Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0012739 (disseminated intravascular coagulation)
 8,673 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

CAP18 (cationic antimicrobial protein, 18kDa) is a 142 amino acid protein originally isolated from rabbit granulocytes using agglutination of LPS-coated erythrocytes as an assay. CAP-18 is composed of an N-terminal domain of unknown function (CAP181-105) and a C-terminal LPS-binding domain (CAP18106-142). Synthetic CAP18106-142 and CAP18106-137, a 32-amino acid peptide resulting from the truncation of 5 amino acids from the C-terminus of CAP18106-142, inhibited LPS-induced tissue factor generation, nitric oxide production and TNF release by macrophages. Mice treated with CAP18106-142 or CAP18106-137 were significantly protected from LPS lethality. Although CAP18106-142 and CAP18106-137 were highly active, other fragments of CAP18106-142, including CAP18110-142 with a truncated N-terminus, did not exhibit LPS-binding and LPS-neutralizing activities. Both peptides had broad anti-microbial activity against both Gram-negative bacteria such as Escherichia coli, Salmonella typhimurium, Klebsiella pneumoniae, Pseudomonas aeruginosa (IC50; 40-100 nM) and Gram-positive bacteria such as Staphylococcus aureus(Methicillin sensitive and resistant strains) and Streptococcus pneumoniae (IC50; 100-200nM). We cloned a CAP18 family protein from human granulocytes. The cloned cDNA encoded 140 amino acid residues. Human CAP18 (CAP181-140) was highly homologous to that of rabbit. A 32- amino-acid C-terminal fragment (CAP18104-135) was shown to bind LPS, inhibit LPS-induced tissue factor generation by murine macrophages, and protect mice from LPS lethality. This peptide exhibited antimicrobial activity against both Gram-negative and Gram-positive bacteria. We hypothesize that CAP18 and the derived peptides bind to LPS and alter the capacity of LPS to initiate disseminated intravascular coagulation. In this regard, CAP may act as host defense protein against infectious diseases, and have therapeutic potential for sepsis and endotoxin shock.
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PMID:Structure and functions of endotoxin-binding peptides derived from CAP18. 852 37

Cilia with paddle-shaped or disc-shaped tips enclosing a curved end of the axoneme (paddle cilia or discocilia) have been described in a variety of marine invertebrates. Although numerous studies, in which fixed specimens were used, claimed that paddle cilia and discocilia are genuine structures of unknown function, several studies, in which fresh living material was used, reported that modified cilia are artifacts. We have re-investigated a recent SEM report that paddle cilia are genuine organelles in veliger larvae of marine bivalves (Campos and Mann, 1988). Using high-speed video and electronic flash DIC microscopy, we find no paddle cilia in living larvae of Spisula solidissima and Lyrodus pedicellatus. Hypotonic seawater, however, induces formation of paddle cilia and vesiculations of the ciliary membrane in these veligers, as does the hypotonic SEM fixative used by Campos and Mann (1988). Fixatives that are isosmotic with seawater, on the other hand, do not induce paddle cilia. We conclude that paddle cilia are artifacts, and we propose a unifying mechanism to explain their production in various animals under different conditions.
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PMID:On the Nature of Paddle Cilia and Discocilia. 2930 55