X

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • The American Association of Immunologists  (10)
Type of Medium
Publisher
  • The American Association of Immunologists  (10)
Person/Organisation
Language
Years
Subjects(RVK)
  • 1
    Online Resource
    Online Resource
    Interleukin 2 regulates the expression of IL 2 receptors on interleukin 3-dependent bone marrow-derived cell lines.
    The American Association of Immunologists ; 1987
    In:  The Journal of Immunology Vol. 138, No. 2 ( 1987-01-15), p. 478-483
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 138, No. 2 ( 1987-01-15), p. 478-483
    Abstract: Two IL 3-dependent bone marrow-derived cell lines, FD.C/1 and 32Dcl-23, have been converted to IL 2-dependent growth states. In the case of the FD.C/1 cell line, a small subpopulation of cells converted to IL 2 growth dependence, whereas for the 32Dcl-23 cell line, most cells readily converted to IL 2 growth dependence. IL 2 receptor expression was followed in FD.C/1 and 32Dcl-23 cells in both IL 3-and IL 2-dependent growth states, by analyzing transcription of IL 2 receptor-specific RNA and the subsequent expression of cell surface receptors. The exposure of IL 3-dependent cell lines to IL 2 resulted in rapid increases in the transcription of IL 2 receptor-specific RNA and receptor expression. The addition of IL 3 to IL 2-dependent cell lines did not alter the expression of the IL 2 receptor. When IL 2 was removed from the culture medium of these cells, the presence of IL 3 maintained a higher level of IL 2 receptor expression than was observed in the absence of lymphokines.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.138.2.478
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1987
    detail.hit.zdb_id: 1475085-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Online Resource
    Open Access Request
    Availability (electronic / print)
  • 2
    Online Resource
    Online Resource
    Natural resistance to intracellular infections: Nramp1 encodes a membrane phosphoglycoprotein absent in macrophages from susceptible (Nramp1 D169) mouse strains.
    The American Association of Immunologists ; 1996
    In:  The Journal of Immunology Vol. 157, No. 8 ( 1996-10-15), p. 3559-3568
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 157, No. 8 ( 1996-10-15), p. 3559-3568
    Abstract: The mouse Nramp1 gene (Bcg/Ity/Lsh) controls innate defense to infection with intracellular parasites such as Mycobacterium, Salmonella, and Leishmania. Sequence analysis of Nramp1 predicts a hydrophobic, membrane-associated protein expressed exclusively in monocyte/macrophage lineages. A single G169D substitution within the fourth predicted transmembrane domain of Nramp1 is associated with susceptibility to infection (Bcg) in inbred mouse strains. To initiate the biochemical characterization of the Nramp1 protein and to analyze the molecular basis of susceptibility associated with the Nramp1(D169) allele, oligopeptides derived from Nramp1 and two fusion proteins containing the first 54 and the last 35 residues of Nramp1 were used to raise specific anti-Nramp1 antisera. In addition, a c-Myc epitope (EQKLISEEDL) was introduced in-frame at the C terminus of Nramp1 to follow its expression in a yeast heterologous system. Western analysis of crude membrane fractions from yeast demonstrated that Nramp1 is indeed an integral membrane protein (resistant to urea extraction). In resident Bcg(r) (129sv, Nramp1(G169)) macrophages, one of the anti-Nramp1 antisera identified by immunoprecipitation a protein of 90,000 to 100,000 apparent m.w. that was absent in macrophages from knockout mice bearing a null mutation at Nramp1. The Nramp1 protein could be metabolically labeled with orthophosphate and was sensitive to glycosylase treatment, verifying that Nramp1 is an integral membrane phosphoglycoprotein. Parallel analysis of macrophage extracts from Bcg(s) mouse strains (C57BL6/J and BALB/c, Nramp1(D169)) failed to detect mature Nrampl protein in these cells, suggesting that the G169D mutation at Nramp1 prevents proper maturation or membrane integration of the protein, resulting in its rapid degradation.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.157.8.3559
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1996
    detail.hit.zdb_id: 1475085-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Online Resource
    Open Access Request
    Availability (electronic / print)
  • 3
    Online Resource
    Online Resource
    Genetic control of natural resistance to Mycobacterium bovis (BCG) in mice.
    The American Association of Immunologists ; 1981
    In:  The Journal of Immunology Vol. 127, No. 6 ( 1981-12-01), p. 2417-2421
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 127, No. 6 ( 1981-12-01), p. 2417-2421
    Abstract: Mice of 12 inbred strains infected i.v. with Mycobacterium bovis (BCG) exhibited 2 distinct patterns of response as determined by the degree of BCG burden in the spleens of animals at 3 wk after infection with 10(4) viable bacilli: susceptible (C57BL/6J and related sublines, BALB/c and DBA/1J) and resistant (A/J, C3H/HeCr, DBA/2J, CBA/J, C57Br, AKR). Mendelian analysis of this trait on segregating backcross and F2 populations derived from the mating of resistant and susceptible progenitors was compatible with the hypothesis that resistance to BCG is controlled by a single, dominant, autosomal gene, which is being given the designation Bcg. The product of the Bcg gene was found to influence the early phase of host response resulting in the genetic advantage of the resistant host being demonstrable as early as 24 hr after infection.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.127.6.2417
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1981
    detail.hit.zdb_id: 1475085-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Online Resource
    Open Access Request
    Availability (electronic / print)
  • 4
    Online Resource
    Online Resource
    Absence of Binding of MDP, a Synthetic Immunoadjuvant, to Anti-Peptidoglycan Antibodies
    The American Association of Immunologists ; 1978
    In:  The Journal of Immunology Vol. 121, No. 4 ( 1978-10-01), p. 1219-1222
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 121, No. 4 ( 1978-10-01), p. 1219-1222
    Abstract: The binding of the synthetic immunoadjuvant N-acetyl-muramyl-l-alanyl-d-isoglutamine (MDP, for muramyl dipeptide) to human and rabbit sera containing peptidoglycan (PG) antibodies was investigated. Studies were performed by employing the corresponding 14C or 125I-labeled compounds in Farr-type binding and inhibition assays. Whereas MDP did not react with naturally occurring or experimentally induced PG-antibodies, the analog of MDP MDP-l-Lys-d-Ala did bind to hyperimmune rabbit anti-PG sera, but not to the human sera tested. These studies indicate that the radioimmunoassays employed basically are applicable for the selection of nonimmunogenic MDP analogs possessing immunoadjuvant activity.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.121.4.1219
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1978
    detail.hit.zdb_id: 1475085-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Online Resource
    Open Access Request
    Availability (electronic / print)
  • 5
    Online Resource
    Online Resource
    Immunopathology of BCG infection in genetically resistant and susceptible mouse strains.
    The American Association of Immunologists ; 1982
    In:  The Journal of Immunology Vol. 129, No. 5 ( 1982-11-01), p. 2179-2185
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 129, No. 5 ( 1982-11-01), p. 2179-2185
    Abstract: Natural resistance to Mycobacterium bovis (BCG) is under the control of a single gene, designated Bcg. Resistant (Bcgr) mice prevent multiplication of an i.v. injected inoculum of congruent to 10(4) dispersed BCG cells, whereas progressive multiplication of this pathogen occurs in the first 3 wk of infection in spleens and livers of susceptible (Bcgs) mice. Striking differences in the development of cellular immunity, as measured by granuloma formation in the liver and spleen, delayed-typed hypersensitivity, and a resistance to the challenge with homologous (BCG) and heterologous (Listeria monocytogenes) pathogens, were detected between Bcgr (C3H/HeN and A/J) and Bcgs (C57BL/6J and B10.A) strains. Cellular immune reactions progressively developed in the Bcgs mice, as a response to the increasing bacterial load, whereas greatly inferior levels of acquired immunity were observed in Bcgr strains. These findings support the concept that mice genetically resistant to BCG infection are able to prevent bacterial multiplication without the need for a cellular immune response, whereas genetically susceptible mice will eventually control bacterial multiplication with the acquisition of cellular immunity.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.129.5.2179
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1982
    detail.hit.zdb_id: 1475085-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Online Resource
    Open Access Request
    Availability (electronic / print)
  • 6
    Online Resource
    Online Resource
    Phenotypic expression of genetically-controlled natural resistance to Mycobacterium bovis (BCG).
    The American Association of Immunologists ; 1984
    In:  The Journal of Immunology Vol. 132, No. 2 ( 1984-02-01), p. 888-892
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 132, No. 2 ( 1984-02-01), p. 888-892
    Abstract: Mycobacterium bovis (BCG), when maintained in vitro, readily incorporates [3H]uracil, the RNA precursor. The rate of [3H] uracil incorporation into bacilli is sharply reduced when the BCG is phagocytized by murine adherent resident peritoneal macrophages and subsequently released by the lysis of monolayers. Macrophages derived from mouse strains that are innately resistant to BCG infection in vivo (Bcgr) are able to inhibit the [3H]uracil incorporation into the bacilli in a significantly more effective way than macrophages from BCG-susceptible (Bcgs) strains. This difference is best demonstrated with a low rate of infection (BCG: macrophage ratio between 1:1 and 2:1), and is most pronounced at 4 to 5 days after in vitro infection of macrophage monolayers. In vivo interaction of BCG with peritoneal macrophages in situ results in the same pattern of enhanced inhibition of [3H] uracil incorporation by Bcgr macrophages. The use of Bcg-congenic mouse strains has confirmed that the Chromosome 1 Bcg (Ity, Lsh) locus is regulating the antimycobacterial activity of macrophages. We conclude that the resident macrophage is the cell population that expresses the phenotype of genetically determined resistance to BCG infection.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.132.2.888
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1984
    detail.hit.zdb_id: 1475085-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Online Resource
    Open Access Request
    Availability (electronic / print)
  • 7
    Online Resource
    Online Resource
    Multifaceted Activities of Seven Nanobodies against Complement C4b
    The American Association of Immunologists ; 2022
    In:  The Journal of Immunology Vol. 208, No. 9 ( 2022-05-01), p. 2207-2219
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 208, No. 9 ( 2022-05-01), p. 2207-2219
    Abstract: Cleavage of the mammalian plasma protein C4 into C4b initiates opsonization, lysis, and clearance of microbes and damaged host cells by the classical and lectin pathways of the complement system. Dysregulated activation of C4 and other initial components of the classical pathway may cause or aggravate pathologies, such as systemic lupus erythematosus, Alzheimer disease, and schizophrenia. Modulating the activity of C4b by small-molecule or protein-based inhibitors may represent a promising therapeutic approach for preventing excessive inflammation and damage to host cells and tissue. Here, we present seven nanobodies, derived from llama (Lama glama) immunization, that bind to human C4b (Homo sapiens) with high affinities ranging from 3.2 nM to 14 pM. The activity of the nanobodies varies from no to complete inhibition of the classical pathway. The inhibiting nanobodies affect different steps in complement activation, in line with blocking sites for proconvertase formation, C3 substrate binding to the convertase, and regulator-mediated inactivation of C4b. For four nanobodies, we determined single-particle cryo-electron microscopy structures in complex with C4b at 3.4–4 Å resolution. The structures rationalize the observed functional effects of the nanobodies and define their mode of action during complement activation. Thus, we characterized seven anti-C4b nanobodies with diverse effects on the classical pathway of complement activation that may be explored for imaging, diagnostic, or therapeutic applications.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.2100647
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 2022
    detail.hit.zdb_id: 1475085-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Online Resource
    Open Access Request
    Availability (electronic / print)
  • 8
    Online Resource
    Online Resource
    Linkage analysis of the Bcg gene on mouse chromosome 1. Identification of a tightly linked marker.
    The American Association of Immunologists ; 1989
    In:  The Journal of Immunology Vol. 142, No. 12 ( 1989-06-15), p. 4507-4513
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 142, No. 12 ( 1989-06-15), p. 4507-4513
    Abstract: We have mapped and determined the gene order of five cloned genes in the vicinity of the murine host resistance gene Bcg on mouse chromosome 1. For this, we have used a RFLP-type analysis in panels of 43 recombinant inbred strains, 3 congenic mouse strains, and 186 segregating backcross progeny derived from inbred strains of Bcgr and Bcgs genotypes. The Bcg alleles of segregating animals were established by in vivo infection with Mycobacterium bovis (Bacillus Calmette-Guérin) strain Montreal. Genomic DNA prepared from progenitor mouse strains was isolated, digested with restriction endonucleases, and analyzed by Southern blotting to identify strain-specific RFLP for each DNA marker tested. Among a number of DNA markers tested, Len2, Fn, Vil, Alpi, and Achrg were found to co-segregate with Bcg in mouse strains congenic for this locus. Detailed segregation analysis of the five markers and Bcg showed that Vil was extremely close to Bcg with no recombinant identified, whereas Fn and Len2 were located 4.5 and 9 cM proximal of Bcg, respectively. Alpi and Achrg mapped 5 and 5.5 cM distal from Bcg, respectively. Pedigree analysis in the recombinant inbred strains and backcross animals indicated the gene order: centromere-Len2-Fn-Vil,Bcg-Alpi-Achrg. The tightly linked Vil marker can now be used as an entry point in recombinant genomic DNA libraries to clone sequences overlapping Bcg. This group of five genes flanking Bcg on mouse chromosome 1 is precisely conserved on the telomeric end of the long arm of human chromosome 2q. Our results suggest that a likely location for a putative human homologue to the murine host resistance gene Bcg is the long arm of human chromosome 2 (2q32-qter).
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.142.12.4507
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1989
    detail.hit.zdb_id: 1475085-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Online Resource
    Open Access Request
    Availability (electronic / print)
  • 9
    Online Resource
    Online Resource
    Cellular mechanisms of genetically controlled host resistance to Mycobacterium bovis (BCG).
    The American Association of Immunologists ; 1983
    In:  The Journal of Immunology Vol. 131, No. 4 ( 1983-10-01), p. 1966-1972
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 131, No. 4 ( 1983-10-01), p. 1966-1972
    Abstract: Multiplication of Mycobacterium bovis (BCG) in the reticuloendothelial tissues of the mouse is controlled by the Chromosome 1 locus (Bcg), which exists in two allelic forms, resistant (Bcgr) and susceptible (Bcgs). We have investigated the phenotypic expression of this locus at the cellular level in vivo. No significant differences were observed in the early clearance of BCG from the bloodstream and peritoneal cavity, nor in the uptake of the infectious inoculum in spleen and liver of the mice of Bcgr and Bcgs strains. Inflammatory response to an i.p. injection of live BCG, with respect to both the cell populations involved and the kinetics of their appearance, was comparable in Bcgr and Bcgs mice. A kinetic study of BCG infection in congenitally athymic mice that carried the "nude" mutation on Bcgr (AKR/J) or Bcgs (BALB/c) background showed that the functional absence of T lymphocytes did not influence the expression of the Bcg gene. The population expressing the Bcg gene seems to be a mature cell of the mononuclear phagocyte lineage: it was resistant to a 950-rad dose of x-irradiation; it was susceptible to a prolonged exposure to silica; and, as demonstrated in radiation chimeras, it originated from bone marrow-derived precursors.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.131.4.1966
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1983
    detail.hit.zdb_id: 1475085-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Online Resource
    Open Access Request
    Availability (electronic / print)
  • 10
    Online Resource
    Online Resource
    Antitubulin antibodies. II. Natural autoantibodies and induced antibodies recognize different epitopes on the tubulin molecule.
    The American Association of Immunologists ; 1988
    In:  The Journal of Immunology Vol. 141, No. 9 ( 1988-11-01), p. 3135-3141
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 141, No. 9 ( 1988-11-01), p. 3135-3141
    Abstract: Natural and induced antitubulin antibodies were compared for their epitope recognition on alpha- and beta-tubulin subunits by immunoenzymatic assays and Western blot techniques on partially digested tubulin molecules. Our results indicated that natural autoantibodies recognized different epitopes from those recognized by induced antibodies, because: 1) all polyspecific natural autoantibodies tested so far recognized the same or very overlapping epitopes in the central part of both alpha- and beta-subunits (between positions 100 and 300 on the tubulin amino acid sequence) and that this epitope differed from the various epitopes recognized by induced antitubulin antibodies on the amino-terminal or carboxy-terminal parts of the tubulin subunits; 2) one human myeloma protein (monoclonal (m)IgA, kappa) with a monospecific antitubulin activity bound to an epitope around position 310 on both alpha- and beta-subunits and a second human mIg (mIgM, kappa) with a monospecific anti-beta activity bound to an epitope on the carboxy-terminal part of the subunit around amino acid position 350. Both epitopes differed from epitopes recognized by induced antitubulin antibodies. These results thus confirmed our previous findings indicating that natural and induced antitubulin antibodies do not share cross-reactive idiotopes.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.141.9.3135
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1988
    detail.hit.zdb_id: 1475085-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Online Resource
    Open Access Request
    Availability (electronic / print)
Nothing or not found what you are looking for? Please check your search query or use the Interlibrary Loan Search.
Close ⊗
This website uses cookies and the analysis tool Matomo. Further information can be found on the KOBV privacy pages