Cellular Localization of Group IIA Phospholipase A<sub>2</sub> in Rats

Yoshikawa, Toshiyuki; Naruse, Satoru; Kitagawa, Motoji; Ishiguro, Hiroshi; Nagahama, Masato; Yasuda, Etsuko; Semba, Reiji; Tanaka, Minoru; Nomura, Kohji; Hayakawa, Tetsuo

doi:10.1177/002215540104900611

Cited by 13 publications

(6 citation statements)

References 24 publications

(34 reference statements)

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“…Relative changes in protein expression were estimated from the mean pixel density using Scion Image program (Scion Corporation), normalized to β-actin, and calculated as ipsilateral/contralateral ratios. Rat platelets were used as a source of sPLA 2 IIA standard (Yoshikawa et al, 2001). …”

Section: Western Blots For Spla 2 Iiamentioning

confidence: 99%

RETRACTED: Secretory phospholipase A2 IIA is up-regulated by TNF-α and IL-1α/β after transient focal cerebral ischemia in rat

Adibhatla

Hatcher

2007

Brain Research

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Cerebral ischemia initiates an inflammatory response in the brain that is associated with induction of a variety of cytokines, including tumor necrosis factor-α (TNF-α) and interleukin-1α/β (IL-1α/β) that contributes to stroke injury. Transient middle cerebral artery occlusion (tMCAO) in spontaneously hypertensive rat (SHR) resulted in significant increases in TNF-α and IL-1β levels. We have previously demonstrated up-regulation of secretory phospholipase A 2 IIA (sPLA 2 IIA) mRNA and protein expression, increased PLA 2 activity, and loss of phosphatidylcholine after 1 hr tMCAO and 24 hr reperfusion in SHR. Treatment with TNF-α antibody or IL-1 receptor antagonist significantly attenuated infarction volume, sPLA 2 IIA protein expression, PLA 2 activity and significantly restored phosphatidylcholine levels after tMCAO. This suggests that cytokine induction up-regulates sPLA 2 IIA protein expression, resulting in altered lipid metabolism that contributes to stroke injury.

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Section: Western Blots For Spla 2 Iiamentioning

confidence: 99%

RETRACTED: Secretory phospholipase A2 IIA is up-regulated by TNF-α and IL-1α/β after transient focal cerebral ischemia in rat

Adibhatla

Hatcher

2007

Brain Research

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“…The protein‐coding regions of the PLA2 genes of French vipers most probably evolved in an accelerated Darwinian manner, as reported for the PLA2 genes expressed in Crotalinae and V. am. ammodytes venom [2,3,5,7,8].…”

Section: Conservation Of the Nucleotide Sequencementioning

confidence: 99%

“…Those belonging to group II have six to eight disulfide bonds and a C‐terminal extension not present in group I venom PLA2s [1]. They are found in the venoms of Crotalinae and Viperinae snakes and in human platelets, liver and spleen [2,3]. Snake venoms contain a large number of PLA2 isoenzymes which differ in neurotoxicity, myotoxicity, cardiotoxicity, anticoagulation and edema‐inducing properties [2].…”

mentioning

confidence: 99%

Sequences and structural organization of phospholipase A₂ genes from Vipera aspis aspis, V. aspis zinnikeri and Vipera berus berus venom

Guillemin

Bouchier

Garrigues

et al. 2003

European Journal of Biochemistry

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We used a PCR-based method to determine the genomic DNA sequences encoding phospholipases A 2 (PLA2s) from the venoms of Vipera aspis aspis (V. a. aspis), Vipera aspis zinnikeri (V. a. zinnikeri), Vipera berus berus (V. b. berus) and a neurotoxic V. a. aspis snake (neurotoxic V. a. aspis) from a population responsible for unusual neurotoxic envenomations in south-east France. We sequenced five groups of genes, each corresponding to a different PLA2. The genes encoding the A and B chains of vaspin from the neurotoxic V. a. aspis, PLA2-I from V. a. zinnikeri, and the anticoagulant PLA2 from V. b. berus are described here. Single nucleotide differences leading to amino-acid substitutions were observed both between genes encoding the same PLA2 and between genes encoding different PLA2s. These differences were clustered in exons 3 and 5, potentially altering the biological activities of PLA2. The distribution and characteristics of the PLA2 genes differed according to the species or subspecies. We characterized for the first time genes encoding neurotoxins from the V. a. aspis and V. b. berus snakes of central France. Genes encoding ammodytins I1 and I2, described previously in Vipera ammodytes ammodytes (V. am. ammodytes), were also present in V. a. aspis and V. b. berus. Three different ammodytin I1 gene sequences were characterized: one from V. b. berus, the second from V. a. aspis, V. a. zinnikeri and the neurotoxic V. a. aspis, and the third from the neurotoxic V. a. aspis. This third sequence was identical with the reported sequence of the V. am. ammodytes ammodytin I1 gene. Genes encoding monomeric neurotoxins of V. am. ammodytes venom, ammodytoxins A, B and C, and the Bov-B LINE retroposon, a phylogenetic marker found in V. am. ammodytes genome, were identified in the genome of the neurotoxic V. a. aspis. These results suggest that the population of neurotoxic V. a. aspis snakes from south-east France may have resulted from interbreeding between V. a. aspis and V. am. ammodytes.

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“…The group IIA sPLA 2 is one of the most extensively studied PLA2 classes, expressed in multiple organs of rats in inflammatory diseases [38]. The adrenal tissues were fixed in 10% (w/v) buffered formalin and 4-μm sections were prepared from paraffin-embedded tissues.…”

Section: Histopathologic Analysismentioning

confidence: 99%

Changes of Inflammation and Apoptosis in Adrenal Gland After Experimental Injury in Rats with Acute Necrotizing Pancreatitis

Wang

et al. 2010

Inflammation

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We hypothesize that adrenal insufficiency in acute necrotizing pancreatitis (ANP) is attributable to hemorrhagic inflammation, necrosis, and apoptosis of the adrenal cortex. Arguments to support this view are presented in the study that investigated morphological and functional changes of adrenal and the distinct roles of inflammatory mediator secretory phospholipase A(2) (sPLA(2)) and apoptosis-related genes Bax and Bcl-2 played in acute adrenal injury in ANP. After ANP model was induced, pancreatic histology, serum amylase, sPLA(2), and corticosterone were analyzed. The adrenal morphology, apoptotic cells by TUNEL assay, and ultrastructures were observed. sPLA(2)-IIA and Bcl-2 and Bax expressions were detected by immunohistochemistry. Histopathologic grading of adrenal was higher in ANP group than in controls. Serum corticosterone was stimulated to maximal level at 3 h, then dropped to the bottom at 24 h (P<0.05). Apoptotic index, sPLA2-IIA, and Bax expression were increased steeply after pancreatitis, and the Bax/Bcl-2 ratio was elevated gradually (P<0.05). Sustained decrease in serum corticosterone level following adrenal injury during ANP appears to be, in part, due to the crucial roles of inflammation and apoptosis in adrenal cortex. These findings could suggest that sPLA2, Bax, and Bcl-2 may be involved in the course of adrenal injury after ANP.

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Cellular Localization of Group IIA Phospholipase A₂ in Rats

Cited by 13 publications

References 24 publications

RETRACTED: Secretory phospholipase A2 IIA is up-regulated by TNF-α and IL-1α/β after transient focal cerebral ischemia in rat

RETRACTED: Secretory phospholipase A2 IIA is up-regulated by TNF-α and IL-1α/β after transient focal cerebral ischemia in rat

Sequences and structural organization of phospholipase A₂ genes from Vipera aspis aspis, V. aspis zinnikeri and Vipera berus berus venom

Changes of Inflammation and Apoptosis in Adrenal Gland After Experimental Injury in Rats with Acute Necrotizing Pancreatitis

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Cellular Localization of Group IIA Phospholipase A2 in Rats

Cited by 13 publications

References 24 publications

RETRACTED: Secretory phospholipase A2 IIA is up-regulated by TNF-α and IL-1α/β after transient focal cerebral ischemia in rat

RETRACTED: Secretory phospholipase A2 IIA is up-regulated by TNF-α and IL-1α/β after transient focal cerebral ischemia in rat

Sequences and structural organization of phospholipase A2 genes from Vipera aspis aspis, V. aspis zinnikeri and Vipera berus berus venom

Changes of Inflammation and Apoptosis in Adrenal Gland After Experimental Injury in Rats with Acute Necrotizing Pancreatitis

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Product

Resources

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Cellular Localization of Group IIA Phospholipase A₂ in Rats

Sequences and structural organization of phospholipase A₂ genes from Vipera aspis aspis, V. aspis zinnikeri and Vipera berus berus venom