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Shock Cognate Protein (shock + cognate_protein)

Distribution by Scientific Domains
Life Sciences40%

Kinds of Shock Cognate Protein

  • heat shock cognate protein
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    Selected Abstracts

    Cognate Hsp70 gene is induced during deep larval diapause in the moth Sesamia nonagrioides

    INSECT MOLECULAR BIOLOGY, Issue 2 2009
    T. Gkouvitsas
    Abstract The complete cDNA sequences of Heat shock cognate protein 70 (SnoHsc70) and Heat shock protein 70 (SnoHsp70) were determined from the corn stalk borer Sesamia nonagrioides (Lef.). They encode 653 amino acids (Hsc70) and 633 amino acids (Hsp70), with calculated molecular masses of 71.5 kDa and 70.2 kDa respectively. SnoHsc70 is constitutively expressed, and SnoHsp70 is heat-inducible in non-diapausing insects. SnoHsp70 is down regulated during diapause, while SnoHsc70 is induced as the larvae enter deep diapause. High temperature stress during diapause has no further effect on transcript levels of SnoHsc70. Our results show that SnoHsc70 may play important roles in assisting protein conformation during specific stages of diapause. [source]

    Heat Shock Transcription Factors and the hsp70 Induction Response in Brain and Kidney of the Hyperthermic Rat During Postnatal Development

    JOURNAL OF NEUROCHEMISTRY, Issue 1 2000
    Andrew J. Morrison
    Abstract : Heat shock transcription factor (HSF) 1 levels increase in brain regions and decline in kidney during postnatal rat development. In both neonatal and adult rats, levels of HSF1 protein in brain and kidney are proportional to the levels of HSF DNA-binding activity and the magnitude of heat shock protein hsp70 induction after thermal stress. There appears to be more HSF1 protein in adult brain than is needed for induction of hsp70 after thermal stress, suggesting that HSF1 may have other functions in addition to its role as a stress-inducible activator of heat shock genes. HSF2 protein levels decline during postnatal rat development in brain regions and kidney. Gel mobility shift analysis shows that HSF2 is not in a DNA-binding form in the neonatal brain and kidney, suggesting that HSF2 may not be involved in the constitutive expression of hsps in early postnatal development. There is no apparent relationship between levels of HSF2 protein and basal levels of hsp90, hsp70, heat shock cognate protein hsc70, and hsp60. [source]

    Proteomic analysis of novel Cry1Ac binding proteins in Helicoverpa armigera (Hübner)

    ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY (ELECTRONIC), Issue 2 2010
    Li-Zhen Chen
    Abstract Aminopeptidase N (APN) and cadherin-like proteins have been previously identified as Cry1Ac-binding proteins in Helicoverpa armigera (Hübner). In this study, a proteomic approach was used to identify novel Cry1Ac-binding proteins in H. armigera. Brush border membrane vesicles (BBMV) of H. armigera were extracted and separated by two-dimensional gel electrophoresis (2-DE). Cry1Ac-binding proteins were detected using antisera against Cry1Ac. Peptide mass fingerprinting (PMF) was used to identify Cry1Ac-binding proteins. In total, four proteins were identified as candidate Cry1Ac-binding proteins in H. armigera: vacuolar ATP synthase (V-ATPase) subunit B, actin, heat shock cognate protein (HSCP), and a novel protein. © 2009 Wiley Periodicals, Inc. [source]

    Both CD4+ and CD8+ T cell epitopes fused to heat shock cognate protein 70 (hsc70) can function to eradicate tumors

    CANCER SCIENCE, Issue 5 2008
    Shusaku Mizukami
    Vaccination with heat shock proteins (HSP) protects mice from challenge with the tumor from which the HSP were isolated. The antigenicity of HSP vaccination is thought to result from HSP-associated endogenous major histocompatibility complex class I peptides or their precursors. The vaccination effect can be achieved in an adjuvant-free manner and is mediated by CD8+ T cells, indicating that HSP can act as a natural adjuvant and cross-prime T cells in vivo. We previously devised a recombinant vaccine composed of a CD8+ T cell epitope fused to the carboxyl-terminus of hsc70 and demonstrated efficient generation of antigen-specific cytotoxic T lymphocyte (CTL) after vaccination with a few micrograms of the hsc70-CTL epitope fusion protein. The present study aimed to determine if the fusion protein vaccine could control tumor growth in vivo and whether simultaneous fusion of a CD4+ T cell epitope to the amino terminus of the hsc70-CTL epitope would be a more potent vaccine compared to the CTL epitope alone. Ovalbumin (OVA),derived 8 mer peptide, OVA257-264, and 16mer peptide, OVA265-280, were used as CD8+ and CD4+ T cell epitopes, respectively. Vaccination with hsc70-OVA257-264 generated peptide specific CTL more effectively than a peptide plus incomplete Freund's adjuvant combination, and suppressed growth of OVA expressing EL4 (E.G7) and B16 melanoma tumor cells. Addition of OVA265-280 to the amino-terminus of hsc70-OVA257-264 (OVA265-280 -hsc70-OVA257-264) enhanced the generation of the OVA257-264 -specific CTL population, leading to better eradication of MO5 lung metastasis compared to hsc70-OVA257-264. Our results suggest that fusion of both CD4+ and CD8+ T cell epitopes to hsc70 enhances tumor immunity beyond the effect of the CD8+ T cell epitope alone. (Cancer Sci 2008; 99: 1008,1015) [source]

    Novel biomarker of HTLV-1-associated disease: Specific appearance of antibody recognizing the receptor-binding site on HTLV-1 envelope protein

    CANCER SCIENCE, Issue 10 2004
    Yasuko Sagara
    We previously showed that 71-kDa heat shock cognate protein (HSC70) functions as a cellular receptor for gp46 protein via the gp46,197 region, corresponding to Asp197 to Leu216 of human T-cell lymphotropic virus type 1 (HTLV-1), leading to cell-to-cell transmission of HTLV-1. We found that HSC70 protein was contained in goat serum and casein used as blocking agents in the usual ELISA method. Here, it was demonstrated that HSC70 contamination in the blocking agents causes a false-negative result in the detection of anti-gp46,197 antibody in serum samples from HTLV-1-infected individuals. By using ELISA without the blocking agents, we detected antibodies recognizing the HSC70-binding site of gp46, and the anti-gp46,197 antibody specifically appeared in sera from patients with HTLV-1-associated diseases. The frequency of serum anti-gp46,197 antibody-positive individuals was 98% and 100% among ATLL and HAM/TSP patients, respectively, but only 6% among asymptomatic HTLV-1-infected carriers (ACs). The antibody titer in ATLL and HAM/TSP patients was higher than that in ACs (P>0.002 for ATLL; P>0.0001 for HAM/ TSP). These findings suggest that appearance of the anti-gp46,197 antibody is a predictive marker for the onset of HTLV-1-associated disease. [source]