Cell Metabolism
Chapters
page 1 of 14 pages | next »5-Aminolaevulinic Acid Dehydratase, Porphobilinogen Deaminase and Uroporphyrinogen III Synthase
Heidi L. Schubert, Peter T. Erskine and Jonathan B. Cooper
The three enzymes 5-aminolaevulinic acid dehydratase (ALAD, E.C.4.2.1.24; sometimes referred to as porphobilinogen synthase), porphobilinogen deaminase (EC 4.3.1.8; also known as hydroxymethylbilane synthase) and uroporphyrinogen III synthase (U3S; E.C.4.2.1.75) together convert 5-aminolaevulinic ac...
A Chaperone System for Glycoprotein Folding: The Calnexin/Calreticulin Cycle
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Lars Ellgaard and Ari Helenius
The endoplasmic reticulum (ER) contains a particularly wide range of molecular chaperones and other proteins that assist the folding and quality control of newly synthesized protein. Some, like BiP/GRP78 and GRP94, belong to classical chaperone families. Others, like protein disulfide isomeras...
A Common Binding Site for Actin-Binding Proteins on the Actin Surface
Roberto Dominguez
The dynamic remodeling of the actin cytoskeleton plays an essential role in many cellular processes, including cell motility, cytokinesis, and intracellular transport. A large number of actin-binding proteins (ABPs) participate in this process, regulating the assembly of actin filaments into...
A Common Trimer of Annexin V as a Basic Unit in 2D and 3D Crystal Forms
Alain Brisson and Anita Lewit–Bentley
Annexins constitute a family of proteins which share the property of binding to lipid membranes in a calcium–dependent manner.1–5 The binding of annexins to phospholipid surfaces has been the subject of many studies which have provided evidence for a Ca2+&...
A Mutational Approach to Elucidate Annexin V Function
Begoña Campos, Jorge M. Naciff and John R. Dedman
Annexins mediate the intracellular calcium (Ca2+) signal by binding phospholipids in a Ca2+–dependent manner. Members of this protein family have been found in different phyla, ranging from single cell organisms to mammalian cells. Annexins compose up to 2% of ...
A Role for Calreticulin in the Clearance of Apoptotic Cells and in the Innate Immune System
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Peter M. Henson
Calreticulin has been shown to bind the collagenous tails of members of the collectin family of pattern recognition molecules. Its presence on cell surfaces then, implies a potential role for recognition of the collectins, and anything they may have bound via their globular head groups. In add...
Accelerated Protein Evolution Using Ribosome Display
Julie Douthwaite, Lutz Jermutus and Ronald Jackson
Ribosome display is a powerful selection technology for the identification of proteins with desired functions and has wide applicability across biologics drug discovery and basic research. Ribosome display is based on polymerase chain reaction and cell-free translation technologies that combine to p...
Acidic pH-Induced Ion Channels Formed by Annexin A6: Transformation of the Molecule from Soluble to Membrane Integral Protein
Slawomir Pikula
It has been recently described that annexin A6 (ANXA6), a member of the annexin family of human and verterbrate homologous Ca2+- and lipid-binding proteins, interacts with membranes in a Ca2+-independent manner and behaves as a true membrane protein. However, the...
Acrosomal Exocytosis
Claudia Nora Tomes
Sexual reproduction to perpetuate a given species occurs through fertilization, during which a diploid zygote is formed to produce a genetically distinct individual. To this end, the haploid sperm and haploid egg must collide to allow entry of the sperm head delivering the male chromatin into ...
Active Sites and Assembly of the 20S Proteasome
Wolfgang Heinemeyer
During the past decade, rapid progress was made in elucidating the 20S proteasomes structure, as well as in establishing its unusual proteolytic mechanism. This was enormously facilitated by the discovery of ancestral proteasome particles in certain bacterial species which led to the fir...
Adaptation of the Secretory Machinery to Pathophysiological Conditions
Abderrahmani Amar
Regulated exocytosis is a fundamental and common feature of all secretory cells specialized in the release of essential bioactive substances. This process is tightly controlled to adapt the amount of released products in response to the variable physiological cues. However it occurs that ina...
Adaptor Proteins in Lysosomal Biogenesis
P. Schu
Lysosomal membrane proteins and soluble lysosomal proteins are transported from the trans-Golgi network (TGN) to endosomes and lysosomes via coated-vesicles, which bud from the donor compartment and are transported to and fuse with the proper acceptor compartment. The proteins forming the vesicle...
Adipose Tissue Pathology in Human Obesity
Hans Hauner, Thomas Skurk
Human obesity is characterized by an excess of adipose tissue mass that has potential adverse health consequences and may finally result in a reduced quality of life and life expectancy.1 In normal-weight subjects the adipose tissue organ constitutes between 10 and 20% of t...
Advances in Insect-Based Cell-Free Protein Expression
Uritza von Groll, Stefan Kubick, Helmut Merk, Wolfgang Stiege and Frank Schäfer
Cell-free protein expression systems are becoming more widely used as they allow fast synthesis of recombinant proteins and an easy manipulation of reaction conditions. Here, we report on recent advances of a eukaryotic system based on extracts derived from Spodoptera frugiperda insect cells. We dem...
Advantages and Applications of the Batch-Formatted E. coli Cell-Free Expression System
Julia E. Fletcher, Federico Katzen, Shiranthi Keppetipola, Ashley Getbehead and Wieslaw Kudlicki
From the first procedure standardized in the early 1960s to its most recent modifications, cell-free expression using Escherichia coli lysates has evolved into a robust method for protein expression capable of producing protein in milligram quantities. Free from the constraints of a cell, the compon...
alpha(1)-Microglobulin
Bo Åkerström and Lennart Lögdberg
alpha(1)-Microglobulin is one of the three original members of the lipocalin superfamily. It has been found in mammals, birds, amphibians and fish and is distributed in plasma and extravascular compartments of all organs. a1-Microglobulin has a free cysteine side-chain located in a flexible loop, gi...
An Historical Introduction to Porphyrin and Chlorophyll Synthesis
Michael R. Moore
Porphyrins are the extroverts of chemistry. Bright purple and fluorescent, they are used biologically in the processes of energy capture and utilization. Porphyrins are the key to life. It has been suggested that abiotic formation of porphyrins, in particular uroporphyrinogen would have provid...
Annexin 1 Crystal Structure: Interaction of Annexins with Membranes
Anja Rosengarth and Hartmut Luecke
Annexins are structurally divided into a highly conserved core domain and a variable N-terminal domain. The core domain mediates the calcium-dependent phospholipid binding of annexins, whereas the N-terminal domain, which is unique in sequence and length for each member of this protein family,...
Annexin Binding to Lipid Assemblies
Paul Meers
Proteins that transiently and peripherally associate with biological mem–branes are emerging as a large and important group responsible for some of the basic functions of cells. It has become clear that cell membranes can act as sites for catalysis of important protein–protein ...
Annexin Functions in Phagocytic Leukocytes
Joel D. Ernst
By a variety of approaches, annexins have been discovered as abundant proteins in phagocytic leukocytes. No essential role for any of the annexins has been firmly established, but recent studies provide evidence for annexin involvement in membrane traffic during phagocytosis and in exocy...
Annexin Gene Knock-Out Models
Alejandra Tomas, Matthew J. Hayes, Debipriya Das, Barry P. Young and Stephen E. Moss
Progress in understanding the functions of annexins has accelerated recently through the generation of cell lines and mice containing targeted disruptions of annexin genes. Annexin null mutant mice exhibit distinct phenotypes ranging from mild to embryonic lethal, and analysis of cells i...
Annexin Gene Structure
Nicholas J. Nevid and Nelson D. Horseman
The annexins comprise a relatively large family of calcium- and phos-pholipid-binding proteins. There are at least 10 distinct annexins in vertebrates (annexins I-VIII, XI and XIII), and additional members of this family have been identified in drosophila (annexins IX and X) and hydra (a...
Annexin II: Analysis of a Pleiotropic Protein
Nolan R. Filipenko and David M. Waisman
The annexins are classically characterized as a family of proteins capable of binding to acidic phospholipids in a Ca2+-dependent manner. The interaction of these proteins with the plasma membrane suggests that they may be involved in membrane trafficking events, such as exocytosis, endocytosi...
Annexin V and Cell Surface–Expressed Phosphatidylserine: A Revealing Pas de Deux
Chris P.M. Reutelingsperger and Waander L. van Heerde
Annexin V acquired the green card for its membership of the annexin family in 1987 when its primary structure was reported for the first time.1 Before 1987 annexin V was investigated by various research groups as an isolated tissue protein. The large list of synonyms for annex...
Annexin V Molecular Structure, Ligand Binding and Biological Function
Barbara A. Seaton
This chapter introduces the molecular features that give rise to com–mon annexin properties. The first section describes the three dimensional structure of annexin V, the "prototypical" annexin. The second section addresses the basis of annexin/ligand binding as derived from complex...
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