PMID- 3305366
OWN - NLM
STAT- MEDLINE
DCOM- 19870930
LR  - 20210526
IS  - 0019-9567 (Print)
IS  - 1098-5522 (Electronic)
IS  - 0019-9567 (Linking)
VI  - 55
IP  - 9
DP  - 1987 Sep
TI  - Respiratory burst facilitates the digestion of Escherichia coli killed by 
      polymorphonuclear leukocytes.
PG  - 2142-7
AB  - We examined factors that may limit degradation of bacterial protein of 
      Escherichia coli S15 killed by polymorphonuclear leukocytes (PMN). Both human and 
      rabbit PMN degraded up to 40% of [14C]amino acid-labeled protein of ingested and 
      killed E. coli in 2 h as determined by loss of acid-precipitable radioactivity. 
      In contrast, equally bactericidal broken-PMN preparations or isolated granules 
      degraded only about 10% of bacterial protein regardless of pH. To determine 
      whether activation of the respiratory burst contributes to digestion, we compared 
      degradation by intact PMN in room air and under N2. Depletion of O2 by N2 
      flushing had no effect on the bactericidal activity of either human or rabbit PMN 
      but reduced degradation by approximately 50%. Protein degradation during 
      phagocytosis was also reduced in the presence of cyanide or azide, inhibitors of 
      myeloperoxidase (MPO). PMN of two patients with chronic granulomatous disease 
      ingested and killed E. coli S15 as well as did normal PMN but degraded bacterial 
      protein as did normal PMN incubated under N2. The low degradative activity of PMN 
      disrupted by sonication could be raised to nearly the level of intact PMN 
      incubated in room air by preincubation of the PMN with 10(-7) M 
      formyl-methionyl-leucyl-phenylalanine (fMLP) before sonication and by 
      pretreatment of E. coli with MPO. Depletion of O2 or chloride during these 
      preincubations with formyl-methionyl-leucyl-phenylalanine respectively, virtually 
      abolished and markedly diminished stimulation of bacterial protein degradation. 
      We conclude that enhanced MPO-mediated O2 metabolism of intact PMN plays a role 
      in the digestion of killed E. coli.
FAU - Weiss, J
AU  - Weiss J
FAU - Kao, L
AU  - Kao L
FAU - Victor, M
AU  - Victor M
FAU - Elsbach, P
AU  - Elsbach P
LA  - eng
GR  - AI 18571/AI/NIAID NIH HHS/United States
GR  - AM 05472/AM/NIADDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Infect Immun
JT  - Infection and immunity
JID - 0246127
RN  - 0 (Azides)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Cyanides)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Animals
MH  - Azides/pharmacology
MH  - Bacterial Proteins/metabolism
MH  - *Blood Bactericidal Activity/drug effects
MH  - Cell-Free System
MH  - Cyanides/pharmacology
MH  - Escherichia coli/*immunology/metabolism
MH  - Granulomatous Disease, Chronic/physiopathology
MH  - Humans
MH  - Neutrophils/*physiology
MH  - Oxygen/metabolism
MH  - Oxygen Consumption
MH  - Rabbits
PMC - PMC260670
EDAT- 1987/09/01 00:00
MHDA- 1987/09/01 00:01
PMCR- 1987/09/01
CRDT- 1987/09/01 00:00
PHST- 1987/09/01 00:00 [pubmed]
PHST- 1987/09/01 00:01 [medline]
PHST- 1987/09/01 00:00 [entrez]
PHST- 1987/09/01 00:00 [pmc-release]
AID - 10.1128/iai.55.9.2142-2147.1987 [doi]
PST - ppublish
SO  - Infect Immun. 1987 Sep;55(9):2142-7. doi: 10.1128/iai.55.9.2142-2147.1987.