Search results for HBD

Showing 15 results out of 16

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Protein (10 results from a total of 11)

HBD

Identifier: R-HSA-1008218
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: HBD: P02042
Identifier: R-HSA-975682
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: P60022
Identifier: R-HSA-1467188
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: DEFB104A: Q8WTQ1
Identifier: R-HSA-1467255
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: DEFB4A: O15263
Identifier: R-HSA-975669
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: DEFB103A: P81534
Identifier: R-HSA-1467258
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: Q8WTQ1
Identifier: R-HSA-1467261
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: O15263
Identifier: R-HSA-1467243
Species: Homo sapiens
Compartment: Golgi lumen
Primary external reference: UniProt: P81534
Identifier: R-HSA-975677
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: O15263
Identifier: R-HSA-975674
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: Q8WTQ1

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-9605273
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSG00000223609

Reaction (4 results from a total of 4)

Identifier: R-HSA-1471322
Species: Homo sapiens
Compartment: Golgi lumen, extracellular region
Beta defensin precursors are more simple in structure than those of alpha defensins, having a signal sequence, a short or absent propiece and the mature defensin sequence at the C-terminus. The signal sequence is cleaved off by a signal peptidase in the endoplasmic reticulum (Ganz 2003). Mature beta defensins 1, 2, 3, and 4 are secreted primarily by epithelial cells but are also produced by some immune cells such as monocytes, macrophages and dendritic cells (Duits et al. 2000, Ryan et al. 2003).
Identifier: R-HSA-1974676
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
Beta defensin 103 (hBD-3) can induce expression of the costimulatory molecules CD80, CD86 and CD40 on monocytes and myeloid dendritic cells in a Toll-like receptor (TLR)-dependent manner. Activation by hBD-3 is mediated by an interaction that requires TLRs 1 and 2 (Funderburg et al. 2007, 2011).
Identifier: R-HSA-1973968
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
human beta-defensin (hBD)4A and 103 interact with CCR2, a chemokine receptor expressed on monocytes, macrophages, and neutrophils.
Identifier: R-HSA-1467269
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
Binding and disruption of microbial membranes is widely believed to be the primary mechanism of action for beta-defensins. There is no direct evidence of this, but a growing number of studies support this model (Pazgier et al. 2006). Beta-defensins have antimicrobial properties that correlate with membrane permeabilization effects (Antcheva et al. 2004, Sahl et al. 2005, Yenugu et al. 2004). The sensitivity of microbes to beta-defensins correlates with the lipid composition of the membrane; more negatively-charged lipids correlate with larger beta-defensin 103-induced changes in membrane capacitance (Bohling et al. 2006). Beta-defensin-103 was observed to give rise to ionic currents in Xenopus membranes (Garcia et al. 2001) and cell wall perforation was observed in S. aureus when treated with HBD-3 (Harder et al. 2001). Two models explain how membrane disruption takes place. The 'pore model' postulates that beta-defenisns form transmembrane pores in a similar manner to alpha-defensins, while the 'carpet model' suggests that beta-defensins act as detergents, causing a less organised disruption. Beta-defensins have a structure that is topologically distinct from that of alpha-defensins, suggesting a different mode of dimerization and an electrostatic charge-based mechanism of membrane permeabilization rather than a mechanism based on formation of bilayer-spanning pores (Hoover et al. 2000).
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