PMID- 2753896
OWN - NLM
STAT- MEDLINE
DCOM- 19890907
LR  - 20210320
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 264
IP  - 22
DP  - 1989 Aug 5
TI  - On the biological occurrence and regulation of 1-acyl and 
      1-O-alkyl-diradylglycerols in human neutrophils. Selective destruction of diacyl 
      species using Rhizopus lipase.
PG  - 12977-82
AB  - The occurrence and regulation of 1-ether-linked diradylglycerol in human 
      neutrophils were investigated using a sensitive and practical analytical mass 
      method which distinguishes 1-O-alkyl- (EAG) versus 1-acyl (DAG) diglycerides. 
      After phosphorylation of diglycerides to the corresponding [32P]phosphatidic 
      acids using [gamma-32P]ATP and diglyceride kinase (Preiss, J., Loomis, C. R., 
      Bishop, W. R., Stein, R., Niedel, J. E., and Bell, R. M. (1986) J. Biol. Chem. 
      261, 8597-8600), lipase from Rhizopus arrhizus selectively degraded the 
      1-acyl-containing species (DAG), but the ether lipid (EAG) was resistant and was 
      identified and quantified after thin layer chromatography separation. By using 
      this method, unstimulated neutrophils were demonstrated to contain both DAG and 
      EAG (100-180 and 40-95 pmol/10(7) cells, respectively). The chemoattractant 
      formyl-methionyl-leucyl-phenylalanine (fMLP) caused a rapid (30 s) and transient 
      increase (1.6-fold) in DAG, but no increase in EAG. Opsonized zymosan produced a 
      6-8-fold sustained increase in DAG peaking at 2 to 3 min, but only a small 
      (1.7-fold) increase in EAG which was not seen until later times (10 min). Thus, 
      under these stimulation conditions, the major diglyceride was DAG. However, in 
      neutrophils "primed" with cytochalasin B or phorbol ester, 
      formyl-methionyl-leucyl-phenylalanine caused a significant increase in EAG. 
      Neutrophils pretreated with cytochalasin B and then stimulated by fMLP showed a 
      rapid (15-60 s) increase (more than 3-fold) in total diglycerides which was 
      sustained beyond 5 min. At the earliest time points (15-30 s), the increase was 
      due almost entirely to DAG (3-fold), but at 1 min and beyond, EAG comprised as 
      much as 40% of the total (up to a 5-fold increase in EAG). Neutrophils pretreated 
      with phorbol ester prior to fMLP stimulation showed a rapid (around 30 s) more 
      than 2-fold increase in both DAG and EAG. Thus, priming conditions (in particular 
      cytochalasin B) may alter either the access of phospholipase(s) C and/or D to 
      membrane phospholipids or may affect their activities, allowing hydrolysis of 
      1-O-alkyl-containing lipids to generate 1-O-alkyl-containing diglycerides.
FAU - Tyagi, S R
AU  - Tyagi SR
AD  - Department of Biochemistry, Emory University Medical School, Atlanta, Georgia 
      30322.
FAU - Burnham, D N
AU  - Burnham DN
FAU - Lambeth, J D
AU  - Lambeth JD
LA  - eng
GR  - AI22809/AI/NIAID NIH HHS/United States
GR  - CA46508/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Diglycerides)
RN  - 0 (Fungal Proteins)
RN  - 0 (Glycerides)
RN  - 0 (Opsonin Proteins)
RN  - 3CHI920QS7 (Cytochalasin B)
RN  - 59880-97-6 (N-Formylmethionine Leucyl-Phenylalanine)
RN  - 9010-72-4 (Zymosan)
RN  - EC 3.1.1.3 (Lipase)
SB  - IM
MH  - Cytochalasin B
MH  - Diglycerides/*metabolism
MH  - Fungal Proteins/pharmacology
MH  - Glycerides/*metabolism
MH  - Humans
MH  - Interphase/drug effects
MH  - Kinetics
MH  - Lipase/*pharmacology
MH  - N-Formylmethionine Leucyl-Phenylalanine/pharmacology
MH  - Neutrophils/drug effects/enzymology/*metabolism
MH  - Opsonin Proteins
MH  - Rhizopus/*enzymology
MH  - Zymosan
EDAT- 1989/08/05 00:00
MHDA- 1989/08/05 00:01
CRDT- 1989/08/05 00:00
PHST- 1989/08/05 00:00 [pubmed]
PHST- 1989/08/05 00:01 [medline]
PHST- 1989/08/05 00:00 [entrez]
AID - S0021-9258(18)51583-0 [pii]
PST - ppublish
SO  - J Biol Chem. 1989 Aug 5;264(22):12977-82.