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  1. Article ; Online: Attacking the source: anti-PDX-1 responses in type 1 diabetes.

    Luzardo, Yaima / Mathews, Clayton Elwood

    Laboratory investigation; a journal of technical methods and pathology

    2009  Volume 90, Issue 1, Page(s) 6–8

    Abstract: Type 1 diabetes (T1D) develops as a consequence of abnormal responses against several self-antigens, eventually leading to the autoimmune attack and destruction of the insulin-producing beta cells in the pancreas. In this issue of Laboratory ... ...

    Abstract Type 1 diabetes (T1D) develops as a consequence of abnormal responses against several self-antigens, eventually leading to the autoimmune attack and destruction of the insulin-producing beta cells in the pancreas. In this issue of Laboratory Investigation, Li et al propose the transcription factor Pancreatic and duodenal homeobox 1 (PDX-1) as a T1D autoantigen by demonstrating autoreactivity to this pancreas-specific protein in both the NOD mouse model and patients with T1D. Because of the known roles of PDX-1 in pancreatic development as well as beta cell maintenance and function, targeting of PDX-1 expressing cells may result in the elimination of not only beta cells but also the progenitor cells required for regeneration of insulin-producing cells.
    MeSH term(s) Animals ; Autoantibodies/immunology ; Autoantigens/immunology ; Diabetes Mellitus, Type 1/immunology ; Homeodomain Proteins/immunology ; Humans ; Trans-Activators/immunology
    Chemical Substances Autoantibodies ; Autoantigens ; Homeodomain Proteins ; Trans-Activators ; pancreatic and duodenal homeobox 1 protein
    Language English
    Publishing date 2009-12-23
    Publishing country United States
    Document type Comment ; Editorial ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80178-1
    ISSN 1530-0307 ; 0023-6837
    ISSN (online) 1530-0307
    ISSN 0023-6837
    DOI 10.1038/labinvest.2009.121
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Physiologic effects of forced down-regulation of dnaK and groEL expression in Streptococcus mutans.

    Lemos, José A / Luzardo, Yaima / Burne, Robert A

    Journal of bacteriology

    2007  Volume 189, Issue 5, Page(s) 1582–1588

    Abstract: Strains of Streptococcus mutans lacking DnaK or GroEL appear not to be isolable. To better distinguish the roles played by these chaperones/chaperonins in the physiology of S. mutans, we created a knockdown strategy to lower the levels of DnaK by over 95% ...

    Abstract Strains of Streptococcus mutans lacking DnaK or GroEL appear not to be isolable. To better distinguish the roles played by these chaperones/chaperonins in the physiology of S. mutans, we created a knockdown strategy to lower the levels of DnaK by over 95% in strain SM12 and the level of GroEL about 80% in strain SM13. Interestingly, GroEL levels were approximately twofold higher in SM12 than in the parent strain, but the levels of DnaK were not altered in the GroEL knockdown strain. Both SM12 and SM13 grew slower than the parent strain, had a strong tendency to aggregate in broth culture, and showed major changes in their proteomes. Compared with the wild-type strain, SM12 and SM13 had impaired biofilm-forming capacities when grown in the presence of glucose. The SM12 strain was impaired in its capacity to grow at 44 degrees C or at pH 5.0 and was more susceptible to H(2)O(2), whereas SM13 behaved like the wild-type strain under these conditions. Phenotypical reversions were noted for both mutants when cells were grown in continuous culture at a low pH, suggesting the occurrence of compensatory mutations. These results demonstrate that DnaK and GroEL differentially affect the expression of key virulence traits, including biofilm formation and acid tolerance, and support that these chaperones have evolved to accommodate unique roles in the context of this organism and its niche.
    MeSH term(s) Bacterial Proteins/physiology ; Chaperonin 60/genetics ; Chaperonin 60/physiology ; Down-Regulation ; Hot Temperature ; Hydrogen-Ion Concentration ; Molecular Chaperones/genetics ; Molecular Chaperones/physiology ; Proton-Translocating ATPases/metabolism ; Streptococcus mutans/physiology
    Chemical Substances Bacterial Proteins ; Chaperonin 60 ; Molecular Chaperones ; Proton-Translocating ATPases (EC 3.6.3.14)
    Language English
    Publishing date 2007-03
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.01655-06
    Database MEDical Literature Analysis and Retrieval System OnLINE

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