Abstract Various silver-coated implants have been developed to prevent implant-associated infections and have shown dramatic effects in vitro . However, the in vivo results have been inconsistent. Recent in vitro studies showed that silver exerts antibacterial activity by mediating the generation of reactive oxygen species in the presence of oxygen. To maintain its antibacterial activity in vivo , the silver should remain in an ionic state and be stably bound to the implant surface. Here, we developed a novel bacteria-resistant hydroxyapatite film in which ionic silver is immobilized via inositol hexaphosphate chelation using a low-heat immersion process. This bacteria-resistant coating demonstrated significant antibacterial activity both in vitro and in vivo . In a murine bioluminescent osteomyelitis model, no bacteria were detectable 21 days after inoculation with S. aureus and placement of this implant. Serum interleukin-6 was elevated in the acute phase in this model, but it was significantly lower in the ionic-silver group than the control group on day 2. Serum C-reactive protein remained significantly higher in the control group than the ionic-silver group on day 14. Because this coating is produced by a low-heat immersion process, it can be applied to complex structures of various materials, to provide significant protection against implant-associated infections.
Stimulation with specific pairs of anti-CD2 antibodies can induce T cell activation and proliferation. In this study, we investigate the significance of ZAP-70 in CD2 signaling using ZAP-70-deficient T cells derived from a CD8-deficient patient and show that ZAP-70 is necessary for cellular proliferation and cytokine production in T cells stimulated via CD2. Biochemical analyses show that CD2 stimulation induces activation of mitogen-activated protein kinase (MAPK) superfamily in ZAP-70-deficient T cells, indicating that a ZAP-70-independent pathway(s) exists for MAPK superfamily activation via CD2. In contrast, intracellular Ca2+ mobilization and activation of nuclear factor of activated T cells (NFAT) upon CD2 triggering were impaired in T cells lacking ZAP-70. Furthermore, we found that pharmacological Ca2+ elevation combined with CD2 stimulation restored NFAT activation and subsequent cytokine production in ZAP-70-deficient T cells. These results indicate that in CD2 signaling, ZAP-70 plays an essential role in Ca2+ mobilization and NFAT activation.
Journal Article 70–75 kd molecules expressed on LGL and T cells recognized by a mitogenic monoclonal antibody YTA-1; co-modulation and functional association with the interleukin 2 receptor p75 Get access Katsuji Sugie, Katsuji Sugie 1Institute for Immunology, Faculty of Medicine, Kyoto UniversityYoshida, Sakyo, Kyoto 606, Japan22nd Department of Internal Medicine, Faculty of MedicineKyoto University, Shogoin-Kawahara chou, Sakyo, Kyoto 606, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar Yoshiaki Nakamura, Yoshiaki Nakamura 1Institute for Immunology, Faculty of Medicine, Kyoto UniversityYoshida, Sakyo, Kyoto 606, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar Yutka Tagaya, Yutka Tagaya 1Institute for Immunology, Faculty of Medicine, Kyoto UniversityYoshida, Sakyo, Kyoto 606, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar Shigeo Koyasu, Shigeo Koyasu 3Department of Cell Biology, The Tokyo Metropolitan Institute of Medical Science3-18-22, Honokomagome, Bunkyo-ku, Tokyo 113, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar Ichiro Yahara, Ichiro Yahara 3Department of Cell Biology, The Tokyo Metropolitan Institute of Medical Science3-18-22, Honokomagome, Bunkyo-ku, Tokyo 113, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar Kenji Takakura, Kenji Takakura 1Institute for Immunology, Faculty of Medicine, Kyoto UniversityYoshida, Sakyo, Kyoto 606, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar Shunichi Kumagai, Shunichi Kumagai 22nd Department of Internal Medicine, Faculty of MedicineKyoto University, Shogoin-Kawahara chou, Sakyo, Kyoto 606, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar Hiroo Imura, Hiroo Imura 22nd Department of Internal Medicine, Faculty of MedicineKyoto University, Shogoin-Kawahara chou, Sakyo, Kyoto 606, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar Junji Yodoi Junji Yodoi 1Institute for Immunology, Faculty of Medicine, Kyoto UniversityYoshida, Sakyo, Kyoto 606, Japan Correspodence to: Dr Junji Yodoi, Institute for Immunology, Faculty of Medicine, Kyoto University, Yoshida, Sakyo, Kyoto 606, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar International Immunology, Volume 2, Issue 5, May 1990, Pages 391–397, https://doi.org/10.1093/intimm/2.5.391 Published: 01 May 1990 Article history Received: 09 October 1989 Accepted: 17 February 1990 Published: 01 May 1990
A rearranged TCR alpha transgene remains transcriptionally inactive in rag-2-/- thymocytes but can be induced by CD3-mediated signals with concomitant maturation of double-negative (DN) thymocytes to the CD4+CD8+ double-positive (DP) stage. Reciprocally, the same signals silence pre-TCR alpha (pT alpha) expression. In normal C57BL/6 thymocytes, TCR alpha expression is not detected in DN thymocytes while, in contrast, TCR beta expression is initiated at the most immature c-kit+CD44+CD25- stage and continues throughout thymocyte development. pT alpha expression is first detected at the intermediate c-kit +/- CD44+CD25+ DN stage, increases during transition to the more mature c-kit-CD44-CD25+ stage and is lost at the DP stage. Thus, although TCR beta and pT alpha expression are independent, the pre-TCR complex mediates signals controlling the appearance of alpha beta TCR through selective regulation of TCR alpha and pT alpha genes.
Properties of the Caulobacter penicillin-binding proteins (PBPs) were studied. Several Caulobacter strains possessed at least five major PBPs, as shown previously for C. crescentus CB15, namely PBP1A, PBP1Bs, PBP2, PBP3 and PBP4. PBP4 was not detected in the C. crescentus strain CB13. None of the strains examined possessed the major PBPs of low molecular weight which have been found in other species of bacteria. The biochemical properties of the Caulobacter PBPs were studied further with two strains, C. crescentus CB13 and C. crescentus CB15. In these strains, PBPs of similar molecular weight were similar in properties such as affinity for β-lactam antibiotics and heat sensitivity. These properties were markedly different from those of PBPs of Escherichia coli and other bacteria. To elucidate the functions of the Caulobacter PBPs, the effects of several β-lactam antibiotics on cell morphology and their affinities for different PBPs were examined. The relationship between the antibiotic effect and its affinity for PBPs suggests that PBP3 is involved in the process of cell division.
List of DRA (http://trace.ddbj.nig.ac.jp/dra/index_e.html) accession numbers of the FANTOM5 samples, sequences and genomic coordinations. Files are in tab-delimited format, which includes * Library ID * FFID * BioSamples accession number * DRA experiment accession number * DRA run accession numbers * DRA analysis accession number for genomic coordination (BAM file) * DRA analysis accession number for CTSS (BED file) * Experiment method (CAGE/RNA-Seq/sRNA-Seq)
a tab delimited flat file (SDRF file) describing the experimental details for mouse quality control samples for the low quantity version of the HeliScopeCAGE protocol
TOMURA, K., KANG, H., MITAMURA, K., TAKEI, M., KARASAKI, M., KOYASU, S. and SAWADA, S. IL-2 Enhancing Factor(s) in B Cell Supernatants from Patients with Rheumatoid Arthritis or Systemic Lupus Erythematosus. Tohoku J. Exp. Med., 1989, 159 (3), 171-183- Culture supernatants of B cells from patients with rheumatoid arthritis (RA) or systemic lupus erythematosus (SLE) in the active stage enhanced interleukin 2 (IL-2) dependent proliferation of CTLL A/J cells. This activity, designated B cell-derived growth-enhancing factor-2 (BGEF-2), was recovered by gel filtration of a molecular weight between 15, 000 and 20, 000. BGEF-2 itself did not show IL-2 activity nor IL-1 activity, and BGEF-2 activity was not detected in the following cytokines: Interferon-α (IFN-α), interferon-γ (IFN-γ), tumor necrosis factor (TNF), interleukin 4 (IL-4), interleukin 5 (IL-5) and interleukin 6 (IL-6). Furthermore, BGEF-2 was distinguishable from B cell-derived growth-enhancing factor described in a previous paper [Kang et al. (1987) J. Immunol., 139, 1154-1160]. BGEF-2 was produced by B cells from patients with RA or SLE only when the patients were in the active stage. BGEF-2 enhanced IL-2-dependent growth of peripheral blood T cells from patients with active RA, but did not enhance the growth of T cells from healthy voluteers. These results suggest that BGEF-2 is a B cell-derived lymphokine which plays an important role in the pathogenesis of RA and SLE.
