PMID- 16529578
OWN - NLM
STAT- MEDLINE
DCOM- 20060620
LR  - 20181201
IS  - 0303-4569 (Print)
IS  - 0303-4569 (Linking)
VI  - 38
IP  - 2
DP  - 2006 Apr
TI  - Destabilization of the acrosome results in release of phospholipase A2 from human 
      spermatozoa and subsequent formation of lysophospholipids.
PG  - 69-75
AB  - Phospholipase A(2) controls the phospholipid composition in spermatozoal 
      membranes and is released from the acrosome of human spermatozoa. The 
      extracellular phospholipase A(2) activity of human spermatozoa was determined by 
      matrix-assisted laser desorption and ionization time-of-flight (MALDI-TOF) mass 
      spectrometry after destabilization of acrosome by the calcium-ionophore 
      calcimycin. MALDI-TOF mass spectrometry allowed the monitoring of changes in both 
      substrate and products of spermatozoal phospholipase A(2) (PLA(2)) without the 
      use of labelled phospholipids. The spermatozoal PLA(2) was characterized as a 
      secretory one (sPLA(2)). Secretory PLA(2) exhibited a high substrate specificity 
      for 1-palmitoyl-2-docosahexaenoyl-sn-glycero-3-phosphocholine (PDPC), the most 
      abundant spermatozoal phospholipid. A time- and cell number-dependent formation 
      of the lysophospholipid PDPC was observed following incubation of extracellular 
      medium of calcimycin-treated spermatozoa (CTS) with PDPC. Antibodies against 
      sPLA(2), specific inhibitors of sPLA(2) and Ca(2+)-chelators could inhibit its 
      generation. An antibody against lysophospholipase enhanced the lysoproduct 
      concentration in the extracellular medium of CTS containing sPLA(2) because 
      further metabolization of these products was blocked. The results demonstrated 
      that destabilization of the acrosome is able to induce a release of secretory 
      phospholipase A(2) from human spermatozoa with subsequent generation of 
      lysophosphocholine in the surrounding of spermatozoa.
FAU - Lessig, J
AU  - Lessig J
AD  - Institute of Medical Physics and Biophysics, Medical Faculty, University of 
      Leipzig, Leipzig, Germany.
FAU - Glander, H-J
AU  - Glander HJ
FAU - Schiller, J
AU  - Schiller J
FAU - Petkovic, M
AU  - Petkovic M
FAU - Paasch, U
AU  - Paasch U
FAU - Arnhold, J
AU  - Arnhold J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Andrologia
JT  - Andrologia
JID - 0423506
RN  - 0 (Lysophospholipids)
RN  - 37H9VM9WZL (Calcimycin)
RN  - EC 3.1.1.32 (Phospholipases A)
RN  - EC 3.1.1.4 (Phospholipases A2)
SB  - IM
MH  - Acrosome/*enzymology
MH  - Animals
MH  - Calcimycin
MH  - Humans
MH  - Lysophospholipids/*biosynthesis
MH  - Male
MH  - Mice
MH  - Phospholipases A/antagonists & inhibitors/*metabolism
MH  - Phospholipases A2
MH  - Spermatozoa
MH  - Substrate Specificity
MH  - Time Factors
EDAT- 2006/03/15 09:00
MHDA- 2006/06/21 09:00
CRDT- 2006/03/15 09:00
PHST- 2006/03/15 09:00 [pubmed]
PHST- 2006/06/21 09:00 [medline]
PHST- 2006/03/15 09:00 [entrez]
AID - AND713 [pii]
AID - 10.1111/j.1439-0272.2006.00713.x [doi]
PST - ppublish
SO  - Andrologia. 2006 Apr;38(2):69-75. doi: 10.1111/j.1439-0272.2006.00713.x.