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EN
Ca 2+ is involved in the regulation of many events in the nucleus, such as gene expression, DNA replication, DNA repair, chromatin fragmentation in apoptosis, modulation of an intranuclear contractile system. In some cases, the function of Ca 2+ is mediated by calmodulin. However, the regulation of nucleoplasmic Ca 2+ concentration has not been explored throughly. The data discussed in this review show that the [Ca 2+]n may be regulated independently of that of cytosolic Ca 2+. IP3 and acid ADP-ribose are the major factors responsible for Ca 2+ release into the nucleus from perinuclear space.
EN
The paper contains available data on the content, composition and metabolism of different lipid fractions in the nuclei. The results on physiological function of the nuclear lipids are also included. Nuclear phosphatidylinositols have been shown to play a role of messengers signalling from the cytoplasm to the nuclei. Most sphingomyeline is located in the nucleoplasm and it effect stability of DNA. A role of nuclear triacylglycerols remains unknown. Polyunsaturated long chain fatty acids control transcription of genes encoding lipogenic and glycolytic enzymes. Cholesterol present in the nuclear envelope plays probably only structural function, but that present in chromatin may be involved in regulation of cholesterol biosynthesis.
EN
The major phospholipid classes of the human red blood cell membrane are: phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine and sphingomyeli. These phospholipids are distributed asymmetrically across the two halves of the lipid bilayer. this asymmetry appears to be generated and maintained by an ATP-dependent translocation of aminophospholipids from outer to inner leaflet, and by the interaction of phospholipids with skeletal proteins. The phosphoinositides account for 3-4% of total erythrocyte membrane phospholipid. They play an important role in signal transduction and are involved in other various membrane functions.
EN
The antimicrobial peptide LL-37 is the only known member of the cathelicidin family of peptides expressed in humans. LL-37 is a multifunctional host defense molecule essential for normal immune responses to infection and tissue injury. LL-37 peptide is a potent killer of different microorganisms with the ability to prevent immunostimulatory effects of bacterial wall molecules such as lipopolysaccharide and can therefore protect against lethal endotoxemia. Additional reported activities of LL-37 include chemoattractant function, inhibition of neutrophil apoptosis, and stimulation of angiogenesis, tissue regeneration, and cytokine release (e.g. IL-8). Cellular production of LL-37 is affected by multiple factors, including bacterial products, host cytokines, availability of oxygen, and sun exposure through the activation of CAP-18 gene expression by vitamin D3. At infection sites, the function of LL-37 can be inhibited by charge-driven interactions with DNA and F-actin released from dead neutrophils and other cells lysed as the result of inflammation. A better understanding of LL-37's biological properties is necessary for its possible therapeutic application for immunomodulatory purposes as well as in treating bacterial infection.
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