Despite similarities in the involved organs, there are considerable clinical and pathological differences between IgG(4)+MOLPS and SS. Based on the clinical features and good response to glucocorticoids, we propose a new clinical entity: IgG(4)+MOLPS.

Influenza A virus RNA genome exists as eight-segmented ribonucleoprotein complexes containing viral RNA polymerase and nucleoprotein (vRNPs). Packaging of vRNPs and virus budding take place at the apical plasma membrane (APM). However, little is known about the molecular mechanisms of apical transport of newly synthesized vRNP. Transfection of fluorescent-labeled antibody and subsequent live cell imaging revealed that punctate vRNP signals moved along microtubules rapidly but intermittently in both directions, suggestive of vesicle trafficking. Using a series of Rab family protein, we demonstrated that progeny vRNP localized to recycling endosome (RE) in an active/GTP-bound Rab11-dependent manner. The vRNP interacted with Rab11 through viral RNA polymerase. The localization of vRNP to RE and subsequent accumulation to the APM were impaired by overexpression of Rab binding domains (RBD) of Rab11 family interacting proteins (Rab11-FIPs). Similarly, no APM accumulation was observed by overexpression of class II Rab11-FIP mutants lacking RBD. These results suggest that the progeny vRNP makes use of Rab11-dependent RE machinery for APM trafficking.

Efficient transcription and replication of the influenza virus genome are dependent upon host-derived factors. Using an in vitro RNA synthesis system, we have purified and identified Hsp90 as one of the host factors that stimulate viral RNA polymerase activity. Hsp90 interacted with the PB2 subunit of the viral RNA polymerase through the amino-terminal chaperone domain and the middle region containing a highly acidic domain. The acidic middle region was also responsible for its stimulatory activity. We found that a portion of Hsp90 is re-localized to the cell nucleus after viral infection. A PB2 fragment containing a Hsp90 binding domain inhibited viral gene expression in a dominant-negative manner. These results suggest that Hsp90 is a host factor for the influenza virus RNA polymerase.Influenza A virus belongs to the Orthomyxoviridae family, and its genome consists of eight segmented, single-stranded RNA of negative polarity (1). The transcription promoter and the replication signal of the viral genome exist at the 3Ј and 5Ј termini of each of the eight segments. Components associated with ribonucleoprotein complexes (vRNP) 1 purified from virions are the minimum factors required for primary transcription. The genome RNA forms vRNP with the viral RNA polymerases consisting of three subunits, PB2, PB1, and PA (2), and nucleocapsid protein (NP). Transcription of the influenza virus genome is initiated with host-derived oligo RNA containing a cap structure. PB2 contains cap recognition domains at its carboxyl-terminal region. The capped RNA bound to PB2 is cleaved by the PB1 subunit 10 -15 bases downstream from the 5Ј end (2-4), and the capped RNA fragment serves as a primer for viral mRNA synthesis catalyzed by PB1 (5). Elongation of the RNA chain proceeds until the polymerase reaches a polyadenylation signal consisting of 5-7 uracil (U) residues located near the 5Ј terminal region of the vRNA (6). The viral RNA polymerase polyadenylates the nascent RNA chain possibly by a slippage mechanism at the U-stretch (7). Replication of the vRNA is thought to take place by a primer-independent, twostep reaction, namely the complementary RNAs (cRNA) are first synthesized from vRNA templates, and then the progeny vRNAs are amplified from cRNA templates. Genetic analyses suggest that PA participates in the replication process (8). However, vRNP complexes isolated from virions are incapable of catalyzing replication reactions.A variety of host proteins have been identified as factors involved in the regulation of the RNA synthesis of viral genomes of Paramyxoviridae, the genome of which contains nonsegmented and single-stranded RNA of negative polarity. Tubulin, an acidic cytoplasmic structural protein, is one of the host factors for RNA synthesis of the measles virus, VSV, and Sendai virus genomes (9, 10). RNA synthesis of these viral genomes is catalyzed by viral RNA polymerases consisting of L and P subunits. Tubulin interacts with L protein, a catalytic subunit of the viral RNA polymerase, and is present in isolated tr...

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Adult height has directionally opposing relationships with risk of death from several different major causes of chronic diseases.

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Evaluation of the Effects of Shift Work on Nutrient Intake: A Cross-sectional Study: Yuko MORIKAWA, et al. Department of Epidemiology andPublic Health, Kanazawa Medical University-The aim of this study was to investigate the effects of shift work on nutrient intakes, including macronutrient intake and micronutrient intake, in a large sample size. The study population included 2,254 male manual workers, 20-59 yr of age, employed in a factory. A selfadministered diet history questionnaire was used. The subjects were classified into 3 groups according to their work schedule: (i) fixed day workers; (ii) shift workers without midnight shifts; and (iii) shift workers with midnight shifts. The nutrient intakes of the groups were compared by age group. There was a significant difference in nutrient intakes between subjects aged 20-29 yr and those aged 30 yr and over. Among subjects aged 20-29 yr, the energy density value for saturated fat and the energy adjusted intakes of calcium, potassium, vitamin A, and vitamin B1 were the lowest among shift workers with midnight shifts. Among subjects aged 30 yr and over, the total energy intake was the highest among shift workers with midnight shifts; the difference was significant compared to fixed day workers. Shift workers with midnight shifts had the highest intake of cereals among subjects 30 yr of age and older. In conclusion, there were no significant differences in nutrient intakes between fixed day workers and shift workers without midnight shift. Shift work, particularly midnight shift work, affected nutrient intake. The impact of shift work on nutrient intakes differed by age and the type of shift work. (J Occup Health 2008; 50: 270-278)