scholarly journals Modifications of Membrane Phospholipids in Response to Extended Aging from Pork Loins

2019 ◽  
Vol 3 (2) ◽  
Author(s):  
M. Chao ◽  
E. Donaldson ◽  
W. J. Wu ◽  
M. Shulte ◽  
S. Lonergan
Keyword(s):  
Shelf Life ◽  
Total Phospholipid ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Fatty Acyl Chain ◽  
Double Bonds ◽  
Aging Period ◽  
Extended Aging ◽  
Phospholipid Classes ◽  
Phospholipid Species

ObjectivesIt is well established that fresh meat shelf-life deteriorates during aging process. We hypothesize that part of the shelf-life reduction is due to membrane phospholipid deterioration through phospholipase activity and/or phospholipid oxidation during aging. Therefore, the objective of this study was to characterize the modifications/deterioration of phospholipid classes/species in pork loins from 3 different aging periods.Materials and MethodsLoins from 20 carcasses were collected at a commercial harvest facility in the Midwest 1 d postmortem from carcasses of Duroc sired crossbred pigs. Four chops from each carcass containing only the longissimus muscle were vacuum packaged and aged at 4°C for 1, 8, and 21 d. A sensitive approach based on electrospray ionization tandem mass spectrometry was used to comprehensively analyze phospholipid composition using the lipid extract from each sample at each aging period (n = 60). Unsaturation index (UI; measurement of the number of double bonds) for each phospholipid species class was also calculated to quantify fatty acyl chain unsaturation for each sample in each aging period.ResultsTotal phospholipid quantity in pork loins was not different between 1d and 8d aged chops but decreased significantly from 8d to 21d of aging (806.6 vs. 297.5 nmol phospholipid/mg lipid; P < 0.01). On the other hand, the mol% data (distribution of each phospholipid species in relative % of total phospholipid) revealed that phosphatidylinositol (PI) and phosphatidylserine (PS) increased in mol% from 1d to 21d of aging in pork loins (P < 0.01). This increase was mainly due to the increase of PI 38:4 (primarily 18:0/20:4) and PS 36:2 (primarily 18:0/18:2) between 1d and 21d samples (P < 0.01). The results showed that phospholipid degradation products like lysophosphatidylcholine (LPC) mol% rose quickly after short term aging (8d) but remained constant through the rest of the 21d aging period (P < 0.01). Conversely, lysophosphatidylethanolamine (LPE) was unaltered between 1d and 8d of aging but decreased between 8d and 21d aged pork loins (P < 0.01). The mol% of phosphatidic acid (PA) also increased between 1d and 21d aged pork loins (P < 0.05). Extended aging did not alter the mol% of total phosphatidylcholine (PC), ether-linked PC (ePC), sphingomyelin (SM), phosphatidylethanolamine (PE) or ether-linked PE (ePE; P > 0.05). Surprisingly, UI revealed the exact opposite trend as the mol% data. The UI of PI and PS decreased (P < 0.01) from 1d to 21 d of aging in pork loins due to the disappearance of many minor PI and PS species with very long chain fatty acids and multiple double bonds such as PI 42:10 and PS 44:10. There was also a slight increase of PC UI after 8 d of aging in pork loins (P < 0.01). The UI for LPC, ePC, SM, LPE, PE, ePE and total phospholipid were not altered in any of the aging periods (P > 0.05).ConclusionThese results confirmed our hypothesis that phospholipids undergo extensive degradation during aging. The data also indicated that the majority of phospholipids in pork loins may maintain integrity over short period aging (1–8d). Among the phospholipid classes, PI and PS were slightly more resistant to deterioration compared with the others due to their ability to modify fatty acyl chain saturation. Additional investigations are necessary to define the role of phospholipid modifications in fresh pork shelf-life and flavor.

scholarly journals Effects of diet on the function of sarcoplasmic reticulum

1987 ◽  
Vol 245 (3) ◽  
pp. 751-755 ◽  
Author(s):  
G W Gould ◽  
J M McWhirter ◽  
J M East ◽  
A G Lee
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Acyl Chain ◽  
Phospholipid Composition ◽  
Fatty Acyl ◽  
Fatty Acyl Chain ◽  
Rabbit Muscle ◽  
Phospholipid Classes ◽  
Chain Composition ◽  
Acyl Chain Composition ◽  
Uptake And Release

We have examined the effect of diet on the phospholipid composition of the sarcoplasmic reticulum of rabbit muscle. Enriching the diet with corn or fish oil results in significant changes in the fatty acyl chain composition of the various phospholipid classes, with relatively little change in the relative contents of the phospholipids. These alterations in composition have no significant effect on the ATPase activity of vesicles of sarcoplasmic reticulum or on the pattern of Ca2+ uptake and release.

Fatty acyl chain structure, orientational order, and the lipid phase transition in Acholeplasma laidlawii B membranes. A review of recent 19F nuclear magnetic resonance studies

1984 ◽  
Vol 62 (11) ◽  
pp. 1134-1150 ◽  
Author(s):  
P. M. Macdonald ◽  
B. D. Sykes ◽  
R. N. McElhaney
Keyword(s):  
Phase Transition ◽  
Fatty Acids ◽  
Nuclear Magnetic Resonance ◽  
Acyl Chain ◽  
Orientational Order ◽  
Membrane Lipid ◽  
Fatty Acyl ◽  
Fatty Acyl Chain ◽  
Lipid Phase ◽  
Lipid Phase Transition

The orientational order parameters of monofluoropalmitic acids biosynthetically incorporated into membranes of Acholeplasma laidlawii B in the presence of a large excess of a variety of structurally diverse fatty acids have been determined via 19F nuclear magnetic resonance (19F NMR) spectroscopy. It is demonstrated that these monofluoropalmitic acids are relatively nonperturbing membrane probes based upon physical (differential scanning calorimetry), biochemical (membrane lipid analysis), and biological (growth studies) criteria. 19F NMR is shown to convey the same qualitative and quantitative picture of membrane lipid order provided by 2H-NMR techniques and to be sensitive to the structural characteristics of the membrane fatty acyl chains, as well as to the lipid phase transition. Representatives of each naturally occurring class of fatty acyl chain structures, including straight-chain saturated, methyl-branched, monounsaturated, and alicyclic-ring-substituted fatty acids, were studied and the 19F-NMR order parameters were correlated with the lipid phase transitions (determined calorimetrically). The lipid phase transition was the prime determinant of overall orientational order regardless of fatty acid structure. Effects upon orientational order attributable to specific structural substituents were discernible, but were secondary to the effects of the lipid phase transition. In the gel state, relative overall order was directly proportional to the temperature of the particular lipid phase transition. Not only the overall order, but also the order profile across the membrane was sensitive to the presence of particular structural substituents. In particular, in the gel state specific fatty acyl structures demonstrated a characteristic disordering effect in the membrane order profile. These various observations can be merged to provide a unified picture of the manner in which fatty acyl chain chemistry modulates the physical state of membrane lipids.

scholarly journals The Role of Ceramide Metabolism and Signaling in the Regulation of Mitophagy and Cancer Therapy

Cancers ◽  
2021 ◽  
Vol 13 (10) ◽  
pp. 2475
Author(s):  
Megan Sheridan ◽  
Besim Ogretmen
Keyword(s):  
Cancer Therapy ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Fatty Acyl Chain ◽  
Cancer Cell Proliferation ◽  
Bioactive Lipids ◽  
Cellular Functions ◽  
Proliferation Response ◽  
Ceramide Synthases

Sphingolipids are bioactive lipids responsible for regulating diverse cellular functions such as proliferation, migration, senescence, and death. These lipids are characterized by a long-chain sphingosine backbone amide-linked to a fatty acyl chain with variable length. The length of the fatty acyl chain is determined by specific ceramide synthases, and this fatty acyl length also determines the sphingolipid’s specialized functions within the cell. One function in particular, the regulation of the selective autophagy of mitochondria, or mitophagy, is closely regulated by ceramide, a key regulatory sphingolipid. Mitophagy alterations have important implications for cancer cell proliferation, response to chemotherapeutics, and mitophagy-mediated cell death. This review will focus on the alterations of ceramide synthases in cancer and sphingolipid regulation of lethal mitophagy, concerning cancer therapy.

Effect of Acylglycerol Composition and Fatty Acyl Chain Length on Lipid Digestion in pH-Stat Digestion Model and SimulatedIn VitroDigestion Model

2015 ◽  
Vol 81 (2) ◽  
pp. C317-C323
Author(s):  
Jin F. Qi ◽  
Cai H. Jia ◽  
Jung A. Shin ◽  
Jeong M. Woo ◽  
Xiang Y. Wang ◽  
...  
Keyword(s):  
Chain Length ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Fatty Acyl Chain ◽  
Lipid Digestion ◽  
Acyl Chain Length ◽  
Ph Stat

scholarly journals Acyltransferase-mediated selection of the length of the fatty acyl chain and of the acylation site governs activation of bacterial RTX toxins

2020 ◽  
Vol 295 (28) ◽  
pp. 9268-9280 ◽  
Author(s):  
Adriana Osickova ◽  
Humaira Khaliq ◽  
Jiri Masin ◽  
David Jurnecka ◽  
Anna Sukova ◽  
...  
Keyword(s):  
Acyl Chain ◽  
Fatty Acyl ◽  
Biologically Active ◽  
Fatty Acyl Chain ◽  
Acyl Carrier Proteins ◽  
E Coli ◽  
Rtx Toxins ◽  
Wide Range ◽  
Lysine Residues ◽  
Acyl Chains

In a wide range of organisms, from bacteria to humans, numerous proteins have to be posttranslationally acylated to become biologically active. Bacterial repeats in toxin (RTX) cytolysins form a prominent group of proteins that are synthesized as inactive protoxins and undergo posttranslational acylation on ε-amino groups of two internal conserved lysine residues by co-expressed toxin-activating acyltransferases. Here, we investigated how the chemical nature, position, and number of bound acyl chains govern the activities of Bordetella pertussis adenylate cyclase toxin (CyaA), Escherichia coli α-hemolysin (HlyA), and Kingella kingae cytotoxin (RtxA). We found that the three protoxins are acylated in the same E. coli cell background by each of the CyaC, HlyC, and RtxC acyltransferases. We also noted that the acyltransferase selects from the bacterial pool of acyl–acyl carrier proteins (ACPs) an acyl chain of a specific length for covalent linkage to the protoxin. The acyltransferase also selects whether both or only one of two conserved lysine residues of the protoxin will be posttranslationally acylated. Functional assays revealed that RtxA has to be modified by 14-carbon fatty acyl chains to be biologically active, that HlyA remains active also when modified by 16-carbon acyl chains, and that CyaA is activated exclusively by 16-carbon acyl chains. These results suggest that the RTX toxin molecules are structurally adapted to the length of the acyl chains used for modification of their acylated lysine residue in the second, more conserved acylation site.

scholarly journals Ectopic expression of ceramide synthase 2 in neurons suppresses neurodegeneration induced by ceramide synthase 1 deficiency

2016 ◽  
Vol 113 (21) ◽  
pp. 5928-5933 ◽  
Author(s):  
Stefka D. Spassieva ◽  
Xiaojie Ji ◽  
Ye Liu ◽  
Kenneth Gable ◽  
Jacek Bielawski ◽  
...  
Keyword(s):  
Acyl Chain ◽  
Strong Association ◽  
Ectopic Expression ◽  
Fatty Acyl ◽  
Chemical Diversity ◽  
Fatty Acyl Chain ◽  
Length Variation ◽  
Ceramide Synthase ◽  
Hydrophobic Moiety

Sphingolipids exhibit extreme functional and chemical diversity that is in part determined by their hydrophobic moiety, ceramide. In mammals, the fatty acyl chain length variation of ceramides is determined by six (dihydro)ceramide synthase (CerS) isoforms. Previously, we and others showed that mutations in the major neuron-specific CerS1, which synthesizes 18-carbon fatty acyl (C18) ceramide, cause elevation of long-chain base (LCB) substrates and decrease in C18 ceramide and derivatives in the brain, leading to neurodegeneration in mice and myoclonus epilepsy with dementia in humans. Whether LCB elevation or C18 ceramide reduction leads to neurodegeneration is unclear. Here, we ectopically expressed CerS2, a nonneuronal CerS producing C22–C24 ceramides, in neurons of Cers1-deficient mice. Surprisingly, the Cers1 mutant pathology was almost completely suppressed. Because CerS2 cannot replenish C18 ceramide, the rescue is likely a result of LCB reduction. Consistent with this hypothesis, we found that only LCBs, the substrates common for all of the CerS isoforms, but not ceramides and complex sphingolipids, were restored to the wild-type levels in the Cers2-rescued Cers1 mutant mouse brains. Furthermore, LCBs induced neurite fragmentation in cultured neurons at concentrations corresponding to the elevated levels in the CerS1-deficient brain. The strong association of LCB levels with neuronal survival both in vivo and in vitro suggests high-level accumulation of LCBs is a possible underlying cause of the CerS1 deficiency-induced neuronal death.

Structure of Escherichia coli membranes. Fatty acyl chain order parameters of inner and outer membranes and derived liposomes

Biochemistry ◽  
1980 ◽  
Vol 19 (8) ◽  
pp. 1638-1643 ◽  
Author(s):  
Hans Ulrich Gally ◽  
Gerd Pluschke ◽  
Peter Overath ◽  
Joachim Seelig
Keyword(s):  
Escherichia Coli ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Order Parameters ◽  
Fatty Acyl Chain ◽  
Outer Membranes ◽  
Chain Order

Optimization of Phosphatidylserine-Modified Titanium Surfaces for Enhanced Osteoblast Response

2006 ◽  
Author(s):  
Neera Satsangi ◽  
Arpan Satsangi ◽  
Joo L. Ong ◽  
Rajiv V. Satsangi
Keyword(s):  
Alkaline Phosphatase ◽  
Protein Production ◽  
Specific Activity ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Separate Experiment ◽  
Calcium Deposition ◽  
Fatty Acyl Chain ◽  
Acyl Chain Length

This report is part of a continued effort to evaluate the in vitro osteoblast responses on different phospholipid coatings on Titanium (Ti) implant materials. It has been established that, among analogous phopholipids, the Ti surfaces coated with calcium phosphate (CaP) complex of phosphatidylserine induce the best calcium deposition and osteoblast growth and metabolism. This communication describes an effort to optimize the chemical structure of phosphatidylserine at its position−1 and −2, as Ti surface coating relative to enhancement in osteoblast differentiation and growth in culture. Four synthetic phosphatidylserine analogs with varying fatty acyl chain length and unsaturation were converted to CaP complex, coated on Ti discs, and the osteoblast progenitor cells were cultured on them for up to 14 days to study their differentiation, growth and biochemistry as marked by the expression of alkaline phosphatase specific activity and protein production. In a separate experiment, the topography of the glass surface (glass Petri-dishes) coated the analogous phosphatidylserines, after immersion in simulated body fluid, was examined by scanning electron microscopy (SEM). The presence of calcium and phosphate ions in this deposit was also confirmed. The inclusion of unsaturation in fatty acyl chain in phosphatidylserine enhanced the Total protein production (TPP) as well as the alkaline phosphatase (ALP) specific activity.

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