Abstract
The mechanisms involved in the origin and development of malignant and neurodegenerative diseases are an important area of modern biomedicine. A crucial task is to identify new molecular markers that are associated with rearrangements of intracellular signaling and can be used for prognosis and the development of effective treatment approaches. The proteolipid plasmolipin (PLLP) is a possible marker. PLLP is a main component of the myelin sheath and plays an important role in the development and normal function of the nervous system. PLLP is involved in intracellular transport, lipid raft formation, and Notch signaling. PLLP is presumably involved in various disorders, such as cancer, schizophrenia, Alzheimer’s disease, and type 2 diabetes mellitus. PLLP and its homologs were identified as possible virus entry receptors. The review summarizes the data on the PLLP structure, normal functions, and role in diseases.
Highlights
Proteolipids were found in normal and tumor brain cells in the early 1950s and identified as a new class of protein–lipid compounds that are insoluble in water, but soluble in a chloroform–methanol mixture [1]
The proteolipid protein (PLP) is a constituent of the first major proteolipid isolated from myelin sheathforming cells, is 30 kDa in molecular weight, and accounts for approximately 10–30% of the total myelin protein [2, 3]
Proteolipid oligomerization facilitates the formation of ion-conducting transmembrane pores, and conformational changes in proteolipids are possibly responsible for their activity
Summary
Proteolipids were found in normal and tumor brain cells in the early 1950s and identified as a new class of protein–lipid compounds that are insoluble in water, but soluble in a chloroform–methanol mixture [1]. The proteolipid plasmolipin (PLLP) was initially isolated from plasma membranes of bovine kidney cells in 1981. Heterodimeric PLLP was termed the plasma membrane proteolipid protein (PMPLP) [10, 11]. There is no convincing evidence that the channels occur in vivo, but a negative correlation was observed between PLLP expression and the K+ conductance of the plasma membrane in cultured cells. A PMPLP heterodimer was initially termed PLLP, but later studies showed that the subunits of the heterodimer are identical and are encoded by the same gene [13, 16, 18]. Human PLLP (hPLLP) is in the long arm of chromosome 16 (16q13) and has four exons and a large first intron (Fig. 2), as is characteristic of the structures of genes coding for proteins with four transmembrane domains (TMs). II teins, such as connexin 32 (Cs32), rat myelin and lymphocyte protein (rMAL), 22-kDa peripheral myelin protein (PMP22), and PLP [16]
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