Asunto(s)
Antiinflamatorios/administración & dosificación , Hipertensión Pulmonar/tratamiento farmacológico , Lupus Eritematoso Sistémico/tratamiento farmacológico , Prednisolona/administración & dosificación , Adulto , Femenino , Hemodinámica/efectos de los fármacos , Hemodinámica/fisiología , Humanos , Hipertensión Pulmonar/complicaciones , Lupus Eritematoso Sistémico/complicaciones , Nifedipino/uso terapéutico , Vasodilatadores/uso terapéuticoRESUMEN
Particles of isolate T of potato mop-top furovirus (PMTV) contain three RNA species (6.5, 3.0 and 2.5 kb). Hybridization tests with cloned cDNA probes showed that none of these species was derived from another. RNA 2 (2962 nt), which was sequenced, has non-coding regions of 368 nt and 285 nt at the 5' end and 3' end, respectively. Near the 5' terminus, nucleotides 46 to 110 are able to form a stem-loop structure, the stem of which has 23 bp with only one mismatch and one unpaired nucleotide. From the 5' end, the four open reading frames encode proteins of 51K, 13K, 21K and 8K. The first three of these have sequence similarity to the triple-gene-block proteins of other viruses, particularly barley stripe mosaic hordeivirus. The 51K protein contains a putative NTP-binding motif and the 13K and 21K proteins each contain two hydrophobic regions separated by a hydrophilic region. The 8K protein is rich in cysteine. PMTV differs from other furoviruses in having a tripartite genome. Its RNA 2 differs in gene content from the RNA 2 of soil-borne wheat mosaic virus, which lacks a triple gene block, and from that of beet necrotic yellow vein virus, which has a coat protein gene and read-through domain to the 5' side of its triple gene block. The gene arrangement in PMTV is therefore novel for a furovirus.
Asunto(s)
Genoma Viral , Virus de Plantas/genética , ARN Viral/genética , Solanum tuberosum/virología , Secuencia de Aminoácidos , Secuencia de Bases , Clonación Molecular , ADN Complementario , Biblioteca de Genes , Datos de Secuencia Molecular , Conformación de Ácido Nucleico , Sistemas de Lectura Abierta/genética , ARN Viral/química , Alineación de Secuencia , Análisis de Secuencia de ADN , Homología de Secuencia de Aminoácido , Proteínas Virales/genéticaRESUMEN
Macrophages infiltrated into synovium play an important role in joint destruction in inflammatory joint diseases. In this study we focused on the production of monocyte chemoattractant protein-1 (MCP-1), a recently identified monocyte chemotactic protein, by inflammatory synovium. Synovial fluid (SF) from rheumatoid arthritis (RA), osteoarthritis, gout, and traumatic arthritis contained MCP-1. MCP-1 was produced in the synovium of patients with RA and other inflammatory joint disease in in vitro culture systems; differences in the amounts produced were not significant. Synovial MCP-1 production in RA was further investigated. Levels of MCP-1 were significantly correlated with levels of IL-1 beta, IL-6, and IL-8 in the culture supernatants of synovia from RA. Using immunohistochemical techniques, MCP-1 was detected in the lining and sublining cells and in the vascular endothelial cells of rheumatoid synovia. Rheumatoid synovia with active inflammation were stained more intensely by anti-MCP-1 antibody than were those with weak or inactive inflammation. IL-1 beta and TNF-alpha stimulated the expression of MCP-1 mRNA and de novo MCP-1 synthesis by cultured synovial cells. These results suggest the production of MCP-1 by synovium of various inflammatory joint diseases. In rheumatoid synovium, a cytokine network involving MCP-1 and other proinflammatory cytokines (IL-1 beta, IL-6, IL-8, and TNF-alpha) contributes to the immunopathogenesis of RA.