Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0149514 (bronchitis)
 6,902 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

L1 protein is a neutrophil cytoplasmic protein and its measurement in body fluids probably reflects neutrophil turnover. The serum range in normal subjects is wide (60-5700 microgram/l) with a median value of 547 microgram/l but lower (2P less than 0.01) than in patients with chronic obstructive bronchitis (median, 750; range, 99-500 microgram/l). Patients with "emphysema" do not have increased serum L1 protein concentrations. On the other hand patients with a variety of active lung diseases have raised concentrations compared to normal subjects suggesting that L1 protein is a marker of inflammation within the lung. The secretion concentration of L1 protein reflects its purulent nature and rapid falls in both serum and secretion L1 concentration occur with treatment. The results suggest that sequential L1 measurements may provide a measure of the inflammatory state of the lung and a rapid indication of the response to treatment.
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PMID:Relationship of neutrophil cytoplasmic protein (L1) to acute and chronic lung disease. 653 50

Chlamydia pneumoniae is an important human respiratory pathogen that is responsible for an estimated 10% of community-acquired pneumonia and 5% of bronchitis and sinusitis cases. We examined changes in global protein expression profiles associated with the redifferentiation of reticulate body (RB) to elementary body (EB) as C. pneumoniae cells progressed from 24 to 48 h postinfection in HEp2 cells. Proteins corresponding to those showing the greatest changes in abundance in the beginning of the RB to EB transition were then identified from purified EBs. Among the 300 spots recognized, 35 proteins that were expressed at sufficiently high levels were identified by mass spectrometry. We identified C. pneumoniae proteins that showed more than 2-fold increases in abundance in the early stages of RB to EB transition, including several associated with amino acid and cofactor biosynthesis (Ndk, TrxA, Adk, PyrH, and BirA), maintenance of cytoplasmic protein function (GroEL/ES, DnaK, DksA, GrpE, HtrA, ClpP, ClpB, and Map), modification of the bacterial cell surface (CrpA, OmpA, and OmcB), energy metabolism (Tal and Pyk), and the putative transcriptional regulator TctD. This study identified C. pneumoniae proteins involved in the process of redifferentiation into mature, infective EBs and indicates bacterial metabolic pathways that may be involved in this transition. The proteins involved in RB to EB transition are key to C. pneumoniae infection and are perhaps suitable targets for therapeutic intervention.
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PMID:Identification of Chlamydia pneumoniae proteins in the transition from reticulate to elementary body formation. 1692 Nov 67