Quasi-Exactly Solvable Spin 1/2 Schr\"odinger Operators

The algebraic structures underlying quasi-exact solvability for spin 1/2 Hamiltonians in one dimension are studied in detail. Necessary and sufficient conditions for a matrix second-order differential operator preserving a space of wave functions with polynomial components to be equivalent to a \sch\ operator are found. Systematic simplifications of these conditions are analyzed, and are then applied to the construction of several new examples of multi-parameter QES spin 1/2 Hamiltonians in one dimension.Comment: 32 pages, LaTeX2e using AMS-LaTeX packag

On form-preserving transformations for the time-dependent Schr\"odinger equation

In this paper we point out a close connection between the Darboux transformation and the group of point transformations which preserve the form of the time-dependent Schr\"odinger equation (TDSE). In our main result, we prove that any pair of time-dependent real potentials related by a Darboux transformation for the TDSE may be transformed by a suitable point transformation into a pair of time-independent potentials related by a usual Darboux transformation for the stationary Schr\"odinger equation. Thus, any (real) potential solvable via a time-dependent Darboux transformation can alternatively be solved by applying an appropriate form-preserving transformation of the TDSE to a time-independent potential. The preeminent role of the latter type of transformations in the solution of the TDSE is illustrated with a family of quasi-exactly solvable time-dependent anharmonic potentials.Comment: LaTeX2e (with amsmath, amssymb, amscd, cite packages), 11 page

A potential immune escape mechanism by melanoma cells through the activation of chemokine-induced T cell death

AbstractThe immune system attempts to prevent or limit tumor growth, yet efforts to induce responses to tumors yield minimal results, rendering tumors virtually invisible to the immune system [1]. Several mechanisms may account for this subversion, including the triggering of tolerance to tumor antigens [2, 3], TGF-α or IL-10 production, downregulation of MHC molecules, or upregulation of FasL expression [4, 5]. Melanoma cells may in some instances use FasL expression to protect themselves against tumor-infiltrating lymphocytes (TIL) [4, 5]. Here, we show another, chemokine-dependent mechanism by which melanoma tumor cells shield themselves from immune reactions. Melanoma-inducible CCL5 (RANTES) production by infiltrating CD8 cells activates an apoptotic pathway in TIL involving cytochrome c release into the cytosol and activation of caspase-9 and -3. This process, triggered by CCL5 binding to CCR5, is not mediated by TNFα, Fas, or caspase-8. The effect is not unique to CCL5, as other CCR5 ligands such as CCL3 (MIP-1α) and CCL4 (MIP-1β) also trigger TIL cell death, nor is it limited to melanoma cells, as it also operates in activated primary T lymphocytes. The model assigns a role to the CXC chemokine CXCL12 (SDF-1α) in this process, as this melanoma cell-produced chemokine upregulates CCL5 production by TIL, initiating TIL cell death

Cu2+ binding triggers αBoPrP assembly into insoluble laminar polymers

AbstractCu2+ binding is so far the best characterized property of the prion protein. This interaction has been mapped to the N-terminal domain of the prion protein where multiple His residues occur largely embedded within the repetitive PHGGGWGQ sequence known as octarepeats. When Cu2+ interaction is studied using a solution of full-length bovine prion protein containing six octarepeats at protein concentrations above 25 μM, a drastic increase in solution turbidity is observed due to the formation of insoluble cation–protein complexes that appear as bidimensional polymer meshes. These bidimensional meshes consist of a single layer of protein molecules crosslinked by Cu2+ cations. Polymer formation is a cooperative process that proceeds by nucleation of protein molecules with a Cu2+ site occupancy of above 2. These results support the hypothesis that the N-terminal domain of prion protein is a ligand binding module that promotes crosslinked assembly, and suggest the existence of inter-repeat Cu2+ sites

Expression analysis of the thyrotropin-releasing hormone receptor (TRHR) in the immune system using agonist anti-TRHR monoclonal antibodies

AbstractMonoclonal anti-rat thyrotropin-releasing hormone (TRH) receptor (TRHR)-specific antibodies (mAb) were generated by immunization with synthetic peptides of rat TRHR partial amino acid sequences; one (TRHR01) was directed against a sequence (84–98) in the extracellular portion of the rat TRHR reported to be constant among different species, including man, and the second (TRHR02) recognizes the C-terminal region sequence 399–412. In lysates from GH4C1 cells, a clonal rat pituitary cell line, both mAb recognize the TRHR in Western blot analysis, and TRHR02 immunoprecipitates the TRHR. Incubation of GH4C1 cells with the mAb causes a fluorescence shift in fluorescence-activated cell sorting analysis. The cells were stained specifically by both mAb using immunocytochemical techniques. Furthermore, TRHR01 is agonistic in its ability to trigger Ca2+ flux, and desensitizes the TRH receptor. We tested for TRHR in several rat organs and found expression in lymphoid tissues. TRHR01 recognizes the human TRHR, and analysis of human peripheral blood lymphocyte and tonsil-derived leukocyte populations showed receptor expression in non-activated and phytohemagglutinin-activated T and B cells

Quantum superintegrability and exact solvability in N dimensions

A family of maximally superintegrable systems containing the Coulomb atom as a special case is constructed in N-dimensional Euclidean space. Two different sets of N commuting second order operators are found, overlapping in the Hamiltonian alone. The system is separable in several coordinate systems and is shown to be exactly solvable. It is solved in terms of classical orthogonal polynomials. The Hamiltonian and N further operators are shown to lie in the enveloping algebra of a hidden affine Lie algebra

DNA polymerase λ, a novel DNA repair enzyme in human cells

DNA polymerase lambda (pol λ) is a novel family X DNA polymerase that has been suggested to play a role in meiotic recombination and DNA repair. The recent demonstration of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in pol λ supports a function of this enzyme in base excision repair. However, the biochemical properties of the polymerization activity of this enzyme are still largely unknown. We have cloned and purified human pol λ to homogeneity in a soluble and active form, and we present here a biochemical description of its polymerization features. In support of a role in DNA repair, pol λ inserts nucleotides in a DNA template-dependent manner and is processive in small gaps containing a 5′-phosphate group. These properties, together with its nucleotide insertion fidelity parameters and lack of proofreading activity, indicate that pol λ is a novel β-like DNA polymerase. However, the high affinity of pol λ for dNTPs (37-fold over pol β) is consistent with its possible involvement in DNA transactions occurring under low cellular levels of dNTPs. This suggests that, despite their similarities, pol β and pol λ have nonredundant in vivo functions.This work was supported by Ministerio de Ciencia y Tecnologı´a Grant BMC2000-1138, Comunidad Auto´noma de Madrid Grant 08.5/0063/2000 (to L. B.) and by an institutional grant from Fundacio´n Ramo´n Areces

Centrality evolution of the charged-particle pseudorapidity density over a broad pseudorapidity range in Pb-Pb collisions at root s(NN)=2.76TeV

Peer reviewe

Recombinant expression of Ole e 6, a Cys-enriched pollen allergen, in Pichia pastoris yeast: Detection of partial oxidation of methionine by NMR

Olive pollen is one of the main causes of allergy in Mediterranean countries. Ole e 6, an olive pollen allergen, is a small (5.8 kDa) and acidic protein (pI 4.2) and no homologous proteins have been isolated or characterized so far. Ole e 6 has been efficiently expressed in the methylotrophic yeast Pichia pastoris. The cDNA encoding Ole e 6 was inserted into the plasmid vector pPIC9 and overexpressed in GS115 yeast cells. The recombinant product was purified by size-exclusion chromatography followed by reverse-phase HPLC. N-terminal sequencing, amino acid composition analysis, CD, NMR, and IgG-binding experiments were employed to characterize the purified protein. NMR data revealed the oxidation of the methionine at position 28 in approximately 50% of the recombinant protein but, although this alters its electrophoretic behavior, it did not affect folding or IgG-binding properties of rOle e 6. The recombinant form of Ole e 6 expressed in P. pastoris can be employed for structural and biochemical studies.This work was supported by Grants SAF2002-02711 from the Dirección General de Investigación (MCYT, Spain) and 07B/0054/2002 from the Comunidad Autónoma de Madrid (CAM, Spain)