-
Revue Scientifique Et Technique... Apr 2016There is a critical need in animal agriculture to develop novel antimicrobials and alternative strategies that will help to reduce the use of antibiotics and address the... (Review)
Review
There is a critical need in animal agriculture to develop novel antimicrobials and alternative strategies that will help to reduce the use of antibiotics and address the challenges of antimicrobial resistance. High-throughput gene expression analysis is providing new tools that are enabling the discovery of host-derived antimicrobial peptides. Examples of gene-encoded natural antibiotics that have gained attention include antimicrobial peptides such as human granulysin and its multi-species homolog, namely NK-lysin, which provide a protective response against a broad range of microbes and are a principal component of innate immunity in vertebrates. Both granulysin and NK-lysin are localised in cytolytic granules in natural killer and cytotoxic T lymphocytes. Host-derived NK-lysins that were first described in mammals are also found in avian species, and they have been shown to have antimicrobial activities that could potentially be used to control important poultry pathogens. Morphological alterations observed following chicken NK-lysin binding to Eimeria sporozoites and Escherichia coli membranes indicate damage and disruption of cell membranes, suggesting that NK-lysin kills pathogenic protozoans and bacteria by direct interaction. Genotype analysis revealed that chicken NK-lysin peptides derived from certain alleles were more effective at killing pathogens than those derived from others, which could potentially affect susceptibility to diseases. Although the host-derived antimicrobial peptides described in this paper may not, by themselves, be able to replace the antibiotics currently used in animal production, their use as specific treatments based on their known mechanisms of action is showing promising results.
Topics: Animals; Antimicrobial Cationic Peptides; Birds; Genomics; Proteolipids
PubMed: 27217171
DOI: 10.20506/rst.35.1.2420 -
Trends in Endocrinology and Metabolism:... Dec 2016Skeletal muscle constitutes ∼40% of body mass and has the capacity to play a major role as thermogenic, metabolic, and endocrine organ. In addition to shivering,... (Review)
Review
Skeletal muscle constitutes ∼40% of body mass and has the capacity to play a major role as thermogenic, metabolic, and endocrine organ. In addition to shivering, muscle also contributes to nonshivering thermogenesis via futile sarcoplasmic/endoplasmic reticulum Ca ATPase (SERCA) activity. Sarcolipin (SLN), a regulator of SERCA activity in muscle, plays an important role in regulating muscle thermogenesis and metabolism. Uncoupling of SERCA by SLN increases ATP hydrolysis and heat production, and contributes to temperature homeostasis. SLN also affects whole-body metabolism and weight gain in mice, and is upregulated in various muscle diseases including muscular dystrophy, suggesting a role for SLN during increased metabolic demand. In this review we also highlight the physiological roles of skeletal muscle beyond contraction.
Topics: Animals; Humans; Muscle Proteins; Muscle, Skeletal; Proteolipids; Sarcoplasmic Reticulum Calcium-Transporting ATPases; Thermogenesis
PubMed: 27637585
DOI: 10.1016/j.tem.2016.08.006 -
Microbiology Spectrum Jan 2019Outer membrane vesicles (OMVs) are nanosized proteoliposomes derived from the outer membrane of Gram-negative bacteria. They are ubiquitously produced both in culture...
Outer membrane vesicles (OMVs) are nanosized proteoliposomes derived from the outer membrane of Gram-negative bacteria. They are ubiquitously produced both in culture and during infection and are now recognized to play crucial roles during host-microbe interactions. OMVs can transport a broad range of chemically diverse cargoes, including lipids and lipopolysaccharides, membrane-embedded and associated proteins and small molecules, peptidoglycan, and nucleic acids. Particularly, virulence factors such as adhesins and toxins are often enriched in OMVs. Here we discuss a variety of ways in which OMVs facilitate host-microbe interactions, including their contributions to biofilm formation, nutrient scavenging, and modulation of host cell function. We particularly examine recent findings regarding OMV-host cell interactions in the oral cavity and the gastrointestinal tract.
Topics: Bacterial Outer Membrane Proteins; Biological Transport; Cell Membrane; Gram-Negative Bacteria; Humans; Lipopolysaccharides; Proteolipids; Transport Vesicles
PubMed: 30681067
DOI: 10.1128/microbiolspec.PSIB-0001-2018 -
Cellular and Molecular Life Sciences :... Apr 2022Proteolipids are proteins with unusual lipid-like properties. It has long been established that PLP and plasmolipin, which are two unrelated membrane-tetra-spanning...
Proteolipids are proteins with unusual lipid-like properties. It has long been established that PLP and plasmolipin, which are two unrelated membrane-tetra-spanning myelin proteolipids, can be converted in vitro into a water-soluble form with a distinct conformation, raising the question of whether these, or other similar proteolipids, can adopt two different conformations in the cell to adapt their structure to distinct environments. Here, we show that MALL, another proteolipid with a membrane-tetra-spanning structure, distributes in membranes outside the nucleus and, within the nucleus, in membrane-less, liquid-like PML body biomolecular condensates. Detection of MALL in one or other environment was strictly dependent on the method of cell fixation used, suggesting that MALL adopts different conformations depending on its physical environment -lipidic or aqueous- in the cell. The acquisition of the condensate-compatible conformation requires PML expression. Excess MALL perturbed the distribution of the inner nuclear membrane proteins emerin and LAP2β, and that of the DNA-binding protein BAF, leading to the formation of aberrant nuclei. This effect, which is consistent with studies identifying overexpressed MALL as an unfavorable prognostic factor in cancer, could contribute to cell malignancy. Our study establishes a link between proteolipids, membranes and biomolecular condensates, with potential biomedical implications.
Topics: Biomolecular Condensates; Cell Nucleus; Humans; Molecular Conformation; Neoplasms; Proteolipids
PubMed: 35399121
DOI: 10.1007/s00018-022-04270-w -
Biochimica Et Biophysica Acta Jan 2015The motional averaging of powder pattern line shapes is one of the most fundamental aspects of sold-state NMR. Since membrane proteins in liquid crystalline phospholipid... (Review)
Review
The motional averaging of powder pattern line shapes is one of the most fundamental aspects of sold-state NMR. Since membrane proteins in liquid crystalline phospholipid bilayers undergo fast rotational diffusion, all of the signals reflect the angles of the principal axes of their dipole-dipole and chemical shift tensors with respect to the axis defined by the bilayer normal. The frequency span and sign of the axially symmetric powder patterns that result from motional averaging about a common axis provide sufficient structural restraints for the calculation of the three-dimensional structure of a membrane protein in a phospholipid bilayer environment. The method is referred to as rotationally aligned (RA) solid-state NMR and demonstrated with results on full-length, unmodified membrane proteins with one, two, and seven trans-membrane helices. RA solid-state NMR is complementary to other solid-state NMR methods, in particular oriented sample (OS) solid-state NMR of stationary, aligned samples. Structural distortions of membrane proteins from the truncations of terminal residues and other sequence modifications, and the use of detergent micelles instead of phospholipid bilayers have also been demonstrated. Thus, it is highly advantageous to determine the structures of unmodified membrane proteins in liquid crystalline phospholipid bilayers under physiological conditions. RA solid-state NMR provides a general method for obtaining accurate and precise structures of membrane proteins under near-native conditions.
Topics: Amino Acid Sequence; Diffusion; Magnetic Resonance Spectroscopy; Membrane Proteins; Molecular Sequence Data; Protein Folding; Proteolipids; Rotation
PubMed: 24747039
DOI: 10.1016/j.bbamem.2014.04.002 -
Chest Jun 1997
Review
Topics: Humans; Infant, Newborn; Lung; Lung Diseases; Proteolipids; Pulmonary Surfactants; Respiratory Distress Syndrome, Newborn
PubMed: 9184562
DOI: 10.1378/chest.111.6_supplement.129s-a -
Plant Physiology Apr 2020Plasma membranes provide a highly selective environment for a large number of transmembrane and membrane-associated proteins. Whereas lateral movement of proteins in... (Review)
Review
Plasma membranes provide a highly selective environment for a large number of transmembrane and membrane-associated proteins. Whereas lateral movement of proteins in this lipid bilayer is possible, it is rather limited in turgid and cell wall-shielded plant cells. However, membrane-resident signaling processes occur on subsecond scales that cannot be explained by simple diffusion models. Accordingly, several receptors and other membrane-associated proteins are organized and functional in membrane nanodomains. Although the general presence of membrane nanodomains has become widely accepted as fact, fundamental functional aspects, the roles of individual lipid species and their interplay with proteins, and aspects of nanodomain maintenance and persistence remain poorly understood. Here, we review the current knowledge of nanodomain organization and function, with a particular focus on signaling processes involving proteins, lipids, and their interactions. Furthermore, we propose new and hypothetical aspects of plant membrane biology that we consider important for future research.
Topics: Cell Membrane; Membrane Microdomains; Models, Biological; Proteolipids; Signal Transduction
PubMed: 31857424
DOI: 10.1104/pp.19.01349 -
American Journal of Physiology. Cell... Feb 2022Duchenne muscular dystrophy (DMD) is an inherited muscle wasting disease. Metabolic impairments and oxidative stress are major secondary mechanisms that severely worsen...
Duchenne muscular dystrophy (DMD) is an inherited muscle wasting disease. Metabolic impairments and oxidative stress are major secondary mechanisms that severely worsen muscle function in DMD. Here, we sought to determine whether germline reduction or ablation of sarcolipin (SLN), an inhibitor of sarco/endoplasmic reticulum (SR) Ca ATPase (SERCA), improves muscle metabolism and ameliorates muscle pathology in the mouse model of DMD. Glucose and insulin tolerance tests show that glucose clearance rate and insulin sensitivity were improved in the SLN haploinsufficient () and SLN-deficient () mice. The histopathological analysis shows that fibrosis and necrosis were significantly reduced in muscles of and mice. SR Ca uptake, mitochondrial complex protein levels, complex activities, mitochondrial Ca uptake and release, and mitochondrial metabolism were significantly improved, and lipid peroxidation and protein carbonylation were reduced in the muscles of and mice. These data demonstrate that reduction or ablation of SLN expression can improve muscle metabolism, reduce oxidative stress, decrease muscle pathology, and protects the mice from glucose intolerance.
Topics: Animals; Blood Glucose; Female; Male; Mice; Mice, Inbred C57BL; Mice, Inbred mdx; Mice, Knockout; Muscle Proteins; Muscle, Skeletal; Oxidative Stress; Proteolipids
PubMed: 34986021
DOI: 10.1152/ajpcell.00125.2021 -
Biochimica Et Biophysica Acta Nov 1998Surfactant protein concentrations are precisely maintained during fetal development and postnatally controlled, at least in part, by the regulation of gene transcription... (Review)
Review
Surfactant protein concentrations are precisely maintained during fetal development and postnatally controlled, at least in part, by the regulation of gene transcription and/or mRNA stability. Together, these mechanisms contribute to the unique temporal-spatial distribution of surfactant protein synthesis that is characteristic of the mammalian lung. Surfactant proteins A, B and C are expressed primarily in subsets of respiratory epithelial cells, wherein their expression is modified by developmental, physiological, humoral and inflammatory stimuli. Cell specific and humoral regulation of surfactant protein transcription is determined by the interactions of a number of nuclear transcription proteins that function in combination, by binding to cis-acting elements located in the 5' regulatory regions of each of the surfactant protein genes. The unique combination of distinct and shared cis-acting elements and transcriptional proteins serves to modulate surfactant protein synthesis in the lung. The present review will summarize efforts to identify the mechanisms contributing to the regulation of surfactant protein gene transcription in the lung, focusing to the nuclear transcription factor, TTF-1 (or thyroid transcription factor-1), a member of the Nkchi2 family of nuclear transcription proteins. A complete review of regulatory aspects of surfactant homeostasis is beyond the scope of the present summary.
Topics: DNA-Binding Proteins; Gene Expression Regulation; Hepatocyte Nuclear Factor 3-beta; Lung; Nuclear Proteins; Proteolipids; Pulmonary Surfactants; Thyroid Nuclear Factor 1; Transcription Factors; Transcription, Genetic
PubMed: 9813380
DOI: 10.1016/s0925-4439(98)00076-3 -
Molekuliarnaia Biologiia 2021The mechanisms involved in the origin and development of malignant and neurodegenerative diseases are an important area of modern biomedicine. A crucial task is to...
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.
Topics: Diabetes Mellitus, Type 2; Humans; Myelin Sheath; Myelin and Lymphocyte-Associated Proteolipid Proteins; Nerve Tissue Proteins; Proteolipids
PubMed: 34837695
DOI: 10.31857/S0026898421060112