Disease relevance of NKL

• NK-lysin showed high anti-bacterial activity against Escherichia coli and Bacillus megaterium and moderate activity against Acinetobacter calcoaceticus and Streptococcus pyogenes [1].
• Both NK-lysin and all synthetic analogues killed Mycobacterium tuberculosis and K562 tumour cells, but did not display haemolytic activity [2].
• One NK-lysin peptide was active against Pseudomonas aeruginosa and Staphylococcus aureus, two organisms against which NK-lysin is inactive [2].
• All of the proteins compared were found to be potently active against Gram-positive bacteria, but only NK-lysin was equally efficient against Gram-negative bacteria [3].

High impact information on NKL

• We suggest that NK-lysin is a new effector molecule of cytotoxic T and NK cells [1].
• A 78 residue antimicrobial, basic peptide, NK-lysin, with three intrachain disulfide bonds was purified from pig small intestine and characterized [1].
• The 780 bp DNA sequence had a reading frame of 129 amino acids which corresponded to NK-lysin [1].
• Granulysin and NK-lysin are antimicrobial proteins found in the granules of human and swine cytotoxic lymphocytes [4].
• Two partial nucleotide sequences corresponding to the complete functional domain of granulysin and NK-lysin were amplified from bovine PBMC mRNA [4].

Biological context of NKL

• Preincubation of HIT T15 cells with NKL for 1 h or 24 h did not influence cell viability [5].

Anatomical context of NKL

• In the present study we show that NKL (1-100 nM) potently and reversibly stimulates insulin secretion in rat pancreatic islets and in the beta-cell line HIT T15 [5].
• Immunostaining showed NKL to be present in different types of lymphocytes [6].
• Untransfected LLC-PK1 cells were readily lysed by the NK cell lines NKL and NK-92, while LLC-PK1 cells expressing HLA-E SCT were almost completely protected [7].
• NK-lysin specific mRNA is also detectable in spleen, bone marrow and colon [6].
• Amoebapores, the pore-forming polypeptides of the protozoan parasite Entamoeba histolytica, and NK-lysin, an effector molecule of porcine NK (natural killer) and cytotoxic T cells, belong to the same protein family, the saposin-like proteins [3].

Associations of NKL with chemical compounds

• Saposins, which solubilize lipids and activate lysosomal hydrolases, the pore-forming amoebapores, and parts of acid sphingomyelinase and acyloxyacylhydrolase, also share 18-27% sequence identities with NK-lysin (and SP-B), including the six conserved half-cystine residues [8].

Other interactions of NKL

• An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B [8].
• Spleen antibacterial peptides: high levels of PR-39 and presence of two forms of NK-lysin [9].

References