Crystal structure of human Charcot–Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins

Leonidas, D.D.; Elbert, Boris L; Zhou, Zheng; Leffler, Hakon; Ackerman, Steven J.; Acharya, K. Ravi

doi:10.1016/s0969-2126(01)00275-1

Cited by 147 publications

(124 citation statements)

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“…Although it is tempting to consider the possibility of a similar physiologic function for the Rana ribonucleases, this interpretation would be decidedly premature, and it is difficult to envision this sort of role for the proteins that are localized in the oocyte. However, it is worthwhile to note that several of the Rana ribonucleases were initially isolated as carbohydrate-binding proteins (Titani et al 1987;Kamiya et al 1990); we can consider the possibility that these "bifunctional" ribonuclease-lectins function in some way similarly to the combined efforts of the eosinophil-associated ribonucleases and the eosinophil-specific galectin, the CharcotLeyden crystal protein (Leonidas et al 1995;Dyer and Rosenberg 1996).…”

Section: Discussionmentioning

confidence: 99%

Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

et al. 2001

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Abstract. We present sequences of five novel RNase A superfamily ribonuclease genes of the bullfrog, Rana catesbeiana. All five genes encode ribonucleases that are similar to Onconase, a cytotoxic ribonuclease isolated from oocytes of R. pipiens. With amino acid sequence data from 14 ribonucleases from three Rana species (R. catesbeiana, R. japonica, and R. pipiens), we have constructed bootstrap-supported phylogenetic trees that reorganize these ribonucleases into five distinct lineagesthe pancreatic ribonucleases (RNases 1), the eosinophilassociated ribonucleases (RNases 2, 3, and 6), the ribonucleases 4, the angiogenins (RNases 5) and the Rana ribonucleases-with the Rana ribonucleases no more closely related to the angiogenins than they are to any of the other ribonuclease lineages shown. Further phylogenetic analysis suggests the division of the Rana ribonucleases into two subclusters (A and B), with positive (Darwinian) selection (d N /d S > 1.0) and an elevated rate of radical nonsynonymous substitution (d R ) contributing to the rapid diversification of ribonucleases within each cluster. This pattern of evolution-rapid diversification via positive selection among sequences of a multigene cluster-bears striking resemblance to what we have described for the eosinophil-associated ribonuclease genes of the rodent Mus musculus, a finding that may have implications with respect the physiologic function of this unique family of proteins.

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Section: Discussionmentioning

confidence: 99%

Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

et al. 2001

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“…The loss of galactose-binding capacity in mammalian GRIFINs relates these proteins to galectin-10 (Charcot-Leyden crystal protein; 10% of the total protein in eosinophils (67)) and the galectin-related protein (GRP) (22,(68)(69)(70). Of note, human galectin-10 (no orthologue present in rodents to enable to study the role of this eosinophil protein on T cell suppression in animal models (71,72); its ovine orthologue is called galectin-14 (73)) has four deviations in the signature sequence, binds mannose instead of galactose (74) and also associates with a protein, i.e., pancreatic lysophospholipase (75) (for information on GRP, please see accompanying review (35)).…”

Section: E Conclusionmentioning

confidence: 99%

Members of the Galectin Network with Deviations from the Canonical Sequence Signature. 1. Galectin-Related Inter-Fiber Protein (GRIFIN)

Caballero¹,

Manning²,

Ludwig³

et al. 2018

TIGG

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Systematic databank-based sequence comparisons with the cDNA sequence for a lens-specific rat protein localized between lens fiber cells disclosed its similarity to galectins. In mammals, two sequence changes occur within the seven positions of amino acids commonly engaged in contacts to the β-galactoside core of glycans. Taking the compilation of GRIFIN genes to the level of diverse vertebrates revealed an exceptional variability: mammals shared alteration at two sites, birds and reptiles at only one site and amphibians and fish presented complete reconstitution. The homodimeric (proto-type) GRIFINs of chicken and zebrafish thus are active lectins. Crystallographical information for chicken GRIFIN illustrates the contact profile to lactose without one otherwise conserved site due to the Arg-to-Val substitution. That GRIFIN is enormously stable in vertebrate lenses, can act like a glue (or a bridge) due to its structure and interacts with α-crystallin (shown for murine GRIFIN) suggests a role in well-ordered packing of lens proteins. Referring to a likely analogy in plants, oligomeric leguminous lectins, β-sandwich proteins as galectins, are also assumed to participate in depositing and spatially organizing cell contents, here storage proteins in protein bodies and their contact to the membrane in carbohydrate-dependent and -independent manners, a likely case of structural and functional convergence. A. IntroductionThe realization of the unsurpassed capacity of glycans to store

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“…The analysis of the published crystal structures of mammalian galectins has even extended the structural similarity to legume lectins beyond this single aspect of the binding site. Mammalian galectin-1 and galectin-2, as well as the CharcotLeyden crystal protein, share a P-sandwich motif with legume lectins without engaging any cations in sugar binding (Lobsanov et al, 1993;Bourne et al, 1994;Liao et al, 1994;Leonidas et al, 1995;Rini, 1995). Dimerization of these galectins causes no distortion of the P-sheet topology termed jelly-roll motif, as it extends continuously across the dimer surface, keeping the sugar-binding sites at the far ends of the dimer (Fig.…”

Section: Galectinsmentioning

confidence: 99%

Animal Lectins

Gabius

1997

European Journal of Biochemistry

435

342

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Protein and lipid glycosylation is no longer considered as a topic whose appeal is restricted to a limited number of analytical experts perseveringly pursuing the comprehensive cataloguing of structural variants. It is in fact arousing curiosity in various areas of basic and applied bioscience. Well founded by the conspicuous coding potential of the sugar part of cellular glycoconjugates which surpasses the storage capacity of oligonucleotide-or oligopeptide-based code systems, recognition of distinct oligosaccharide ligands by endogenous receptors, i.e. lectins and sugar-binding enzymes or antibodies, is increasingly being discovered to play salient roles in animal physiology. Having inevitably started with a descriptive stage, research on animal lectins has now undubitably reached maturity. Besides listing the current categories for lectin classification and providing presentations of the individual families and their presently delineated physiological significance, this review places special emphasis on tracing common structural and functional themes which appear to reverberate in nominally separated lectin and animal categories as well as lines of research which may come to fruition for medical sciences.Keywords: lectin ; glycoprotein; glycolipid; cell adhesion ; molecular recognition ; inflammation; infection ; fertilization ; signal transduction ; tumor biology.The putative multiplicity of functional implications for protein and lipid glycosylation has fueled vigorous and prolific research activities in the last decade. Although glycobiologists continue to be afflicted with the problem of precisely defining the physiological significance of the puzzling variability and complex pattern of carrier-attached saccharide chains, the notion of inherent ligand properties for recognitive protein-carbohydrate interactions is already well established

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Crystal structure of human Charcot–Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins

Cited by 147 publications

References 68 publications

Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

Members of the Galectin Network with Deviations from the Canonical Sequence Signature. 1. <i>G</i>alectin-<i>R</i>elated <i>I</i>nter-<i>F</i>iber Prote<i>in</i> (GRIFIN)

Animal Lectins

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