bluuebunny/crossref_metadata_2025_split huggingface dataset:
An experimentally validated panel of subfamily‐specific oligonucleotide primers (Vα1‐w29/Vβ1‐w24) for the study of human T cell receptor variable V gene segment usage by polymerase chain reaction
Authors: Genevée Catherine , Diu Anita , Nierat Janine , Caignard Anne , Dietrich Pierre‐Yves , Ferradini Laurent , Roman‐Roman Sergio , Triebel Frédéaric , Hercend Thierry 
Published: March 2007

AbstractWe report here the characterization of a series of T cell receptor (TcR) Vα or Vβ subfamily‐specific oligonucleotide primers. Criteria that have guided the design of each oligonucleotide include appropriate thermodynamic parameters as well as differential base‐pairing scores with related and unrelated target sequences. The specificity of the oligonucleotides for each Vα or Vβ subfamily was tested by polymerase chain reaction (PCR) on both a series of TcR encoding plasmid DNA and clonal T cell populations. Unexpected cross‐reactivities were observed with plasmid cDNA sequences corresponding to unrelated subfamily gene segments. This led to the synthesis of additional series of oligonucleotides to obtain a relevant panel. A series of Vα1‐w29/Vβ1‐w24 TcR subfamily‐specific oligonucleotides was eventually selected which generates little, if any, cross‐reactivity. The use of Cα or Cβ primers for the amplification of internal positive control templates (i.e. Cβ for the Vα series and Cα for the Vβ series) has been tested in PCR performed with cDNA derived from peripheral blood lymphocytes; it was shown not to alter the amplification of the V subfamily‐specific DNA fragments. This panel of oligonucleotides will be helpful in the study of TcR V gene segment usage and, thus, may lead to a better characterization of T cell responses in physiological and pathological situations.
Rapid activation‐independent shedding of leukocyte L‐selectin induced by cross‐linking of the surface antigen
Authors: Palecanda Aiyappa , Walcheck Bruce , Bishop D. Keith , Jutila Mark A. 
Published: March 2007

AbstractL‐selectin (also termed LAM‐1, Leu‐8, TQ‐1, gp90MEL‐14, peripheral lymph node homing receptor and LECAM‐1) is an adhesion protein thought to be important in leukocyte entry into lymphoid tissues and sites of inflammation. We, as well as others, have shown that leukocyte activation by chemotactic factors results in rapid shedding (release) of L‐selectin from the cell surface. Here we have used flow cytometry, enzyme‐linked immunosorbent assay, and SDS‐PAGE/Western blot analysis to determine whether cross‐linking of L‐selectin in the absence of activation causes shedding. We found that rapid loss of leukocyte L‐selectin expression (down‐regulation) could be induced by treating cells with a chemical cross‐linker [bis (sulfosuccinimidyl) suberate]. L‐selectin down‐regulation via cross‐linking could occur at 4°C and in the absence of detectable cell activation (increased expression of CD11b/18). The loss of L‐selectin expression was due to shedding of the molecule from the leukocyte cell surface. Cross‐linking of L‐selectin with specific monoclonal antibodies also caused loss of surface expression of L‐selectin at 37°C. Finally, shed L‐selectin was detected in the plasma of healthy adults whose peripheral blood leukocytes demonstrated no obvious signs of activation. Our results suggest that activation‐independent shedding of leukocyte L‐selectin may occur in vivo and a possible mechanism could involve cross‐linking of leukocyte L‐selectin. This provides a novel mechanism for rapid regulation of expression of a leukocyte‐endothelial cell adhesion receptor.
Origin of thymic and peritoneal Ly‐1 B cells
Authors: Than Soe , Inaba Muneo , Inaba Kayo , Fukuba Yoh , Adachi Yasushi , Ikehara Susamu 
Published: March 2007

AbstractMurine Ly‐1 B cells were first found in the peritoneal cavity (Per C). It has been thought that Ly‐1 B cells are responsible for the development of autoimmune diseases, since they spontaneously produce autoantibodies. However, we have found that such Ly‐1 B cells are present in the thymus of normal mice, and that they play a crucial role in negative selection in the Mls system. In addition, thymic Ly‐1 B cells and Per C Ly‐1 B cells have been found to differ in function, ontogeny and location. In this communication, we report on the different origins of these cells. C57BL/6 mice are lethally irradiated and reconstituted with fetal (day 14) liver cells or bone marrow cells from 4‐, 6‐ or 12‐week‐old mice. Fetal liver cells are shown to have the capacity to reconstitute both thymic and Per C Ly‐1 B cells, whereas bone marrow cells from 6‐ or 12‐week‐old mice have the capacity to reconstitute thymic Ly‐1 B cells, but not Per C Ly‐1 B cells, indicating that fetal hemopoietic stem cells (HSC) differ from HSC in the bone marrow of adult mice, and that thymic and Per C Ly‐1 B cells have different origins.
A common ancestor of the mammalian transcription factors TCF‐1 and TCF‐1α/LEF‐1 expressed in chicken T cells
Authors: Gastrop Jan , Hoevenagel Ronald , Young John R. , Clevers Hans C. 
Published: March 2007

AbstractSeveral mammalian T cell‐specific transcription factors have been cloned recently. Two of these, TCF‐1 and TCF‐1α/LEF‐1, display a moderate level of overall sequence similarity, and contain virtually identical versions of a novel type of DNA‐binding domain, the HMG box. To study evolutionary aspects of the TCF transcription factors in relation to lymphoid differentiation, we have isolated chicken TCF clones from a spleen cDNA library. Low‐stringency screening with human probes as well as a polymerase chain reaction‐aided strategy resulted in the cloning of a single chicken TCF (chTCF) gene. Sequence comparison revealed that chTCF contained a TCF‐1α‐like N terminus, and a TCF‐1‐like C terminus. Furthermore, TCF‐1 and TCF‐1α were more homologous to chTCF than to each other. We postulate that chTCF is the direct descendant of a single ancestral gene, which has been duplicated in mammals to yield TCF‐1 and TCF‐1α.
Functional characterization of non‐human primate erythrocyte immune adherence receptors: implications for the uptake of immune complexes by the cells of the mononuclear phagocytic system
Authors: Edberg Jeffrey C. , Kimberly Robert P. , Taylor Ronald P. 
Published: March 2007

AbstractErythrocytes from primates express an immune adherence (IA) receptor that binds complement‐opsonized immune complexes (IC) both in vivo and in vitro.We have analyzed the immunochemical and functional properties of theIA receptor from erythrocytes from species that have been used for in vivo IC clearance studies and have compared these properties to the human IA receptor (which is called complement receptor type 1, CR1). Erythrocytes from all species (chimpanzee, baboon, rhesus and cynomolgus monkey) bind antibody/double‐stranded DNA IC when opsonized with autologous complement. However, IC which are bound to chimpanzee erythrocytes are not released upon addition of chimpanzee serum (which contains factor I activity), while IC bound to baboon erythrocytes and human erythrocytes are released upon addition of autologous serum. Anti‐human CR1 monoclonal antibodies (mAb) E11 and HB8592 bind to erythrocytes from all species examined and the number of mAb epitopes per erythrocyte correlated with the number of IC that could bind to the erythrocyte under saturating conditions. However, a number of interesting differences between the species are observed withother mAb. The anti‐CR1 mAb 1B4 and 3D9, which block recognition of ligand by CR1, did not bind to chimpanzee erythrocytes and bound partially to rhesus and cynomolgusmonkey erythrocytes. In addition, the ability of autologous serum to induce release of erythrocyte‐bound IC correlates with the presence of these epitopes. These findings, taken in context with previous clearance studies, suggest that serum‐mediated release may not be required for the rapid transfer of the IC from the erythrocyte tothe mononuclear phagocytic system.
Murine epidermal Langerhans cells are potent stimulators of an antigen‐specific T cell response to Leishmania major, the cause of cutaneous leishmaniasis
Authors: Will Antje , Blank Christine , Röllinghoff Martin , Moll Heidrun 
Published: March 2007

AbstractCutaneous leishmaniasis is initiated by the bite of an infected sandfly and inoculation of Leishmania major parasites into the mammalian skin. Macrophages are knownto play a central role in the course of infection because they are the prime host cellsand function as antigen‐presenting cells (APC) for induction of the cell‐mediated immune response. However, in addition to macrophages in the dermis, the skin contains epidermal Langerhans cells (LC) which can present antigen (Ag) to T cells. Therefore, using a murine model of cutaneous leishmaniasis, we analyzed the ability of epidermal cells to induce a T cell response to L.major. The results demonstrated that freshly isolated LC, but not cultured LC, are highly active in presenting L.major Ag in vitro to T cells from primed mice and toa L.major‐specific T cell clone. Furthermore, freshly isolated LC had theability to retain L.major Ag in immunogenic form for at least 2 days. Their efficiency was much greater than that of irradiated spleen cells, a standard population of APC. LC stimulated both Tcell proliferation and production of the lymphokines interleukin (IL)‐2 and IL‐4. The response was Ag specific and could be induced by lysate of L.major parasites and by live organisms. The data suggest that epidermal LC are important APC in cutaneous leishmaniasis. They may perform a critical function by capturing L.major Ag in the skin and presenting it either to quiescent T cells circulating through the draining lymph node or locally to T effector cells infiltrating the cutaneous lesion.
Bee venom phospholipase A2‐specific T cell clones from human allergic and non‐allergic individuals: cytokine patterns change in response to the antigen concentration
Authors: Carballido José M. , Carballido‐Perrig Nicole , Terres GeróNimo , Heusser Christoph H. , Blaser Kurt 
Published: March 2007

AbstractProtein antigens with both allergenic and immunoprotective properties represent appropriate molecules to study IgE and IgG regulation. We have established a panel of T cell clones specific to bee venom phospholipase A2 (PLA) from human individuals allergic, hyposensitized or immune (protected) to bee sting. All clones obtained were CD3+, CD4+ and expressed α,β T cell receptor. Depending on the T cell clone, maximal stimulation required 1 to 100 μg/ml of PLA, and the addition of interleukin (IL)‐2 and/or IL‐4 increased their antigen‐dependent proliferation. Following antigen stimulation, the clones produced IL‐4, interferon‐γ (IFN‐γ) and granulocyte‐macrophage colony‐stimulating factor. Most clones also produced tumor necrosis factor α (TNF‐α) and tumor necrosis factor β (TNF‐β), and some produced IL‐5 and/or IL‐2. Both absolute and relative amounts of secreted cytokines depended on the antigen concentration. At low antigen doses, IL‐4 was producedbut little or not IFN‐γ, whereas at higher PLA concentrations significant amounts of both IL‐4 and IFN‐γ were obtained. Thus, these PLA‐specific Tcell clones could be classified according to the changes in the ratio of IL‐4/IFN‐γ production in response to increasing antigen concentrations. Clones derived from allergic and hyposensitized individuals required higher critical amounts of antigen for IFN‐γ induction, and expressed increasing IL‐4/IFN‐γ ratios with increasing concentrations of PLA. Modulation of cytokine patterns by thedose of the antigen may be a driving force for IgE or IgG formation resulting in allergy or immunoprotection.
Mycobacterial heat‐shock proteins as carrier molecules. II: The use of the 70‐kDa mycobacterial heat‐shock protein as carrier for conjugated vaccinescan circumvent the need for adjuvants and Bacillus Calmette Guérin priming)
Authors: Barrios Christy , Lussow Alexander R. , Embden Jan Van , Zee Ruurd Van Der , Rappuoli Rino , Costantino Paolo , Louis Jacques A. , Lambert Paul‐Henri , Giudice Giuseppe Del 
Published: March 2007

AbstractIn a recent work, we have shown that mycobacterial heat‐shock proteins (hsp)of 65‐kDa (GroEL‐type) and 70‐kDa (DnaK‐type) acted as carrier molecules in mice, previously primed with Mycobacterium tuberculosis var. bovis (bacillus Calmette‐Guérin, BCG), for the induction of high andlong‐lasting titers of IgG against the repetitive malaria synthetic peptide (NANP)40. Anti‐peptide antibodies were induced when the malaria peptide, conjugated to the mycobacterial hsp, was given in the absence of any adjuvants (Lussow etal., Eur. J. Immunol. 1991. 87: 2960). In this report, we show that mice immunized with peptides or oligosaccharides conjugated to the 70‐kDa hsp produced high titers of IgG antibodies in the absence of any previous priming with BCG.The anti‐peptide antibody response persisted for at least 1 year. This adjuvant‐free carrier effect of the 70‐kDa hsp was T cell dependent, since no anti‐peptide nor anti‐70‐kDa IgG antibodies were induced in athymic nu/nu mice. Previous immunization of mice with the 65‐kDa or 70‐kDa hsp did not have any negative effect on the induction of anti‐peptide IgG antibodies after immunization with hsp‐peptide conjugates in the absence of adjuvants. Furthermore, preimmunization with the 65‐kDa hsp could substitute for BCG in providingan effective priming for the induction of anti‐(NANP) antibodies. Finally, both the 65‐kDa and 70‐kDa hsp acted as carrier molecules for the induction ofIgG antibodies to group C meningococcal oligosaccharides, in the absence of adjuvants. These findings strongly suggest that the use of hsp as carriers in conjugated constructs for the induction of anti‐peptide and anti‐oligosaccharide antibodies could be of value in the design of new vaccines for eventual use in humans.
Interaction of C1q receptor with lung surfactant protein A
Authors: Malhotra Rajneesh , Haurum John , Thiel Steffen , Sim Robert B. 
Published: March 2007

AbstractEarlier we reported the purification of C1q receptor (C1qR) from U937 cells and human tonsil lymphocytes (Malhotra, R. and Sim, R. B., Biochem. J. 1989. 218: 625) and showed that C1qR interacts with the ligands C1q, mannose‐binding protein, conglutinin and lung surfactant protein A (SP‐A) (Malhotra, R., Thiel, S., Reid, K. B. M. and Sim, R. B., J. Exp. Med. 1990. 172: 955). C1qR was characterized as an acidic glycoprotein, which, when solubilized, exists as a dimer of Mr 115000 under non‐denaturing conditions. In this article we provide evidence for binding of radioiodinated SP‐A to U937 cells and show that binding of radioiodinated SP‐A to U937 cells is specific, saturable, salt dependent and is inhibited by purified C1qR and byC1q. The interaction of SP‐A withU937 cells was found to up‐regulate the surface expression of C1qR. Incubation of SP‐A with U937 cells at 37°C for 80 min was found to increase the receptornumber per cell. Increase in receptor number was inhibited in the presence of sodium azide and monensin. Incubation of cells with calcium ionophore A 23187 induced increased surface expression in the absence of SP‐A. The results indicate that interactionof SP‐A with U937 cells triggers the expression of an intracellular pool of C1qR.
Molecular cloning and expression of the murine RANTES cytokine: structural and functional conservation between mouse and man
Authors: Schall Thomas J. , Simpson Nancy J. , Mak John Y. 
Published: March 2007

AbstractThe infiltration and activation of monocytes is a hallmark of chronic inflammation, including that associated with a variety of disease states such as rheumatoid arthritis, atherosclerosis, and various autoimmune conditions. Recently, a family of small molecular mass proteins has been described which appear to have inflammatory properties, including chemoattractant effects on monocytes. We report here on the molecular cloning, characterization, and functional expression of muRANTES, a new murine member of this family. muRANTES expressed in a mammalian expression system is an approximately 8‐kDaprotein exhibiting immune cross‐reactivity with a rabbit polyclonal antiserumgenerated against human RANTES. Boyden chamber chemotaxis experiments reveal some lack of species specificity in monocyte chemoattractant potential, as recombinant muRANTES attracts human monocytes in a dose‐dependent fashion in vitro. muRANTES and its human homolog share approximately 85% amino acid identity, a higher level of conservation than that seen with any other species homologs in this cytokine family, and second only to transforming growth factor‐β among reported immune cytokines.
Suppression of lymphocyte proliferation by a retroviral p15E‐derived hexapeptide
Authors: Oostendorp Robert A. J. , Schaaper Wim M. M. , Post Jacob , Von Blomberg B. Mary E. , Meloen Rob H. , Scheper Rik J. 
Published: March 2007

AbstractCKS‐17 (LQNRRGLDLLFLKEGGL), a synthetic peptide derived from a conserved region of retroviral transmembrane proteins, has previously been shown to suppress severaldifferent immune effector mechanisms. The present study was undertaken to further delineate immunosuppressive site(s) of CKS‐17. Overlapping hexapeptides covering the complete sequence of CKS‐17 were synthesized. One CKS‐17‐derived hexapeptide, LDLLFL, suppressed ligand [CD3, interleukin (IL)‐2]‐induced lymphocyte proliferation. Spontaneous proliferation of transformed lymphoid cell lines, as well as cell lines from myeloid or epitheloid origin, was not inhibited byLDLLFL. Full suppression required the continuous presence of LDLLFL during culturing, and did not involve interference with monocyte function. Radiolabeling studies showed that the hexapeptide did not compete with IL‐2 for IL‐2 receptor binding. Most likely the LDLLFL motif inteferes with steps shared bythe IL‐2 and CD3 receptor‐induced signaling pathways. Since LDLLFL displays multiple immunosuppressive activities, it may constitute a biologically relevant immunosuppressive site of retroviral transmembrane proteins.
Tissue‐specific and allelic expression of the complement regulator CD46 is controlled by alternative splicing
Authors: Russell Sarah M. , Sparrow Rosemary L. , McKenzie Ian F. C. , Purcell Damian F. J. 
Published: March 2007

AbstractCD46 (membrane cofactor protein) is a human cell surface glycoprotein withcofactoractivity for factor I‐mediated cleavage of complement components C3b andC4b. The CD46 protein from normal lymphocytes resolves on sodium dodecyl sulfate‐polyacrylamide gel electrophoresis as two major bands of 66 and 56 kDa. CD46 cDNA encodes four extracellular short consensus repeat domains, a Ser/Thr/Pro (STP) ‐ rich region, a transmembrane region and a cytoplasmic tail. We now show that exquisite control ofmRNA splicing is responsible for the heterogeneous expression of CD46 isoforms. Differential splicing of 5 exons generates at least 14 CD46 mRNA variants whose expression is stringently regulated by allelic, tissue‐specific and malignancy‐related factors, as: (a) leukemic cells and Epstein‐Barr virus‐transformed B cells preferentially incorporate the first of three STP exons (exon 7) into mRNA, and produce a larger CD46 isoform of 74 kDa, (b) an allelic difference in the proportion of 66‐ and 56‐kDa CD46 isoforms on lymphocytes corresponds to the preferential inclusion or exclusion of the second STP exon (exon 8), (c) the third STP exon (exon 9) isspecifically deleted in some placentae, (d) spermatozoa delete both exons 12 and 13, encoding a shorter transmembrane region and a unique cytoplasmic tail and (e) all tissues tested differentially splice exon 13, resulting in two alternative cytoplasmic tails. The distribution of the 14 alternatively spliced RNA transcripts correlated with the presence of protein isoforms of the predicted size, indicating that alternative splicing leads to heterogeneity of CD46 glycoproteins.
T cell recognition of donor major histocompatibility complex class Ipeptides during allograft rejection
Authors: Fangmann Josef , Dalchau Rosemarie , Sawyer Greta J. , Priestley Carol A. , Fabre John W. 
Published: March 2007

AbstractLEW (RTI1) recipients of DA (RTIavl) skin and kidney allografts were tested for the capacity of their T lymphocytes to proliferate to three 22–24‐amino acid peptides from the hypervariable regions of the RTI‐Aavl classical MHC class I molecule. Ten days after rejecting second‐set DA kidneyallografts, spleen cells (but interestingly not lymph node cells) from LEW recipients showed strong, LEW antigen‐presenting cell‐dependent, CD4+ Tcell proliferation to peptide 1 (from the α helical region of the α1 domain). CD8+ T cells showed no response to peptide 1. There was no response by the spleen cells to peptide 2 (from the β sheet of the α2 domain) or peptide 3 (from the α helical region of the α2 domain). Immunization of LEW rats with pure RTI‐Aavl class I H chain in Freund's adjuvant gave responses identical to that seen after grafting, i.e. good CD4+ T cell proliferation to peptide 1, but none to peptides 2 and 3. However, immunization of LEW rats with peptides 1, 2 and 3 in Freund's adjuvant resulted in good CD4+ T cell proliferation responses to each of the peptides. These data demonstrate that indirect allorecognition can be stimulated by allograft rejection, and emphasize that the physiological processing of donor antigens will influence which peptides will be important in indirect allorecognition in transplantation.
Soluble anti‐μ monoclonal antibodies prime resting B cells to secrete immunoglobulins in response to interleukins‐4 and ‐5
Authors: Phillips Catherine , Klaus Gerry G. B. 
Published: March 2007

AbstractSoluble anti‐immunoglobulin (Ig) antibodies have been generally found to inhibit Ig secretion in B cells, via largely unknown mechanisms. To investigate this phenomenon further a two‐step culture system was used in which B cells are primed for24–72 h with various soluble monoclonal or polyclonal anti‐Ig antibodies: after washing the cells were placed in readout cultures with a combination of interleukin (IL)‐5 and IL‐4. Using this protocol B cells primedwith (mitogenic ornonmitogenic) anti‐μ monoclonal antibodies differentiated into large numbers of IgM‐secreting cells, comparable to responses to lipopolysaccharide. In contrast, priming with polyclonal rabbit anti‐Ig or monoclonal anti‐x antibodies, markedly inhibited Ig secretion induced by IL‐4 + IL‐5. In addition, anti‐μ was markedly inhibitory if left in thereadout cultures with the two lymphokines. These results, therefore, indicate that appropriate cross‐linking of surface IgM receptors on B cells can prime the cells tosecrete Ig when they are restimulated by T cell‐derived lymphokines in the absence of anti‐μ. Incontrast co‐ligation of both surface IgM and surface IgD receptors apparently results in powerful inhibition of Ig secretion, which is not reversed by stimulation withIL‐4 plus IL‐5.
Ongoing Vx−Jx recombination after formation of a productiveVx−Jx coding joint
Authors: Huber Christian , Klobeck Hans‐Gustav , Zachau Hans G. 
Published: March 2007

AbstractVx genes of man can recombine with the Jx gene segments eitherbyan inversion or by a deletion mechanism. Back‐to‐back fusion products of the respective recombination signal sequences (signal joints) are retained on the chromosome after the formation of a Vx−Jx coding joint by an inversion. Our knowledge of the structure of the human x locus and the application of the polymerase chain reaction allowed us now to establish a direct relationshipbetween different x recombination products in the lymphoid cell line JI. Two consecutive inversions fully explain the existence of two coding joints and two signal joints on the same chromosome of this cell line. Although the initially formed coding joint is productively rearranged and expressed, a second Vx−Jx rearrangement took place which leads to an aberrant joint. In this process a Jx gene segment of the signal joint that had been created in the first Vx−Jx joining was used as the recombination target. The sequence of the two rearrangements is unequivocal since a product of the first (productive) reaction is a partner in the second (aberrant) one.