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The Lipocalin Protein Family: Perspectives for Future Research

This chapter appears in the following book:

Lipocalins

Edited by: Bo Åkerström, Niels Borregaard, Darren R. Flower and Jean-Philippe Salier
ISBN: 1-58706-297-6
» Get more information about this book at landesbioscience.com «

Chapter authors:
Darren R. Flower and Arne Skerra


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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 period of solid and significant maturity. The modern era of lipocalin research is marked by the astonishing and burgeoning diversity of function currently becoming apparent among members of this remarkable family. The lipocalins are, perhaps, best known to those outside the field for two notable properties. First, the simplicity and aesthetic appeal of their highly symmetrical b-barrel fold. Secondly, and more significantly, is the seeming paradox of their low sequence conservation, which stands in marked contrast to their high structural propinquity.1 While it is now clear that neither property is unique to the lipocalins, nonetheless the family remains noteworthy for several reasons. Three kinds of intriguing molecular recognition events have long been seen to characterize the lipocalins: small molecule binding within the intra-calyx cavity, macromolecular complex formation, and receptor binding. Deep insights have been gained into these properties, and it is clear that we still understand structural and biophysical aspects of the lipocalins better than we grasp their physiological role and thus their place in biology. While it is true that lipocalinists have now catalogued many important physiological functions, much of biological significance remains to be discovered. However, gone are the days when the family could be dismissed as a small group of obscure transporters of hydrophobic molecules. Lipocalins are important proteins doing important things, not only in the delivery of essential metabolic compounds but also in cellular signalling or as part of the innate immune response, to name just a few examples. However, the link between their molecular recognition properties and their function is not always obvious. Biological function, itself, can remain cryptic. The underlying coherence of the apparently separate biochemical activities of individual lipocalins can appear obscure. Nonetheless, in the time since the first definitive review of the family was written,1 our view of the lipocalin family has changed dramatically. Important strides are being made and will continue to be made, and it is the future perspectives for lipocalin research that forms the focus of this chapter. Specifically, we will endeavour to throw light upon the way that certain recent developments will shape the future of lipocalin research.

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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

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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...

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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 ...

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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...

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Roland K. Strong

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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 ...


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