Effect of pancreatic type phospholipase A<sub>2</sub> on isolated porcine cerebral arteries via its specific binding sites

Nakajima, Miki; Hanasaki, Kohji; Ueda, Motohiko; Arita, Hitoshi

doi:10.1016/0014-5793(92)80785-f

Cited by 54 publications

(26 citation statements)

References 11 publications

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“…[35][36][37] The correlation between sPLA 2 -IIA levels and disease status has led to the development of pharmacological agents that are capable of inhibiting sPLA 2 -IIA and possibly the activities of other sPLA 2 , which would be expected to be beneficial for the mitigation of disease. As a result of our ongoing efforts to develop new sPLA 2 inhibitors from natural products using an activity-guided isolation procedure, we isolated a new human sPLA 2 -IIA and -V inhibitor, papyriflavonol A, from B. papyrifera.…”

Section: Discussionmentioning

confidence: 99%

Papyriflavonol A from Broussonetia papyrifera Inhibits the Passive Cutaneous Anaphylaxis Reaction and Has a Secretory Phospholipase A2-Inhibitory Activity.

Kwak¹,

Moon

Lin

et al. 2003

Biological & Pharmaceutical Bulletin

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Papyriflavonol A, a new prenylated flavonol isolated from Broussonetia papyrifera, selectively inhibits recombinant human secretory phospholipase A 2 s (sPLA 2 s). Papyriflavonol A was found to inhibit human group IIA and V sPLA 2 s potently and irreversibly in a dose-dependent manner, with respective IC 50 values of 3.9 and 4.5 m mM. The inhibitory effects of papyriflavonol A against bovine group IB (IC 50 of 76.9 m mM) and the human group X (IC 50 of 225 m mM) sPLA 2 s were weaker than those against human group IIA and V sPLA 2 s, and human group IIF sPLA 2 was not inhibited. In addition, papyriflavonol A potently inhibited the stimulus-induced production of leukotriene C 4 with an IC 50 value of approximately 0.64 m mM in mouse bone marrow-derived mast cells. In addition, papyriflavonol A significantly reduced IgE-dependent passive cutaneous anaphylaxis in rats. These results indicate that papyriflavonol A provides a basis for novel types of antiinflammatory drugs.

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Section: Discussionmentioning

confidence: 99%

Papyriflavonol A from Broussonetia papyrifera Inhibits the Passive Cutaneous Anaphylaxis Reaction and Has a Secretory Phospholipase A2-Inhibitory Activity.

Kwak¹,

Moon

Lin

et al. 2003

Biological & Pharmaceutical Bulletin

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“…We have previously reported that sPLA 2 -IB can elicit various biological responses possibly via PLA 2 R binding, such as proliferation and chemokinetic migration of vascular smooth muscle cells and potent vasoactive actions in cerebral arteries (17,38). In addition, we have recently demonstrated that sPLA 2 -X elicits marked release of arachidonic acid leading to lipid mediator productions in various cell types, including monocytes/ macrophages (15,16,39).…”

Section: Discussionmentioning

confidence: 99%

Identification of a Soluble Form Phospholipase A2Receptor as a Circulating Endogenous Inhibitor for Secretory Phospholipase A2

Higashino

Yokota

Ono

et al. 2002

Journal of Biological Chemistry

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Venomous snakes have various types of phospholipase A 2 inhibitory proteins (PLIs) in their circulatory system to protect them from attack by their own phospholipase A 2 s (PLA 2 s). Here we show the first evidence for the existence of circulating PLI against secretory PLA 2 s (sPLA 2 s) in mammals. In mouse serum, we detected specific binding activities of group IB and X sPLA 2 s, which was in contrast with the absence of binding activities in serum prepared from mice deficient in PLA 2 receptor (PLA 2 R), a type I transmembrane glycoprotein related to the C-type animal lectin family. Western blot analysis after partial purification with group IB sPLA 2 affinity column confirmed the identity of serum sPLA 2 -binding protein as a soluble form of PLA 2 R (sPLA 2 R) that retained all of the extracellular domains of the membrane-bound receptor. Both purified sPLA 2 R and the recombinant soluble receptor having all of the extracellular portions blocked the biological functions of group X sPLA 2 , including its potent enzymatic activity and its binding to the membrane-bound receptor. Protease inhibitor tests with PLA 2 R-overexpressing Chinese hamster ovary cells suggested that sPLA 2 R is produced by cleavage of the membrane-bound receptor by metalloproteinases. Thus, sPLA 2 R is the first example of circulating PLI that acts as an endogenous inhibitor for enzymatic activities and receptor-mediated functions of sPLA 2 s in mice.

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“…The pancreatic sPLA 2 has long been thought to act only as a digestive enzyme (8). However, the presence of this sPLA 2 in several non-digestive tissues has been demonstrated (9 -11), and it is now thought to play a role in airway and vascular smooth muscle contraction (12,13) as well as in cell proliferation (14). The inflammatory sPLA 2 has been purified and cloned from several sources (15,16) and is believed to play a central role in inflammatory processes (reviewed in Refs.…”

Section: Receptor Essentially Via Crds 3-6mentioning

confidence: 99%

Identification of the Binding Domain for Secretory Phospholipases A2 on Their M-type 180-kDa Membrane Receptor

Nicolas¹,

Lambeau²,

Lazdunski³

1995

Journal of Biological Chemistry

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The rabbit muscle (M)-type receptor for secretory phospholipases A 2 (sPLA 2 s) has a large extracellular domain of 1394 amino acids, composed of an N-terminal cysteine-rich domain, a fibronectin-like type II domain, and eight carbohydrate recognition domains (CRDs). It is thought to mediate some of the physiological effects of mammalian sPLA 2 s, including vascular smooth muscle contraction and cell proliferation, and is able to internalize sPLA 2 s. Here, we show by site-directed mutagenesis that OS 1 , a snake venom sPLA 2 , binds to the receptor via its CRDs and that deletion of CRD 5 completely abolishes the binding of sPLA 2 s. Moreover, a receptor lacking all CRDs but CRD 5 was still able to bind OS 1 although with a lower affinity. Deletion of CRDs 4 and 6, surrounding the CRD 5, slightly reduced the affinity for OS 1 , thus suggesting that these CRDs are also involved in the binding of OS 1 . The M-type sPLA 2 receptor and the macrophage mannose receptor are homologous and are predicted to share the same tertiary structure. p-Aminophenyl-␣-D-mannopyranoside bovine serum albumin, a known ligand of the macrophage mannose receptor, binds to the M-type sPLA 2 receptor essentially via CRDs 3-6.

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Effect of pancreatic type phospholipase A₂ on isolated porcine cerebral arteries via its specific binding sites

Cited by 54 publications

References 11 publications

Papyriflavonol A from Broussonetia papyrifera Inhibits the Passive Cutaneous Anaphylaxis Reaction and Has a Secretory Phospholipase A2-Inhibitory Activity.

Papyriflavonol A from Broussonetia papyrifera Inhibits the Passive Cutaneous Anaphylaxis Reaction and Has a Secretory Phospholipase A2-Inhibitory Activity.

Identification of a Soluble Form Phospholipase A2Receptor as a Circulating Endogenous Inhibitor for Secretory Phospholipase A2

Identification of the Binding Domain for Secretory Phospholipases A2 on Their M-type 180-kDa Membrane Receptor

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Effect of pancreatic type phospholipase A2 on isolated porcine cerebral arteries via its specific binding sites

Cited by 54 publications

References 11 publications

Papyriflavonol A from Broussonetia papyrifera Inhibits the Passive Cutaneous Anaphylaxis Reaction and Has a Secretory Phospholipase A2-Inhibitory Activity.

Papyriflavonol A from Broussonetia papyrifera Inhibits the Passive Cutaneous Anaphylaxis Reaction and Has a Secretory Phospholipase A2-Inhibitory Activity.

Identification of a Soluble Form Phospholipase A2Receptor as a Circulating Endogenous Inhibitor for Secretory Phospholipase A2

Identification of the Binding Domain for Secretory Phospholipases A2 on Their M-type 180-kDa Membrane Receptor

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Effect of pancreatic type phospholipase A₂ on isolated porcine cerebral arteries via its specific binding sites