Chapter category: Cell Metabolism
Siderocalins
Lipocalins
Edited by: Bo Åkerström, Niels Borregaard, Darren R. Flower and Jean-Philippe SalierISBN: 1-58706-297-6
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Chapter authors:
Roland K. Strong
Siderocalin (Lipocalin 2), first identified as a neutrophil granule component, is also found in uterine secretions, in serum and synovium during bacterial infection and secreted from epithelial cells in response to inflammation or tumorigenesis. Siderocalin is a potent bacteriostatic agent in vitro and, when knocked-out in mice, confers a remarkable susceptibility to bacterial infection in the absence of any other phenotype. However, Siderocalin lacked any precise function until specific, high-affinity ligands were identified: bacterial ferric siderophores. Siderophores, small-molecule iron (III) chelators, are synthesized, secreted and reabsorbed by microorganisms in a competition to obtain iron, a scarce resource in the environment, and have been linked to virulence, though through previously undefined mechanisms. Siderocalin employs degenerate molecular recognition machinery to bind to two distinct families of siderophores: the catecholate siderophores of enteric bacteria and the mycobacterial carboxymycobactins. Siderocalin therefore functions as an anti-bacterial component of innate immune responses by sequestering iron away from invading pathogens; pathogens use siderophores that escape Siderocalin capture to help establish virulence. However, the limited pattern of Siderocalin siderophore specificity, the use of alternate or modified siderophores by bacteria and the possible existence of other siderophore-binding lipocalins (‘siderocalins’) clearly demonstrates that the battle for virulence is ongoing. Siderocalin may also have pleiotropic activities, having been implicated in diverse cellular processes such as apoptosis and differentiation.
Additional chapters from this book:
Lipocalin Genes and Their Evolutionary History
Diego Sanchez, María D. Ganfornina, Gabriel Gutierrez, Anne-Christine Gauthier-Jauneau, Jean-Loup Risler and Jean-Philippe Salier
As extensively detailed elsewhere in this book, lipocalins exhibit three characteristic features, which include: (i) an unusually low amino acid sequence similarity (typically 15-25% between paralogs)...
Lipocalins 2005: An Introduction
Bo Åkerström, Niels Borregaard, Darren R Flower and Jean-Philippe Salier
The Lipocalin protein family is discussed, in its totality, in Chapters 2 and 3 and most lipocalins are reviewed individually, or in groups, elsewhere in this volume. In this chapter, written afte...
Lipocalins in Arthropoda: Diversification and Functional Explorations
María D. Ganfornina, Hartmut Kayser and Diego Sanchez
The number of sequenced arthropodan lipocalins adds up to over eighty (see Table1). From our currently fragmented knowledge of arthropodan genomes, the last common ancestor of this phylum is propos...
Bacterial Lipocalins: Origin, Structure, and Function
Russell E. Bishop,* Christian Cambillau, Gilbert G. Privé, Derek Hsi, Desiree Tillo and Elisabeth R. M. Tillier
The bacterial lipocalins were discovered in 1995 and first reviewed in the year 2000. In the subsequent 5 years, two important developments have been made. First, an explosion of molecular sequence ...
The Plasma Lipocalins a1-Acid Glycoprotein, Apolipoprotein D, Apolipoprotein M and Complement Protein C8g
Willem Van Dijk, Sonia Do Carmo, Eric Rassart, Björn Dahlbäck and James M. Sodetz
Avariety of molecules have been identified in blood plasma that exhibit lipocalin-like properties, but they do not seem to be functionally related. This review is restricted to four of these lipoc...
Plant Lipocalins
Jean-Benoit F. Charron and Fathey Sarhan
Lipocalins are widely distributed in animals, insect and bacteria but very little is known about plant lipocalins. The first lipocalin-like proteins reported in plants were the two key enzymes of ...
The Lipocalin Protein Family: Protein Sequence, Structure and Relationship to the Calycin Superfamily
Lola Ganfornina, Diego Sanchez, Lesley H Greene and Darren R. Flower
Lipocalins are remarkable in their diversity, as manifest at the levels of protein sequence and protein function. At the level of 3-dimensional structure, however, they are very similar. The lipocal...
Lipocalin-Type Prostaglandin D Synthase as an Enzymic Lipocalin
Yoshihiro Urade, Naomi Eguchi and Osamu Hayaishi
Lipocalin-type prostaglandin (PG) D synthase (L-PGDS) is the first member of the lipocalin family to be recognized as an enzyme. L-PGDS catalyzes the isomerization of PGH2, a common precursor of v...
Glycodelin: A Lipocalin with Diverse Glycoform-Dependent Actions
Markku Seppala,* Hannu Koistinen, Riitta Koistinen, Philip CN Chiu, and William SB Yeung
Glycodelin has many names in the literature, such as placental protein 14 (PP14), human placental organ-specific a2-globulin, or progesterone-dependent endometrial protein, based on electrophoretic ...
Functional Aspects of b-Lactoglobulin, Major Urinary Protein and Odorant-Binding Protein
Andrea Cavaggioni, Paolo Pelosi, Stephen G. Edwards and Lindsay Sawyer
The lipocalin family contains more than 30 distinct proteins that are widely distributed throughout the living world. However, the exact physiological functions of many members of the family are unkno...
The Lipocalin Protein Family: Perspectives for Future Research
Darren R. Flower and Arne Skerra
Lipocalinology, as a discipline, has been with us for more or less twenty years. After an initial period of exciting, if capricious, growth, study of the lipocalin protein family has now entered a p...
Siderocalins
Roland K. Strong
Siderocalin (Lipocalin 2), first identified as a neutrophil granule component, is also found in uterine secretions, in serum and synovium during bacterial infection and secreted from epithelial cells ...
Lipocalins in Clinical Medicine
Lennart Lögdberg and Bo Åkerström
This review highlights several possible future roles of lipocalins in human clinical medicine. Generically, due to their metabolism as low molecular weight plasma proteins, lipocalins are candidate ma...
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 compar...
Lipocalin Receptors: Into the Spotlight
B.J. Burke, C. Redondo, B. Redl and J.B.C. Findlay
Evidence has been steadily accruing over time that a significant number of lipocalins interact with specific membrane receptors. The transfer of RBP:retinol across the cell membrane, faciliated by the...
Important Mammalian Respiratory Allergens Are Lipocalins
Tuomas Virtanen* and Rauno Mantyjarvi
Allergy is an expanding problem in the industrialized countries. Allergenic proteins, the allergens, causing the allergic symptoms are ubiquitous materials in the environment, normally not harmful f...
Retinol Binding Protein and Its Interaction with Transthyretin
Marcia E. Newcomer* and David E. Ong
Transport of vitamin A to the target cells is mediated by the lipocalin retinol-binding protein. In plasma, RBP is found in a complex with its carrier protein Transthyretin (TTR). The structures of ...
