ライフサイエンスコーパス: cryptdin

1 intestinal anti-microbial peptides, known as cryptdins.

2 l peptides including alpha-defensins, termed cryptdins.

3 hospholipase A2, and alpha-defensins, termed cryptdins.

4 In contrast, cryptdins 1, 4, 5, and 6 lacked this activity, demonstra

5 Mouse cryptdins 1-6 and recombinant human Paneth cell alpha-de

6 Using an antibody specific for mouse cryptdin-1, -2, -3, and -6, immunogold-localization stud

7 ryptdin-2, -4, and -6 as well as variants of cryptdin-1, -4, and -6 that have N termini truncated by

8 When administered apically, mouse cryptdins 2 and 3 can reversibly stimulate human T-84 in

9 Thus cryptdins 2 and 3 can selectively permeabilize the apica

10 Of the six peptides tested, cryptdins 2 and 3 stimulated Cl- secretion from polarize

11 These data define the capability of cryptdins 2 and 3 to function as novel intestinal secret

12 Nucleotides -6500 to +34 of the mouse cryptdin-2 gene (CR2) were used to express an attenuated

13 riptional regulatory elements from the mouse cryptdin-2 gene (CR2-TAg).

14 ce that utilize regulatory elements from the cryptdin-2 gene (Defcr2) to express simian virus 40 larg

15 Nucleotides -6500 to +34 of the mouse cryptdin-2 gene were used to direct expression of simian

16 ed peptides identical to the tissue forms of cryptdin-2, -4, and -6 as well as variants of cryptdin-1

17 ranes of the human intestinal cell line T84, cryptdin 3 (Cr3) induces secretion of the proinflammator

18 On the other hand, cryptdin 3 elicited a secretory response that correlated

19 efensins, MBD-2, MBD-3, and alpha-defensins (cryptdins)-3 and -17, consistent with a gene cluster.

20 ays inhibited the bactericidal activities of cryptdin-3 and -4 in trans, suggesting possible cytoprot

21 nsins, including mouse Paneth cell defensins cryptdin-3 and cryptdin-4, human neutrophil defensin HNP

22 residues in mouse Paneth cell alpha-defensin cryptdin 4 (Crp4) and rhesus myeloid alpha-defensin 4 (R

23 of the transcriptional initiation site, the cryptdin 4 gene contains a repeated 130-bp element that

24 latory role in the positional specificity of cryptdin 4 gene expression.

25 f the known Paneth cell alpha-defensins, the cryptdin 4 gene is unique, because it is inactive in the

26 Structurally, the cryptdin 4 gene resembles other Paneth cell alpha-defens

27 Every independent cryptdin 4 genomic clone examined carries the repeated e

28 Consistent with the pattern of cryptdin 4 mRNA distribution along the length of the gut

29 istribution along the length of the gut, the cryptdin 4 peptide was not detected in duodenum.

30 xpression of antimicrobial (defensin-related cryptdin 4, defensin-related cryptdin 5, RegIIIgamma) an

31 channels in mammalian cell membranes because cryptdin 4, which does not form pores in T84 cells, does

32 With a cryptdin 4-specific antibody, immunohistochemical staini

33 In mouse cryptdin-4 (Crp4) and rhesus myeloid alpha-defensin-4 (R

34 Cryptdin-4 (Crp4) is an alpha-defensin expressed in Pane

35 fensins into the small intestinal lumen, and cryptdin-4 (Crp4) is the most bactericidal of the mouse

36 To investigate mechanisms of cryptdin-4 (Crp4) peptide interactions with membrane bil

37 alpha-defensin bactericidal activity, mouse cryptdin-4 (Crp4) tertiary structure was disrupted by pa

38 The antimicrobial peptide cryptdin-4 (Crp4), a member of the alpha-defensin family

39 ved peptide P2 and the murine alpha-defensin cryptdin-4 (Crp4).

40 The microbicidal activities of recombinant cryptdin-4 and (des-Gly)-cryptdin-4 peptides against E.

41 to killing by the host antimicrobial peptide cryptdin-4 but decreases bacterial transmigration across

42 The mouse cryptdin-4 gene is expressed with positional specificity

43 N-terminal Gly residue or the length of the cryptdin-4 N terminus are determinants of microbicidal a

44 ties of recombinant cryptdin-4 and (des-Gly)-cryptdin-4 peptides against E. coli, and S. typhimurium

45 eu), (des-Leu-Arg)-cryptdin-6, and (des-Gly)-cryptdin-4 peptides were markedly less active.

46 g mouse Paneth cell defensins cryptdin-3 and cryptdin-4, human neutrophil defensin HNP-1, and human P

47 a manner different from mouse alpha-defensin cryptdin-4.

48 ited diminished intestinal Paneth cell alpha-cryptdin 5 and 7 expression.

49 efensin-related cryptdin 4, defensin-related cryptdin 5, RegIIIgamma) and antiapoptotic, prorestituti

50 -terminal-truncated (des-Leu), (des-Leu-Arg)-cryptdin-6, and (des-Gly)-cryptdin-4 peptides were marke

51 ccurs within minutes and alpha-defensins, or cryptdins, account for 70% of the released bactericidal

52 e, which produce procryptdins but not mature cryptdins (alpha-defensins) in the intestine, were more

53 ilysin-deficient (MAT-/-) mice lacked mature cryptdins and accumulated precursor molecules.

54 l tract, and expression of Paneth cell alpha-cryptdins and beta-defensins was determined by real-time

55 taining bactericidal proteins like defensins/cryptdins and lysozyme, PCs regulate the microbiome of t

56 Thus, cryptdins and varied Paneth cell secretory products seem

57 intestinal crypt release enteric defensins (cryptdins) apically into the lumen.

58 Cryptdins are coded by separate, two-exon genes that are

59 ogold-localization studies demonstrated that cryptdins are constituents of mouse Paneth cell secretor

60 Because cryptdins are homologs of molecules known to form anion

61 ecific antimicrobial alpha-defensins, termed cryptdins, are secreted into the intestinal lumen by mou

62 secrete microbicidal alpha-defensins, termed cryptdins, as components of enteric innate immunity.

63 The peptides comigrated with cryptdin control peptides in acid-urea-PAGE and SDS-PAGE

64 man alpha-defensin 5, mouse alpha-defensins, cryptdins (Crp) 3 and 4, and rhesus macaque myeloid alph

65 Enteric alpha-defensins, termed cryptdins (Crps) in mice, are highly abundant in Paneth

66 secrete microbicidal alpha-defensins, termed cryptdins (Crps) in mice, as mediators of innate immunit

67 mouse Paneth cells, alpha-defensins, termed cryptdins (Crps), are activated by matrix metalloprotein

68 f mature Paneth cell alpha-defensins, termed cryptdins (Crps), requires proteolytic activation of ina

69 Alpha-defensins (or Cryptdins [Crps]) are a group of antimicrobial peptides

70 icrobial products, including peptides termed cryptdins, for crypt defensins.

71 along the longitudinal intestinal axis, and cryptdin genes are active in the intestinal epithelium p

72 the differential expression of certain mouse cryptdin genes provides markers for studies of crypt ont

73 Paneth cells secrete antimicrobial peptides (cryptdins), growth factors, as well as two gene products

74 ella typhimurium phoP(-) mutant, full-length cryptdins had the same in vitro antibacterial activities

75 es the expression of alpha-defensins (called cryptdins in mice) and lysozyme.

76 peptides, including alpha-defensins, termed cryptdins in mice.

77 matrilysin colocalized with alpha-defensins (cryptdins) in Paneth cell granules, and in vitro it clea

78 The isolated luminal cryptdins included peptides identical to the tissue form

79 vity of mouse Paneth cell alphadefensins, or cryptdins, is dependent on processing of cryptdin precur

80 The cryptdin isoforms 2 and 3 also can form anion-conductive

81 rent defensin mRNAs, but in mice at least 19 cryptdin isoforms are predicted from cDNA sequencing dat

82 stine and the most bactericidal of the known cryptdin isoforms.

83 Cryptdins kill microbes by forming pores in their limiti

84 These results show that selective cryptdins may amplify their roles in innate immunity by

85 Because cryptdins mediate innate immunity in the hostile environ

86 etween Ser(43) and Val(44) as well as at the cryptdin peptide N terminus between Ser(58) and Leu(59).

87 Several cryptdin peptides have been purified from rinses of adul

88 Cryptdin peptides that differ only by single amino acid

89 o-localized precursor prosegments and mature cryptdin peptides to Paneth cell granules, providing evi

90 or cryptdins, is dependent on processing of cryptdin precursors (pro-Crps) by matrix metalloproteina

91 and in vitro it cleaved the pro segment from cryptdin precursors.

92 we report on the intracellular processing of cryptdin proforms in mouse Paneth cells.

93 d both as bactericidal activity and secreted cryptdin protein, but the inactive analog, TRAM-7, did n

94 Cryptdin-related sequence peptides form a subfamily of a

95 The bactericidal activity of cryptdins requires proteolytic activation of precursors

96 tericidal activity of mouse alpha-defensins (cryptdins) requires proteolytic activation of inactive p

97 c acid, lipid A and muramyl dipeptide elicit cryptdin secretion.

98 duction of IL-8 secretion is specific to the cryptdins that form channels in mammalian cell membranes

99 In contrast to cryptdins, the mouse intestinal defensins, rHD-5 is acti

100 Levels of activated cryptdins were normal in small bowel of germ-free mice a