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The Structures and Functions of Intracellular Phospholipase A1 Family Proteins

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Phospholipases in Health and Disease

Part of the book series: Advances in Biochemistry in Health and Disease ((ABHD,volume 10))

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Abstract

Phospholipase A1 is an enzyme that hydrolyzes phospholipids, producing 2-acyl-lysophospholipids and fatty acids. Intracellular phospholipase A1 (iPLA1) functions inside cells. Except for a short lipase consensus sequence (G–X–S–X–G), the overall primary structures of iPLA1 proteins differ from those of other phospholipases. While yeast, nematode, fruit fly, and Arabidopsis each have only one iPLA1 gene, mammals including humans possess three iPLA1 genes (phosphatidic acid-preferring phospholipase A1 (PA-PLA1)/DDHD1/iPLA1α, p125/Sec23IP/iPLA1β, and KIAA0725p/DDHD2/iPLA1γ). The three mammalian iPLA1 proteins are localized in different subcellular compartments, suggesting their different roles. All the iPLA1 family proteins have a domain named DDHD, in addition to a lipase consensus sequence, and some of them have a sterile alpha motif (SAM). Studies of the three mammalian iPLA1 proteins have demonstrated that the lipase consensus sequence and the DDHD domain are involved in their enzymatic activity, and that the tandem SAM-DDHD domain is important for binding to intracellular membranes. Recent studies have revealed the physiological functions of the iPLA1 proteins. p125 plays a role in vesicular transport and seems to be involved in spermiogenesis. As to human diseases, mutations of the PA-PLA1 and KIAA0725p genes are responsible for hereditary spastic paraplegia, a neurodegenerative disorder. In this chapter, we focus on the mammalian iPLA1 proteins and provide an overview of their structures and functions. We also briefly mention the physiological functions of nonmammalian iPLA1 family proteins.

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Acknowledgment

We thank Tomoyuki Shishido for critical reading of the manuscript.

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Authors and Affiliations

  1. School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, 192-0392, Japan

    Katsuko Tani, Takashi Baba & Hiroki Inoue

Authors
  1. Katsuko Tani
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  2. Takashi Baba
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  3. Hiroki Inoue
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Corresponding author

Correspondence to Katsuko Tani .

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Editors and Affiliations

  1. I.H. Asper Clinical Research Institute St. Boniface Hospital Research, Winnipeg, Manitoba, Canada

    Paramjit S. Tappia

  2. St. Boniface Hosp. Research, Univ. of Ma Institute of Cardiovascular Sciences, Winnipeg, Manitoba, Canada

    Naranjan S. Dhalla

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Tani, K., Baba, T., Inoue, H. (2014). The Structures and Functions of Intracellular Phospholipase A1 Family Proteins. In: Tappia, P., Dhalla, N. (eds) Phospholipases in Health and Disease. Advances in Biochemistry in Health and Disease, vol 10. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-0464-8_5

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