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Peroxisomes are a class of ubiquitous and dynamic single
membrane-bounded cell organelles, devoid of DNA, with an
essentially oxidative type of metabolism. In recent years it has
become increasingly clear that peroxisomes are involved in a range
of important cellular functions in almost all eukaryotic cells. In
higher eukaryotes, including humans, peroxisomes catalyze ether
phospholipids biosynthesis, fatty acid alpha-oxidation, glyoxylate
detoxification, etc, and in humans peroxisomes are associated with
several important genetic diseases. In plants, peroxisomes carry
out the fatty acid beta-oxidation, photorespiration, metabolism of
ROS, RNS and RSS, photomorphogenesis, biosynthesis of
phytohormones, senescence, and defence against pathogens and
herbivores. In recent years it has been postulated a possible
contribution of peroxisomes to cellular signaling. In this volume
an updated view of the capacity and function of peroxisomes from
human, animal, fungal and plant origin as cell generators of
different signal molecules involved in distinct processes of high
physiological importance is presented.
Oxygen (O ) appeared in significant amounts in the Earth's
atmosphere over 2. 2 2 billion years ago, largely due to the
evolution of photosynthesis by cyanobacteria (Halliwell 2006). The
O molecule is a free radical, as it has two impaired electrons 2
that have the same spin quantum number. This spin restriction makes
O prefer to 2 accept its electrons one at a time, leading to the
generation of the so-called reactive oxygen species (ROS). The
chemical nature of these species dictates that they can create
damage in cells. This has contributed to the creation of the
"oxidative stress" concept; in this view, ROS are unavoidable toxic
products of O metabolism and 2 aerobic organisms have evolved
antioxidant defences to protect against this tox- ity (Halliwell
1981; Fridovich 1998). Indeed, even in present-day plants, which
are full of antioxidants, much of the protein synthetic activity of
chloroplasts is used to replace oxidatively damaged D1 and other
proteins (Halliwell 2006). Yet, the use of the "oxidative stress"
term implies that ROS exert their effects through indiscriminate
widespread inactivation of cellular functions. In this context, ROS
must not be able to react with lipids, proteins or nucleic acids in
order to avoid any damage to vital cellular components. However,
genetic evidence has suggested that, in planta, purely physicoche-
cal damage may be more limited than previously thought (Foyer and
Noctor 2005).
This new edited volume in the Springer Subcellular Biochemistry
Series presents a comprehensive, state-of-the-art overview of the
proteomics of peroxisomes derived from mammalian, Drosophila,
fungal, and plant origin, and contains contributions from leading
experts in the field. The development of sensitive proteomics and
mass spectrometry technologies, combined with bioinformatics
approaches now allow the identification of low-abundance and
transient peroxisomal proteins and permits to identify the complete
proteome of peroxisomes, with the consequent increase of our
knowledge of the metabolic and regulatory networks of these
important cellular organelles. The book lines-up with these
developments and is organized in four sections including: (i) mass
spectrometry-based organelle proteomics; (ii) prediction of
peroxisomal proteomes; (iii) analysis of peroxisome proteome
interaction networks; and (iv) peroxisomes in relation to other
subcellular compartments. The editor Luis A. del Rio is Professor
ad honorem of the Spanish National Research Council (CSIC) in the
Group of Antioxidants, Free Radicals and Nitric Oxide in
Biotechnology, Food and Agriculture, Department of Biochemistry and
Cell & Molecular Biology of Plants, at the Estacion
Experimental del Zaidin, Granada, Spain. Del Rio's research group
focuses on the metabolism of reactive oxygen species (ROS),
reactive nitrogen species (RNS) and antioxidants in plant
peroxisomes, and the ROS- and RNS-dependent role of peroxisomes in
plant cell signalling. The editor Michael Schrader is Professor of
Cell Biology & Cytopathology in the Department of Biosciences
at the University of Exeter, UK. Using mammalian peroxisomes as
model organelles, Prof. Schrader and his team aim to unravel the
molecular machinery and signalling pathways that mediate and
regulate the formation, dynamics and abundance of these medically
relevant cellular compartments.
This new edited volume in the Springer Subcellular Biochemistry
Series presents a comprehensive, state-of-the-art overview of the
proteomics of peroxisomes derived from mammalian, Drosophila,
fungal, and plant origin, and contains contributions from leading
experts in the field. The development of sensitive proteomics and
mass spectrometry technologies, combined with bioinformatics
approaches now allow the identification of low-abundance and
transient peroxisomal proteins and permits to identify the complete
proteome of peroxisomes, with the consequent increase of our
knowledge of the metabolic and regulatory networks of these
important cellular organelles. The book lines-up with these
developments and is organized in four sections including: (i) mass
spectrometry-based organelle proteomics; (ii) prediction of
peroxisomal proteomes; (iii) analysis of peroxisome proteome
interaction networks; and (iv) peroxisomes in relation to other
subcellular compartments. The editor Luis A. del Rio is Professor
ad honorem of the Spanish National Research Council (CSIC) in the
Group of Antioxidants, Free Radicals and Nitric Oxide in
Biotechnology, Food and Agriculture, Department of Biochemistry and
Cell & Molecular Biology of Plants, at the Estacion
Experimental del Zaidin, Granada, Spain. Del Rio's research group
focuses on the metabolism of reactive oxygen species (ROS),
reactive nitrogen species (RNS) and antioxidants in plant
peroxisomes, and the ROS- and RNS-dependent role of peroxisomes in
plant cell signalling. The editor Michael Schrader is Professor of
Cell Biology & Cytopathology in the Department of Biosciences
at the University of Exeter, UK. Using mammalian peroxisomes as
model organelles, Prof. Schrader and his team aim to unravel the
molecular machinery and signalling pathways that mediate and
regulate the formation, dynamics and abundance of these medically
relevant cellular compartments.
Peroxisomes are a class of ubiquitous and dynamic single
membrane-bounded cell organelles, devoid of DNA, with an
essentially oxidative type of metabolism. In recent years it has
become increasingly clear that peroxisomes are involved in a range
of important cellular functions in almost all eukaryotic cells. In
higher eukaryotes, including humans, peroxisomes catalyze ether
phospholipids biosynthesis, fatty acid alpha-oxidation, glyoxylate
detoxification, etc, and in humans peroxisomes are associated with
several important genetic diseases. In plants, peroxisomes carry
out the fatty acid beta-oxidation, photorespiration, metabolism of
ROS, RNS and RSS, photomorphogenesis, biosynthesis of
phytohormones, senescence, and defence against pathogens and
herbivores. In recent years it has been postulated a possible
contribution of peroxisomes to cellular signaling. In this volume
an updated view of the capacity and function of peroxisomes from
human, animal, fungal and plant origin as cell generators of
different signal molecules involved in distinct processes of high
physiological importance is presented.
Oxygen (O ) appeared in significant amounts in the Earth's
atmosphere over 2. 2 2 billion years ago, largely due to the
evolution of photosynthesis by cyanobacteria (Halliwell 2006). The
O molecule is a free radical, as it has two impaired electrons 2
that have the same spin quantum number. This spin restriction makes
O prefer to 2 accept its electrons one at a time, leading to the
generation of the so-called reactive oxygen species (ROS). The
chemical nature of these species dictates that they can create
damage in cells. This has contributed to the creation of the
"oxidative stress" concept; in this view, ROS are unavoidable toxic
products of O metabolism and 2 aerobic organisms have evolved
antioxidant defences to protect against this tox- ity (Halliwell
1981; Fridovich 1998). Indeed, even in present-day plants, which
are full of antioxidants, much of the protein synthetic activity of
chloroplasts is used to replace oxidatively damaged D1 and other
proteins (Halliwell 2006). Yet, the use of the "oxidative stress"
term implies that ROS exert their effects through indiscriminate
widespread inactivation of cellular functions. In this context, ROS
must not be able to react with lipids, proteins or nucleic acids in
order to avoid any damage to vital cellular components. However,
genetic evidence has suggested that, in planta, purely physicoche-
cal damage may be more limited than previously thought (Foyer and
Noctor 2005).
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