NK-lysin, structure and function of a novel effector molecule of porcine T and NK cells

Andersson, Mats; Gunne, Hans; Agerberth, Birgitta; Boman, Anita; Bergman, Tomas; Olsson, Berit; Dagerlind, Å.; Wigzell, Hans; Boman, Hans G.; Guðmundsson, Guðmundur H.

doi:10.1016/s0165-2427(96)05677-2

Cited by 56 publications

(40 citation statements)

References 10 publications

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“…As seen in Fig. 1 the six halfcystine residues, at positions 8, 11, 35, 46, 71 and 77 (numbering according to the SP-B sequence), are strictly conserved and the disulphide bridges formed between these half-cystines are identical in NK-lysin [1] and SP-B [8,9], i.e. the half-cystines are linked in the order 1-6, 2-5, and 3~,.…”

Section: Nk-lysin Is Homologous To Sp-b and Belongs To The Saposinlikmentioning

confidence: 91%

“…NK-lysin was purified from porcine upper small intestine, via a concentrate of thermostable intestinal peptides [1], and SP-B was isolated from porcine pulmonary phospholipids by repeated chromatography on Sephadex LH-60 in chloroform/methanol/0.1 M HC1 [17].…”

Section: Polypeptide Isolation and Analysmentioning

confidence: 99%

“…These polypeptides exhibit 18-27% pairwise residue identities. NKG5 and 519, two proteins postulated from cDNA sequences from activated human T-and natural killer cells [22,23], show high amino acid sequence similarities to NK-lysin [1] but are not included in the comparisons now since they have not been isolated and their functions are unknown. For the same reasons the two SP-B-like repeats in the proSP-B sequence [14] are also excluded.…”

Section: Nk-lysin Is Homologous To Sp-b and Belongs To The Saposinlikmentioning

confidence: 99%

“…NK-lysin is a 78-residue polypeptide with three intrachain disulphide bridges [1]. It was recently isolated from porcine small intestine and found to possess antimicrobial and tumourolytic properties (named NK-lysin from peptide with possible Natural Killer cell origin and lytic properties).…”

Section: Introductionmentioning

confidence: 99%

“…Many of those highlight the importance of charge and secondary structure, such as for example illustrated by PR-39 that contains 26% Arg and 49% Pro [3] and forms poly-proline helices [4]. NK-lysin is homologous to postulated peptides from human lymphocytes, suggesting immunoregulatory properties in common [1]. Likewise, several structurally different polypeptides are important in the regulation of the activity of pulmonary surfactant [5,6].…”

Section: Introductionmentioning

confidence: 99%

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An amphipathic helical motif common to tumourolytic polypeptide NK‐lysin and pulmonary surfactant polypeptide SP‐B

et al. 1995

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The tumour-lysing and antimicrobial polypeptide NKlysin and the pulmonary surfactant-associated polypeptide SP-B exhibit 24% residue identities (49% similarities), including six half-cystine residues in the same disulphide bonding pattern, and similar far-UV circular dichroism spectra corresponding to 45-55% c~-helix and 20-25%/]-sheet structures. From this, we conclude that the conformations of NK-lysin and SP-B are similar. In contrast, the functional properties of the two proteins are dissimilar: SP-B does not exhibit antibacterial activity and NKlysin does not significantly effect phospholipid spreading at an air/water interface. 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. The inclusion of NK-lysin extends the family of saposin-like polypeptides, all members of which appear to interact with lipids. Strictly conserved structural features with implications for helix topology and lipid interactions are observed.Key words: Lipid-binding polypeptide; Secondary structure; Saposin-like module linking two polypeptides into a homodimer [8][9][10]. SP-B is considered important for alveolar stability at low lung volumes by contributing to the reduction of the alveolar surface tension [5,6]. However, the precise function of SP-B is not known and several different mechanisms of action have been suggested (cf. [11][12][13]). Sequence-wise, SP-B, two SP-B-like repeats in the SP-B precursor (absent in alveolar surfactant), and saposins which solubilize sphingolipids and activate lysosomal hydrolases, constitute a family of distantly related proteins [14]. In addition, a pore-forming peptide (amoebapore A) from Entamoeba histolytica [15], acid sphingomyelinase and acyloxyacyl hydrolase [16] belong to this 'saposin-like' family. These 80-odd residue modules exhibit about 20% pairwise residue identities including six conserved half-cystines [16].We now notice that the disulphide pattern of NK-lysin is identical to the intrachain disulphide pattern of SP-B, and that NK-lysin belongs to the saposin-like family. Furthermore, the overall secondary structure of NK-lysin and SP-B are similar. From all this and the pattern of strictly conserved residues within the saposin family, a possible four-helix topology is proposed which is compatible with lipid-interacting properties of these proteins.

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Section: Nk-lysin Is Homologous To Sp-b and Belongs To The Saposinlikmentioning

confidence: 91%

Section: Polypeptide Isolation and Analysmentioning

confidence: 99%

Section: Nk-lysin Is Homologous To Sp-b and Belongs To The Saposinlikmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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An amphipathic helical motif common to tumourolytic polypeptide NK‐lysin and pulmonary surfactant polypeptide SP‐B

et al. 1995

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Patterns of gene expression in the developing chick thymus

Cui

Sofer

Cloud

et al. 2004

Developmental Dynamics

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Gene expression in thymic T cells during late embryogenesis and early growth in chicks was examined using cDNA microarrays. Gene expression patterns were profiled into nine clusters by using self-organizing maps (SOM) clustering analysis. The expression patterns for a set of genes confirmed current information on the development of immune response. Expression of cell surface markers (MHC class I ␣ chain, MHC class II associated invariant chain, CD8 ␤ chain, CD18, and ␤2-microglobulin), and genes involved in the innate immune response (NK lysin-like) increased with age, and these patterns were consistent with an increase in the immune responsiveness of the young chick. The expression of cytokine receptor common gamma chain (␥c), death receptor-3 (DR3), and TCR ␣ chain increased up to 1 day of age and then decreased. DR3 could play a role in the apoptosis during T-cell maturation, while the differential expression of TCR genes could reflect regulation of the rearrangement of TCR genes and TCR-mediated signal transduction during T cell development. Three genes coding for previously uncharacterized proteins are included in the clusters. These gene expression profiling studies provide background information on the developing chick immune system and provide preliminary functional information on unknown proteins.

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An Expressed Sequence Tag Database of T-Cell-Enriched Activated Chicken Splenocytes: Sequence Analysis of 5251 Clones

et al. 2000

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NK-lysin, structure and function of a novel effector molecule of porcine T and NK cells

Cited by 56 publications

References 10 publications

An amphipathic helical motif common to tumourolytic polypeptide NK‐lysin and pulmonary surfactant polypeptide SP‐B

An amphipathic helical motif common to tumourolytic polypeptide NK‐lysin and pulmonary surfactant polypeptide SP‐B

Patterns of gene expression in the developing chick thymus

An Expressed Sequence Tag Database of T-Cell-Enriched Activated Chicken Splenocytes: Sequence Analysis of 5251 Clones

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