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Scandinavian Journal of Immunology.... 1982
Review
Topics: Amino Acids; Animals; Antibodies; Antigen-Antibody Complex; Brain; Brain Chemistry; Humans; Molecular Weight; Proteolipids; Species Specificity
PubMed: 6763766
DOI: 10.1111/j.1365-3083.1982.tb03762.x -
Biokhimiia (Moscow, Russia) Nov 1993A convenient procedure is proposed for extracting mitochondrial proteolipids using a single phase mixture chloroform-methanol-water (1:2:0.8 v/v) with subsequent...
A convenient procedure is proposed for extracting mitochondrial proteolipids using a single phase mixture chloroform-methanol-water (1:2:0.8 v/v) with subsequent separation of the phases. The proteolipids were concentrated at the interface between the phases and thus purified from the bulk of the phospholipids. It was found that the mitochondrial proteolipids represent stable complexes of phospholipids with some low molecular weight proteins (M(r) = 7-18 kDa). The latter are destroyed at acid pH values. The phospholipid/protein ratio was found to be equal to 6 (assuming the molecular masses of the proteins and phospholipids to be equal to 10 and 0.8 kDa, respectively). The phospholipid composition of the tightly bound proteolipids thus obtained did not differ from that of the mitochondrial phospholipids. Using 31P-NMR, nonbilayer structures were found to arise from proteolipid reconstitution into multibilayer liposomes.
Topics: Animals; Cattle; Chromatography, Liquid; Chromatography, Thin Layer; Electrophoresis, Polyacrylamide Gel; Liposomes; Magnetic Resonance Spectroscopy; Mitochondria, Heart; Mitochondria, Liver; Proteolipids; Rats
PubMed: 8268319
DOI: No ID Found -
Journal of Dental Research Mar 1988De novo formation of calcium hydroxyapatite in biological systems occurs on membrane surfaces through specific interactions of Ca, Pi, phospholipids, calcifiable...
De novo formation of calcium hydroxyapatite in biological systems occurs on membrane surfaces through specific interactions of Ca, Pi, phospholipids, calcifiable proteolipids, and ion flux to and from the nucleating site. This paper reports an in vitro model demonstrating an ion transport function for calcifiable proteolipid. Bacterionema matruchotii proteolipid was incubated with a radiolabeled H+-channel inhibitor, 14C-dicyclohexyl-carbodiimide, and binding characterized by displacement studies with DCCD or ethyldimethylaminopropylcarbodiimide. A carboxyl binding site was suggested by displacement of DCCD by the nucleophile, glycine ethyl ester. The displacement studies indicated that proteolipid bound DCCD via carboxyl group interaction in a hydrophobic region of the protein. SDS-polyacrylamide gel electrophoresis showed that all label was associated with a single band of 8500 Mr. No non-specific binding of 14C-DCCD to phospholipids occurred, since all bound label was associated with protein following Sephadex LH-20 chromatography of crude proteolipid. Phospholipid liposomes were prepared containing bacteriorhodopsin and proteolipid or proteolipid-14C-DCCD, via cholate dialysis. Transmembrane pH changes established by the bacteriorhodopsin H+ pump were measured in the presence and absence of added proteolipid. Proteolipid had an effect similar to those of uncouplers such as tetraphenylboron. Both the rate and extent of proton translocation increased following addition of proteolipid to BR-liposomes. 14C-DCCD abolished the proteolipid-augmented ion transport. When tetraphenylboron was used to abolish the transmembrane electrical potential, calcifiable proteolipid did not augment proton transport.(ABSTRACT TRUNCATED AT 250 WORDS)
Topics: Actinomycetaceae; Binding Sites; Carbodiimides; Carrier Proteins; Dicyclohexylcarbodiimide; Durapatite; Hydroxyapatites; Ion Channels; Proteolipids; Protons
PubMed: 2459167
DOI: 10.1177/00220345880670030101 -
Zhurnal Evoliutsionnoi Biokhimii I... 1984The Folch-Lees proteolipid complexes of different purity (crude proteolipids and relative pure proteolipids) were isolated from vertebrate brain: mammalia (Macaca irus,... (Comparative Study)
Comparative Study
The Folch-Lees proteolipid complexes of different purity (crude proteolipids and relative pure proteolipids) were isolated from vertebrate brain: mammalia (Macaca irus, Macaca rhesus and white rat), birds (Columbia livia), reptilia (Testudo horsfieldi), amphibia (Rana temporaria) and fishes (Salmo irideus). The proteolipid complexes were isolated by emulsion-centrifugation method. The content of proteolipid protein (mg/g w. w.) correlates with the level of phylogenetic development of the animals studied. It is the highest in monkey brain (10.5 and 8.6 mg/g) and the lowest in fish brain (2.2 mg/g). The yield of proteolipids from the brains of animals studied shows the same pattern. Crude proteolipids of mammalia, birds and reptiles contain 40-50% of protein and 60-50% of lipids. The content of phospholipids is about 40%. Proteolipids of amphibia and fish brain contain less protein--about 30%. In the conditions of mild purification, the protein content in mammalia, birds and reptilia makes up about 70% and lipid content--about 30-35%. The crude and purified proteolipids in all the animals studied (as compared with the original lipid extracts from which they were isolated) are enriched in acid phospholipids: phosphatidyl serine, phosphatidyl inositol and diphosphatidyl glycerol. Acid phospholipids in total lipid extract make up 10-20% of total phospholipids, in crude proteolipids 16-32 and in purified proteolipids--56-75%. There are no marked differences between fatty acid composition of phospholipids in proteolipids and in the same phospholipids isolated from total lipid extract.
Topics: Animals; Brain Chemistry; Columbidae; Fatty Acids; Macaca; Macaca mulatta; Phospholipids; Proteolipids; Rana temporaria; Rats; Salmonidae; Turtles; Vertebrates
PubMed: 6610997
DOI: No ID Found -
Current Opinion in Neurobiology Oct 1993Myelin formation and maintenance requires complex interactions between neurons and glia, and between the integral protein and lipid components of the myelin sheath. Many... (Review)
Review
Myelin formation and maintenance requires complex interactions between neurons and glia, and between the integral protein and lipid components of the myelin sheath. Many of the underlying mechanisms may be examined by studying the perturbations caused by spontaneous and targeted mutations in myelin protein genes. This review summarizes the progress in our understanding of these mutations with an emphasis on integrating the recent advances in the genetics of myelin into a more generalized view of myelin organization and function.
Topics: Amino Acid Sequence; Animals; Apoproteins; Humans; Models, Genetic; Molecular Sequence Data; Myelin Basic Protein; Myelin P0 Protein; Myelin Proteins; Myelin Proteolipid Protein; Proteolipids
PubMed: 7505139
DOI: 10.1016/0959-4388(93)90140-t -
Neurochemical Research Nov 1985In this report data are summarized on changes in the quantity of proteolipid protein (PLP), its amino acid composition, and the lipid moiety of these lipid-protein... (Comparative Study)
Comparative Study
In this report data are summarized on changes in the quantity of proteolipid protein (PLP), its amino acid composition, and the lipid moiety of these lipid-protein complexes in rat brain during postnatal development. In all three parts of the central nervous system (CNS) studied (cerebral hemispheres, medulla oblongata and spinal cord) the main pattern of PLP accumulation is on the whole similar. PLP content is very low in the newborn, and it increased 12 to 20-fold during development. The highest rate of PLP accumulation is observed in the period from 10 to 30 days after birth. Against the background of general similarity the concentration of some amino acids such as lysine, proline, tyrosine in PLP somewhat increased during development, while that of aspartic acid, glutamic acid, glycine, and leucine decreased. Soluble proteolipid complexes, purified to various degree from lipids were isolated from brain of rats of different ages. As compared with the original lipid extracts from which they were obtained, the crude and especially purified proteolipids in all the animals studied were enriched in acidic phospholipids (PhL). This prevalence of acidic PhL increased with age. During the development in phospholipid moiety of proteolipids (PL) the content of phosphatidyl serine, sphingomyelin and mainly diphosphatidyl glycerol increases and that of phosphatidyl inositol and especially phosphatidyl choline decreases. The concentration of acidic PhL more tightly bound with PLP appreciably increases with age. Most of these changes occur mainly during the second decade after birth.
Topics: Age Factors; Amino Acids; Animals; Central Nervous System; Chemical Phenomena; Chemistry; Medulla Oblongata; Myelin Sheath; Proteolipids; Rats; Spinal Cord; Telencephalon
PubMed: 4088430
DOI: No ID Found -
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 -
Methods in Molecular Biology (Clifton,... 2003
Topics: Animals; Cell Line; DNA, Complementary; Dogs; Kidney; Membrane Microdomains; Membrane Proteins; Proteolipids
PubMed: 12824556
DOI: 10.1385/1-59259-400-X:223 -
Calcified Tissue International Mar 1984This study demonstrates that calcium-phospholipid-phosphate complexes (CPLX) and calcifiable proteolipid are associated in vivo by establishing that they can be...
This study demonstrates that calcium-phospholipid-phosphate complexes (CPLX) and calcifiable proteolipid are associated in vivo by establishing that they can be co-isolated from calcified bacteria. Both of these membrane constituents, which support apatite formation in vitro, have been isolated independently from Bacterionema matruchotii. However, isolation of proteolipid was preceded by demineralization in 2N formic acid, thereby dissociating bound Ca, whereas isolation of CPLX included sonication of calcified bacteria in 2:1:1.5 chloroform:methanol:Tris buffer, thereby dissociating any protein. Co-isolation is possible by demineralizing the calcified bacteria with 50 mM phthalic acid, pH 5.5, followed by extraction with 2:1 chloroform:methanol, and precipitation of crude phospholipid with acetone. CPLX and proteolipid are present in all Sephadex LH-20 chromatographic fractions of the crude phospholipid and of diethyl ether precipitates of the crude phospholipid. CPLXs contain protein:phospholipid:Ca:Pi but differ in relative composition from each other and from independently isolated CPLX. The Ca:phospholipid:Pi molar ratio of diethyl ether precipitable proteolipid-CPLX is most similar to previously published values for CPLX. The protein content of CPLX accounts for all of the proteolipid apoprotein in each Sephadex LH-20 fraction.
Topics: Actinomycetaceae; Calcium; Chromatography, Gel; Phospholipids; Phthalic Acids; Proteolipids
PubMed: 6430504
DOI: 10.1007/BF02405320 -
Zhurnal Evoliutsionnoi Biokhimii I... 1984From the whole brain of animals representing 5 classes of vertebrates--mammals (Macaca rhesus and albino rat), birds (the pigeon Columba livia), reptiles (the tortoise...
From the whole brain of animals representing 5 classes of vertebrates--mammals (Macaca rhesus and albino rat), birds (the pigeon Columba livia), reptiles (the tortoise Testudo horsfieldi), amphibians (the frog Rana temporaria) and fishes (the trout Salmo irideus), as well as from myelin preparations of mammals (dog, rabbit and rat) proteolipids have been isolated by emulsion--centrifugation method. It was shown that extraction procedure results in the loss and destruction of several proteolipid complexes. In all the animals investigated, the main loss (from 25 to 75% of all complexes) was observed during emulsion--centrifugation stage, especially during 10-min centrifugation at 200 g. During extraction of proteolipids from the whole brain, under the conditions employed, the lost proteolipids are presumably those which belong to the myelin fraction. To prevent excessive proteolipid loss, the final low speed centrifugation step should be avoided. It was shown that in order to obtain proteolipids in a soluble form in a mixture of chloroform and methanol, total proteolipids from the brain of mammals should contain not less than 27% of phospholipids. Studies were also made on the composition and relative content of phospholipids in proteolipids extracted from the whole mammalian brain and myelin preparations. With respect to phospholipid composition, proteolipids from the whole brain significantly differ from those obtained from myelin fraction. Myelin fraction, being itself rich in proteolipids, contain large amounts of phosphatidyl serine (up to 69); however, proteolipids of this fraction contain lower amounts (4%) of diphosphatidyl glycerol as compared to proteolipids from the whole brain (22%).(ABSTRACT TRUNCATED AT 250 WORDS)
Topics: Animals; Brain Chemistry; Centrifugation; Columbidae; Dogs; Macaca mulatta; Methods; Myelin Sheath; Phospholipids; Proteolipids; Rabbits; Rana temporaria; Rats; Trout; Turtles
PubMed: 6335333
DOI: No ID Found