Bactericidal Permeability Increasing Protein Cap57

From Anvita Health Wiki

Contents 1 Function 2 Structure 3 Compartment 4 Expression 5 More General Terms 6 Internet Database 7 References

Function

• cytotoxic action of BPI is limited to many species of Gram-negative bacteria specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope
• has antibacterial activity against the P. aeruginosa, this activity is inhibited by LPS from P. aeruginosa
• during phagocytosis & degranulation, proteases may be released & activated & cleave BPI at the junction of the N- & C-terminal portions of the molecule, providing controlled release of the N-terminal antibacterial fragment when bacteria are ingested

Structure

• monomer. homodimer; disulfide-linked
• the N-terminal region may be exposed to the interior of the granule, whereas the C-terminal portion may be embedded in the membrane
• belongs to the BPI/ LBP/ plunc superfamily, BPI/ LBP family
• contains 2 LRR repeats ( leucine-rich repeats)

Compartment

• secreted
• cytoplasmic granule membrane
• membrane-associated in polymorphonuclear leukocyte ( PMN) granules

Expression

• restricted to cells of the myeloid series

More General Terms

• secreted protein
• membrane protein
• leucine-rich repeat-containing protein (LRRC)
• glycoprotein

Internet Database

UniProt: [1]
Entrez gene: 671
Kegg: [2]
OMIM: 109195
Prosite: [3]

References

UniProt [4]

bactericidal permeability-increasing protein; BPI; CAP 57 (BPI)