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At least 55 records · Page 3Linked to original sources
PubMed1999

Odorant receptors: a plethora of G-protein-coupled receptors.

Odorant receptors (ORs) comprise the largest family of G-protein-coupled receptors (GPCRs). They are located in the nasal epithelium, at the ciliated surface of olfactory sensory neurones, where the initial steps of the olfactory transduction cascade occur. ORs are encoded by a large and diverse multi-gene family, which has been characterized in cyclostomes, teleosts, amphibia, birds and mammals, as well as in Drosophila and Caenorhabditis elegans. Here, the range of diversity in OR and chemoreceptor structure is examined, noting that their functions are fundamentally similar to those of many neurotransmitter or neurohormone receptors. It is argued that ORs have emerged directly from other GPCRs independently in many species. According to this view, there is no structural prerequisite for OR identity and any GPCR has the potential to be or become an OR at a given point in evolution.

Animals↗
PubMed1999

Regulation of hematopoiesis in a sea of chemokine family members with a plethora of redundant activities.

The field of chemokine biology is a rapidly advancing one, with over 50 chemokines identified that mediate their effects through one or more of 16 different chemokine receptors. Chemokines, originally identified as chemotactic cytokines, manifest a number of functions, including modulation of blood cell production at the level of hematopoietic stem/progenitor cells and the directed movement of these early blood cells. This report reviews chemokines and chemokine/receptor activities mainly in the context of hematopoietic cell regulation and the numerous chemokines that manifest suppressive activity on proliferation of stem/progenitor cells. This is contrasted with the specificity of only a few chemokines for the chemotaxis of these early cells. The large number of chemokines with suppressive activity is hypothesized to reflect the different cell, tissue, and organ sites of production of these chemokines and the need to control stem/progenitor cell proliferation in different organ sites throughout the body.

Animals↗
PubMed1999

Endocytic vacuoles formed following a short pulse of K+ -stimulation contain a plethora of presynaptic membrane proteins.

It is now well established that the membrane of synaptic vesicles is recycled following exocytosis. However, little is known concerning the identity of the primary or secondary endocytic structures and their molecular composition. Using cultured rat cerebellar granule cells we combined uptake of horseradish peroxidase as a fluid phase marker and immunogold labeling for a variety of presynaptic proteins to assess the molecular identity of the stimulation-induced endocytic compartments. Short periods (5 or 30 s) of stimulation with 50 mM KCl were followed by periods of recovery for up to 30 min. Stimulation resulted in the formation of horseradish-peroxidase-filled vacuoles in the axonal varicosities as the apparent primary endocytic compartment. Horseradish peroxidase-filled synaptic vesicles were formed when stimulated cells were allowed to recover in horseradish peroxidase-free culture medium. Horseradish peroxidase-filled vacuoles as wells as vesicles contained the synaptic vesicle membrane proteins VAMP II, synaptotagmin, SV2, and synaptophysin, the vesicle-associated proteins rab 3A and synapsin I, and in addition SNAP-25. No incorporation of vesicle proteins into the plasma membrane was observed. Horseradish peroxidase-filled vesicles and vacuoles generated on incubation of unstimulated granule cells with horseradish peroxidase for prolonged periods of time were equally immunolabeled. Renewed stimulation of prestimulated granule cells with either 100 mM KCl or 30 microM Ca2+ ionophore A23187 resulted in a reduction of horseradish peroxidase-filled vacuoles suggesting that the vacuolar membrane compartment was exocytosis-competent. Our results suggest that varicosities of cultured cerebellar granule cells possess a fast stimulation-induced pathway for recycling the entire synaptic vesicle membrane compartment. The primary endocytic compartment represents not a synaptic vesicle but a somewhat larger vesicle protein-containing vacuolar entity from which smaller vesicles of identical protein composition may be regenerated. Endocytic vacuoles and synaptic vesicles share membrane and membrane-associated proteins and presumably also major functional properties.

Animals↗
PubMed1998

Isolation and characterization of an estrogen binding protein which may integrate the plethora of estrogenic actions in non-reproductive organs.

A putative estrogen receptor (pER) from mouse liver has been characterized. The heterodimer protein (81-84 kDa) consists of two covalently bound subunits (61-67 and 17-27 kDa) with following characteristics: sedimentation constant--4.9 S; IP--4.8; dissociation constant (Kd) for estradiol-17beta binding--0.7 nmol; binding sites--0.746 pmol/mg protein; relative binding affinity--estradiol-17beta--100, estrone--80 and estriol--30; specificity--does not bind, other natural steroids, synthetic estrogens, antiestrogens and bioflavonoids. Importantly, immunosuppressants, neuroleptic and carcinogens influence 3H-estradiol-17beta binding to pER. Interestingly, pER is a serine phosphatase and this may have relevancy to estrogen action in Alzheimer's disease. The polyclonal anti-pER antibody does not react with estrogen receptors (ER). ER antibody does not react with pER. Remarkably, anti-pER antibody reacts with calcineurin, a brain phosphatase and anti-calcineurin antibody reacts with pER. Immunohistochemical analyses showed that pER is undetectable in reproductive organs (except ovary). It is localized on the plasma or the nuclear membranes in some, in cytoplasm and/or nucleus in other cells of non-reproductive organs (skeletal, neural, vascular, hair and retina), and in tumors (mammary, endometrial and prostate cancers, and prostatic hyperplasia). The information presented justifies the proposition that pER may mediate the estrogenic actions in non-reproductive organs.

9,10-Dimethyl-1,2-benzanthracene↗
PubMed2001

An unexpected plethora of trehalose biosynthesis genes in Arabidopsis thaliana.

Trehalose accumulation has been documented in many organisms, such as bacteria and fungi, where it serves a storage and stress-protection role. Although conspicuously absent in most plants, trehalose biosynthesis genes were discovered recently in higher plants. We have uncovered a family of 11 TPS genes in Arabidopsis thaliana, one of which encodes a trehalose-6-phosphate (Tre6P) synthase, and a subfamily of which might encode the still elusive Tre6P phosphatases. A regulatory role in carbon metabolism is likely but might not be restricted to the TPS control of hexokinase activity as documented for yeast. Incompatibility between high trehalose levels and chaperone-assisted protein folding might be a reason why plants have evolved to accumulate some alternative stress-protection compounds to trehalose.

Arabidopsis↗
PubMed2001

A plethora of carbene interconversions on the C(5)H(4)S energy surface: a computational study.

The potential energy surface for the reaction of atomic carbon with thiophene has been studied computationally. Intermediates which are energetically viable include the 2- and 3-thienylcarbenes 8 and 11, thiacyclohexa-3,5-dien-2-ylidene, 10, and thiacyclohexa-2,3,5-triene, 6. In accord with experimental data, 6 and 8 are in equilibrium. The lowest-energy pathway for rearrangement of 6 to 8, which is endothermic by 14.5 kcal/mol, involves ring opening to Z-2-penten-4-ynthial which then recloses to carbene 8. A 1,4 addition of C across the diene system in thiophene generates an ylid which rearranges with little or no barrier to cyclopentadienethione, the global minimum on this potential energy surface.

Journal Article↗
PubMed2002

A density functional theory study clarifying the reactions of conjugated ketenes with formaldimine. A plethora of pericyclic and pseudopericyclic pathways.

The reactions of vinylketene (1a), imidoylketene (1b), and formylketene (1c) with formaldimine (2) were studied at the B3LYP/6-31G* level. For the cycloadditions of these conjugated ketenes with 2, several possible pathways to both [4 + 2] and [2 + 2] products were examined. The lowest energy [2 + 2] pathways are, in most cases, calculated to be stepwise, forming the products via rate-determining conrotatory electrocyclization of zwitterionic intermediates. However, concerted transition structures analogous to the ketene plus ethene [2 + 2] cycloaddition reaction were also located; the existence of multiple transition states offers a resolution to a long-standing controversy regarding the mechanism of ketene plus imine cycloadditions. Both stepwise and concerted [4 + 2] pathways were calculated for 2b and for 2c; both these pathways are pseudopericyclic. The inherently low barriers associated with pseudopericyclic transition states provide an explanation of the experimental preference for [4 + 2] cycloadditions of alpha-oxoketenes and predict [4 + 2] cycloadditions should also be favored for imidoylketenes. For a vinylketene constrained to a Z-geometry, the concerted [4 + 2] cycloaddition is also predicted to be the lowest energy pathway. An explanation is offered for the unusual thermal equilibration from a six-membered ring (3d) to a four-membered ring (4d) observed by Sato et al. Transition structures for facile pseudopericyclic 1,3- and 1,5-hydrogen shifts in the zwitterions were also calculated.

Journal Article↗
PubMed2004

A plethora of plant serine/arginine-rich proteins: redundancy or evolution of novel gene functions?

Precursor-mRNA (pre-mRNA) processing is an important step in gene expression and its regulation leads to the expansion of the gene product repertoire. SR (serine-arginine)-rich proteins are key players in intron recognition and spliceosome assembly and significantly contribute to the alternative splicing process. Due to several duplication events, at least 19 SR proteins are present in the Arabidopsis genome, which is almost twice as many as in humans. They fall into seven different subfamilies, three of them homologous with metazoan splicing factors, whereas the other four seem to be specific for plants. The current results show that most of the duplicated genes have different spatiotemporal expression patterns indicating functional diversification. Interestingly, most of the SR protein genes are alternatively spliced and in some cases this process was shown to be under developmental and/or environmental control. This might greatly influence gene expression of target genes as also exemplified by ectopic expression studies of particular SR proteins.

Alternative Splicing↗
PubMed2005

Coagulation factor V: a plethora of anticoagulant molecules.

PURPOSE OF REVIEW: Thrombin is necessary for survival and is produced after activation of prothrombin by prothrombinase at the site of a vascular injury. While the enzyme component of prothrombinase alone, factor Xa, bound to a membrane surface can activate prothrombin, incorporation of the cofactor molecule, factor Va, into prothrombinase results in a five orders of magnitude increase in the catalytic efficiency of factor Xa that provides the physiologic pathway for thrombin generation. While the kinetic constants and the identity of peptide bonds cleaved in prothrombin to generate alpha-thrombin have been long established, the peptidyl portions of the factor Va molecule responsible for its interactions with factor Xa, prothrombin, and the lipid surface are still the subject of intense investigation. In this review, we summarize the current state of knowledge with respect to the interactions of the factor Va molecule with the various components of prothrombinase. RECENT FINDINGS: Binding sites for factor Xa have been identified on both the heavy and light chains of factor Va. Two amino acid regions that interact with factor Xa have been delineated on the heavy chain of the cofactor. It has also been demonstrated that the carboxyl-terminal portion of the heavy chain of factor Va contains hirudin-like motifs and appears to be responsible for the interaction of factor Va with prothrombin. This region of the molecule is important for procofactor activation by thrombin as well as cofactor function. Finally, the membrane-binding site of factor Va is contributed by several elements of the light chain and involves both electrostatic and hydrophobic interactions. SUMMARY: The absence or dysfunction of factor Va leads to hemorrhagic diseases while prolonged existence of the active cofactor species is associated with thrombosis. Thus, modulation of the incorporation of factor Va into prothrombinase in vivo by using synthetic peptides that have the potential to impair factor Va binding to any of the components of prothrombinase, will allow for control of the rate of thrombin generation at the site of vascular damage. As a consequence, a systematic definition of the regions of factor Va governing its incorporation within prothrombinase will provide the scaffold for the synthesis of potent anticoagulant molecules that could modulate thrombin formation and suppress excessive clotting in thrombotic individuals.

Animals↗