Immunohistochemical localization of phospholipase A2 isoforms in human myometrium during pregnancy and parturition

Skannal, Deborah G.; Eis, Annie; Brockman, Diane E.; Siddiqi, Tariq A.; Myatt, Leslie

doi:10.1016/s0002-9378(97)70614-8

Cited by 28 publications

(13 citation statements)

References 12 publications

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“…The PLA2 isoforms include the secretory (also called synovial-type) group II extracellular 14 kD isoform (sPLA2) and the group IV cytosolic 85-110 kD isoforms (cPLA2) [6,21,22].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…The secretory phospholipase (sPLA2) is assumed to be active only in the extracellular space in the presence of millimolar concentration of Ca 2+ , whereas cytosolic phospholipase (cPLA2) is the enzyme responsible for intracellular-signal-mediated release of arachidonic acid, which is regulated by intracellular Ca 2+ concentration and phosphorylation [2,19,21,22].…”

Section: Introductionmentioning

confidence: 99%

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mentioning

confidence: 99%

“…These enzymes catalyze the release of arachidonic acid, which is then converted, for instance, to prostaglandins by the cyclo-oxygenases (COX-1 and COX-2). Thus arachidonic acid mobilization seems to be dependent on both types of PLA2 [6,16,19,21,22].Abstract Phospholipase A 2 (PLA2) has been suggested to be present in herniated disc tissue and it could possibly be involved in sciatica/ discogenic back pain mechanisms. In the present study the occurrence of two different phospholipase A 2 enzymes, (1) low molecular weight (14 kDa) group II synovial-type (sPLA2) and (2) high molecular weight (85 kDa) group IV cytosolic (cPLA2), were compared.…”

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confidence: 99%

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Comparative immunohistochemical study of group II (synovial-type) and group IV (cytosolic) phospholipases A 2 in disc prolapse tissue

Habtemariam

Grönblad

Virri

et al. 1998

European Spine Journal

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IntroductionThe PLA2 isoforms include the secretory (also called synovial-type) group II extracellular 14 kD isoform (sPLA2) and the group IV cytosolic 85-110 kD isoforms (cPLA2) [6,21,22].It has been suggested that both types of PLA2 (sPLA2 and cPLA2) are implicated in inflammation. These enzymes catalyze the release of arachidonic acid, which is then converted, for instance, to prostaglandins by the cyclo-oxygenases (COX-1 and COX-2). Thus arachidonic acid mobilization seems to be dependent on both types of PLA2 [6,16,19,21,22].Abstract Phospholipase A 2 (PLA2) has been suggested to be present in herniated disc tissue and it could possibly be involved in sciatica/ discogenic back pain mechanisms. In the present study the occurrence of two different phospholipase A 2 enzymes, (1) low molecular weight (14 kDa) group II synovial-type (sPLA2) and (2) high molecular weight (85 kDa) group IV cytosolic (cPLA2), were compared. Fifty-three disc prolapses obtained at disc operations were analyzed by immunohistochemistry, using anti-human monoclonal antibodies to sPLA2 and cPLA2, respectively. Only cell-associated (disc cells, hyaline cartilage chondrocytes) sPLA2 and cPLA2 immunoreactivity could be observed. The results showed that sPLA2 was more common (25/53, 47%) than cPLA2 (13/53, 25%). sPLA2 and cPLA2 were simultaneously present in 13 of 53 samples (25%). However, both PLA2 enzymes were predominantly present in hyaline cartilage cells (sPLA2: 16/53, cPLA2: 5/53), being less commonly observed in disc cells (sPLA2: 6/53, cPLA2: 3/53). In addition, three samples for sPLA2 and two samples for cPLA2 exhibited immunoreactivity in cartilage and disc cells simultaneously. sPLA2 was observed in no other locations, but in 3 of 53 samples cPLA2 was observed more diffusely in areas of granulation tissue, possibly in macrophages. No gender-or age-related dependence for either type of PLA2 enzyme immunoreactivity could be observed. Neither did their occurrence relate to clinical data such as straight leg raising or neurological deficit. The results do not support a major role for either of the two disc-cell-associated PLA2s in disc pathophysiology. For both enzymes, the major pool appears to reside in cartilage tissue cells, presumably in dislodged end-plate fragments. Disc cells are apparently unlikely candidates for major PLA2 storage.

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“…The PLA2 isoforms include the secretory (also called synovial-type) group II extracellular 14 kD isoform (sPLA2) and the group IV cytosolic 85-110 kD isoforms (cPLA2) [6,21,22].…”

Section: Introductionmentioning

confidence: 99%