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Bovine brain cytosol contains three immunologically distinct forms of inositolphospholipid-specific phospholipase C.

作者信息

Ryu S H, Suh P G, Cho K S, Lee K Y, Rhee S G

机构信息

Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD 20892.

出版信息

Proc Natl Acad Sci U S A. 1987 Oct;84(19):6649-53. doi: 10.1073/pnas.84.19.6649.

DOI:10.1073/pnas.84.19.6649
PMID:3477795
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC299140/
Abstract

We previously reported that cytosolic fractions of bovine brain contain two immunologically distinct forms of phospholipase C (PLC), PLC-I and PLC-II. We now report the purification of another form of inositolphospholipid-specific phospholipase C from bovine brain cytosol, designated PLC-III, and the comparison of the catalytic properties of the three isozymes. Approximately 450 micrograms of pure PLC-III was obtained from 36 bovine brains, and it had a final specific activity of 30-40 mumol of phosphatidylinositol hydrolyzed per min per mg of enzyme in the presence of 0.1% deoxycholate. PLC-III exhibited an apparent Mr of 85,000 in NaDodSO4/PAGE, which is considerably smaller than the Mr of 150,000 for PLC-I and 145,000 for PLC-II. Neither of the two mixtures of monoclonal antibodies nor the rabbit polyclonal antibodies directed against either PLC-I or PLC-II cross-reacted with PLC-III. The catalytic properties of the three isozymes were studied by using small unilamellar vesicles prepared from either phosphatidylinositol (PtdIns) or phosphatidylinositol 4,5-bisphosphate (PtdInsP2) as substrates. Hydrolysis of both PtdIns and PtdInsP2 by the three enzymes was dependent on Ca2+. However, at low Ca2+ concentration, PtdInsP2 was the preferred substrate for all three enzymes. When PtdIns was the substrate, the three enzymes exhibited similar specific activities at their optimum pH, which was 4.8 for PLC-I, 5.0 for PLC-II, and 5.5 for PLC-III. But at neutral pH, the order of specific activity was PLC-III greater than PLC-II greater than PLC-I. In contrast, the order of specific activity was PLC-I greater than PLC-III greater than PLC-II for PtdInsP2 hydrolysis, which means that PLC-I is the most specific for PtdInsP2. The three enzymes were affected differently by bovine serum albumin: inhibition of PLC-I and activation of PLC-III were observed, whereas PLC-II was unaffected. This observation suggests that any putative protein effectors for PLC should be critically scrutinized.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5c8/299140/afc8750aedbd/pnas00334-0049-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5c8/299140/d00d0d36af88/pnas00334-0048-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5c8/299140/57d182def2d3/pnas00334-0048-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5c8/299140/4272a1c33e2b/pnas00334-0048-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5c8/299140/afc8750aedbd/pnas00334-0049-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5c8/299140/d00d0d36af88/pnas00334-0048-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5c8/299140/57d182def2d3/pnas00334-0048-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5c8/299140/4272a1c33e2b/pnas00334-0048-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5c8/299140/afc8750aedbd/pnas00334-0049-a.jpg

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Proc Natl Acad Sci U S A. 1987 Oct;84(19):6649-53. doi: 10.1073/pnas.84.19.6649.
2
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本文引用的文献

1
Purification of phosphatidylinositol-specific phospholipase C from rat liver.从大鼠肝脏中纯化磷脂酰肌醇特异性磷脂酶C
J Biol Chem. 1981 Jul 10;256(13):6769-75.
2
Modulation of phosphatidylinositol-specific phospholipase C activity by phospholipid interactions, diglycerides, and calcium ions.磷脂相互作用、甘油二酯和钙离子对磷脂酰肌醇特异性磷脂酶C活性的调节
J Biol Chem. 1982 Dec 10;257(23):14359-64.
3
Identification and properties of two distinct phosphatidylinositol-specific phospholipase C enzymes from sheep seminal vesicular glands.
细胞内酸化通过PLCδ1以钙依赖的方式促进受体介导的TRPC4激活。
J Physiol. 2020 Jul;598(13):2651-2667. doi: 10.1113/JP279658. Epub 2020 May 22.
4
Phospholipase C.磷脂酶 C
Adv Exp Med Biol. 2020;1131:215-242. doi: 10.1007/978-3-030-12457-1_9.
5
Intramolecular electrostatic interactions contribute to phospholipase Cβ3 autoinhibition.分子内静电相互作用有助于磷脂酶 Cβ3 的自动抑制。
Cell Signal. 2019 Oct;62:109349. doi: 10.1016/j.cellsig.2019.109349. Epub 2019 Jun 26.
6
A catalytic career: Studies spanning glutamine synthetase, phospholipase C, peroxiredoxin, and the intracellular messenger role of hydrogen peroxide.催化生涯：研究横跨谷氨酰胺合成酶、磷脂酶 C、过氧化物还原酶以及过氧化氢的细胞内信使作用。
J Biol Chem. 2019 Mar 29;294(13):5169-5180. doi: 10.1074/jbc.X119.007975.
7
Charge Shielding of PIP2 by Cations Regulates Enzyme Activity of Phospholipase C.阳离子对磷脂酰肌醇-4,5-二磷酸（PIP2）的电荷屏蔽调节磷脂酶C的酶活性。
PLoS One. 2015 Dec 11;10(12):e0144432. doi: 10.1371/journal.pone.0144432. eCollection 2015.
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