pasini, EM, Kirkegaard, M, Salerno, D, Mortensen, PV, Mann, M & Thomas, AW 2008, 'Deep coverage mouse red blood cell proteome: a first comparison with the human red blood cell', Molecular and Cellular Proteomics, bind 7, nr. 7, s. 1317-1330. https://doi.org/10.1074/mcp.M700458-MCP200

Deep coverage mouse red blood cell proteome: a first comparison with the human red blood cell. / Pasini, Erica M; Kirkegaard, Morten; Salerno, Doris; Mortensen, Peter V.; Mann, Matthias; Thomas, Alan W.

I: Molecular and Cellular Proteomics, Bind 7, Nr. 7, 01.07.2008, s. 1317-1330.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Deep coverage mouse red blood cell proteome: a first comparison with the human red blood cell

AU - Pasini, Erica M

AU - Kirkegaard, Morten

AU - Salerno, Doris

AU - Mortensen, Peter V.

AU - Mann, Matthias

AU - Thomas, Alan W

PY - 2008/7/1

Y1 - 2008/7/1

N2 - Mice have close genetic/physiological relationships to humans, breed rapidly, and can be genetically modified, making them the most used mammal in biomedical research. Because the red blood cell (RBC) is the sole gas transporter in vertebrates, diseases of the RBC are frequently severe; much research has therefore focused on RBC and cardiovascular disorders of mouse and humans. RBCs also host malaria parasites. Recently we presented an in-depth proteome for the human RBC. Here we present directly comparable data for the mouse RBC as membrane-only, soluble-only, and combined membrane-bound/soluble proteomes (comprising, respectively, 247, 232, and 165 proteins). All proteins were identified, validated, and categorized in terms of subcellular localization, protein family, and function, and in comparison with the human RBC, were classified as orthologs, family-related, or unique. Splice isoforms were identified, and polypeptides migrating with anomalous apparent molecular weights were grouped into putatively ubiquitinated or partially degraded complexes. Overall there was close concordance between mouse and human proteomes, confirming the unexpected RBC complexity. Several novel findings in the human proteome have been confirmed here. This comparison sheds light on several open issues in RBC biology and provides a departure point for more comprehensive understanding of RBC function.

AB - Mice have close genetic/physiological relationships to humans, breed rapidly, and can be genetically modified, making them the most used mammal in biomedical research. Because the red blood cell (RBC) is the sole gas transporter in vertebrates, diseases of the RBC are frequently severe; much research has therefore focused on RBC and cardiovascular disorders of mouse and humans. RBCs also host malaria parasites. Recently we presented an in-depth proteome for the human RBC. Here we present directly comparable data for the mouse RBC as membrane-only, soluble-only, and combined membrane-bound/soluble proteomes (comprising, respectively, 247, 232, and 165 proteins). All proteins were identified, validated, and categorized in terms of subcellular localization, protein family, and function, and in comparison with the human RBC, were classified as orthologs, family-related, or unique. Splice isoforms were identified, and polypeptides migrating with anomalous apparent molecular weights were grouped into putatively ubiquitinated or partially degraded complexes. Overall there was close concordance between mouse and human proteomes, confirming the unexpected RBC complexity. Several novel findings in the human proteome have been confirmed here. This comparison sheds light on several open issues in RBC biology and provides a departure point for more comprehensive understanding of RBC function.

KW - Amino Acid Sequence

KW - Animals

KW - Cluster Analysis

KW - Cytosol

KW - Databases, Protein

KW - Erythrocytes

KW - Humans

KW - Membrane Proteins

KW - Mice

KW - Mice, Inbred C57BL

KW - Molecular Sequence Data

KW - Protein Isoforms

KW - Proteome

KW - Sequence Homology, Amino Acid

U2 - 10.1074/mcp.M700458-MCP200

DO - 10.1074/mcp.M700458-MCP200

M3 - Journal article

VL - 7

SP - 1317

EP - 1330

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 7

ER -