RAT MEMBRANE PHOSPHATIDATE PHOSPHOHYDROLASE AND THE REASON FOR ITS MG+ INDEPENDENCE

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HEYDARIAN E.; HAGHIGHI BAHRAM

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Journal: Journal of Ilam University of Medical Sciences Year:2006 | Volume:14 | Issue:3 Page(s): 12-21

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Title

RAT MEMBRANE PHOSPHATIDATE PHOSPHOHYDROLASE AND THE REASON FOR ITS MG+ INDEPENDENCE

Author(s)

HEYDARIAN E. | HAGHIGHI BAHRAM | Issue Writer Certificate

Keywords

MEMBRANE PHOSPHATIDATE PHOSPHOHYDROLASEQ3

PHOSPHATIDIC ACIDQ3

LA AND HII PHOSPHATIDATEQ3

Abstract

Introduction: phosphatidate phosphohydrolase (PAP) catalyzes the dephosphorylation of PHOSPHATIDIC ACID to yield Pi and diacylglycerol. Two forms of PAP in rat hepatocyte have been reported. A cytosolic form (PAP1) that is responsible for glycerolipid metabolism and requires Mg2for its activity. Another form (PAP2) is primarily involved in lipid signaling pathways which dose not need Mg2+. It has two isoforms; PAP 2a and PAP2b. Little information is known about enzymological characterization of PAP2 especially its substrate. We investigated the enzyme behavior against Mg2+ structure- breaking agents (urea and guanidine HCl) with respect to its substrate. Materials & Methods: PAP2b was purified from rat hepatocyte membrane using a multi – stage chromatography. The enzyme activity was determined against La (lamellar) and HII (Hexagonal) forms of substrate in the presence of triton X-100. The effect of Mg2+ concentration and urea and guanidine HCl (structure- breaking agents) were examined on La to HII phase transition and enzyme activity. Results: PAP2b consumes La form of phosphatidate. Cations such as Mg2+ result in HII from La phase of substrate and therefore reduce enzyme activity. Urea and guanidine HCl increase enzyme activity due to prevention of HII formation. Both can also reduce the effect of cations on La to HII transition of phosphatidate.Conclusion: Since PAP2b consumes La form of substrate parameters can induce La to HII phase transition which result in low enzyme activity. In contrast, factors such as urea and guanidine HCl increase activity due to prevention of La to HII phase transition . As Mg2+ stimulates HII formation and the enzyme needs La form substrate, it can be concluded that, Not only does the enzyme need no Mg2+,but it is controlled by it too.

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References

IDENTIFICATION OF ESSENTIAL LYSINE RESIDUE FOR CATALYTIC ACTIVITY OF PLASMA MEMBRANE PHOSPHATIDATE PHOSPHOHYDROLASE OF RAT LIVER

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APA: Copy

HEYDARIAN, E., & HAGHIGHI, BAHRAM. (2006). RAT MEMBRANE PHOSPHATIDATE PHOSPHOHYDROLASE AND THE REASON FOR ITS MG+ INDEPENDENCE. JOURNAL OF ILAM UNIVERSITY OF MEDICAL SCIENCES, 14(3), 12-21. SID. https://sid.ir/paper/90366/en

Vancouver: Copy

HEYDARIAN E., HAGHIGHI BAHRAM. RAT MEMBRANE PHOSPHATIDATE PHOSPHOHYDROLASE AND THE REASON FOR ITS MG+ INDEPENDENCE. JOURNAL OF ILAM UNIVERSITY OF MEDICAL SCIENCES[Internet]. 2006;14(3):12-21. Available from: https://sid.ir/paper/90366/en

IEEE: Copy

E. HEYDARIAN, and BAHRAM HAGHIGHI, “RAT MEMBRANE PHOSPHATIDATE PHOSPHOHYDROLASE AND THE REASON FOR ITS MG+ INDEPENDENCE,” JOURNAL OF ILAM UNIVERSITY OF MEDICAL SCIENCES, vol. 14, no. 3, pp. 12–21, 2006, [Online]. Available: https://sid.ir/paper/90366/en

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