plasmalogen

Glycerophospholipids of biochemical relevance are divided into three subclasses based on the substitution present at the sn-1 position of the glycerol backbone: acyl, alkyl and alkenyl.{{cite journal |vauthors=Yamashita S, Honjo A, Aruga M, Nakagawa K, Miyazawa T |date=2014 |title=Preparation of marine plasmalogen and selective identification of molecular species by LC-MS/MS |journal=J Oleo Sci |volume=63 |issue=5 |pages=423–30 |doi=10.5650/jos.ess13188 |pmid=24717546 |doi-access=free}} Of these, the alkyl and alkenyl moiety in each case form an ether bond, which makes for two types of ether phospholipids, plasmanyl (alkyl moiety at sn-1), and plasmenyl (alkenyl moiety with vinyl ether linkage at sn-1). Plasmalogens are plasmenyls with an ester (acyl group) linked lipid at the sn-2 position of the glycerol backbone,{{cite journal |vauthors=Wallner S, Schmitz G |date=September 2011 |title=Plasmalogens the neglected regulatory and scavenging lipid species |journal=Chem Phys Lipids |volume=164 |issue=6 |pages=573–89 |doi=10.1016/j.chemphyslip.2011.06.008 |pmid=21723266}}{{cite journal |vauthors=Hu C, Wang M, Han X |date=August 2017 |title=Shotgun lipidomics in substantiating lipid peroxidation in redox biology: Methods and applications |journal=Redox Biol |volume=12 |issue= |pages=946–955 |doi=10.1016/j.redox.2017.04.030 |pmc=5423350 |pmid=28494428}} chemically designated 1-0(1Z-alkenyl)-2-acyl-glycerophospholipids.{{cite journal |vauthors=Braverman NE, Moser AB |date=September 2012 |title=Functions of plasmalogen lipids in health and disease |journal=Biochim Biophys Acta |volume=1822 |issue=9 |pages=1442–52 |doi=10.1016/j.bbadis.2012.05.008 |pmid=22627108}} The lipid attached to the vinyl ether at sn-1 can be C16:0, C18:0, or C18:1 (saturated and monounsaturated), and the lipid attached to the acyl group at sn-2 can be C22:6 ω-3 (docosahexaenoic acid) or C20:4 ω-6 (arachidonic acid), (both are polyunsaturated acids).{{cite journal |vauthors=Fuchs B |date=May 2015 |title=Analytical methods for (oxidized) plasmalogens: Methodological aspects and applications |journal=Free Radic Res |volume=49 |issue=5 |pages=599–617 |doi=10.3109/10715762.2014.999675 |pmid=25536419 |s2cid=5443009}} Plasmalogens are classified according to their head group, mainly as PC plasmalogens (plasmenylcholines) and PE plasmalogens (plasmenylethalomines).{{cite journal |vauthors=Maeba R, Nishimukai M, Sakasegawa S, Sugimori D, Hara H |date=2015 |title=Plasma/Serum Plasmalogens: Methods of Analysis and Clinical Significance |journal=Adv Clin Chem |volume=70 |issue= |pages=31–94 |doi=10.1016/bs.acc.2015.03.005 |pmid=26231485 |doi-access=free}}{{Cite journal |last1=Messias |first1=Márcia Cristina Fernandes |last2=Mecatti |first2=Giovana Colozza |last3=Priolli |first3=Denise Gonçalves |last4=De Oliveira Carvalho |first4=Patrícia |year=2018 |title=Plasmalogen lipids: Functional mechanism and their involvement in gastrointestinal cancer |journal=Lipids in Health and Disease |volume=17 |issue=1 |page=41 |doi=10.1186/s12944-018-0685-9 |pmc=5842581 |pmid=29514688 |doi-access=free}} Plasmalogens should not be confused with plasmanyls.

Plasmalogens are found in numerous human tissues, with particular enrichment in the nervous, immune, and cardiovascular systems. In human heart tissue, nearly 30–40% of choline glycerophospholipids are plasmalogens. Even more striking is the fact that 32% of the glycerophospholipids in the adult human heart and 20% in brain and up to 70% of myelin sheath ethanolamine glycerophospholipids are plasmalogens.{{Cite journal

| last1 = Farooqui | first1 = A. A.

| last2 = Horrocks | first2 = L. A.

| title = Plasmalogens: Workhorse lipids of membranes in normal and injured neurons and glia

| journal = The Neuroscientist

| volume = 7

| issue = 3

| pages = 232–245

| year = 2001

| pmid = 11499402

| doi=10.1177/107385840100700308

| s2cid = 85868497

}}

Although the functions of plasmalogens have not yet been fully elucidated, it has been demonstrated that they can protect mammalian cells against the damaging effects of reactive oxygen species. In addition, they have been implicated as being signaling molecules and modulators of membrane dynamics.

Plasmalogens were first described by Feulgen and Voit in 1924 based on studies of tissue sections. They treated these tissue sections with acid or mercuric chloride as part of a method to stain the nucleus. This resulted in the breakage of the plasmalogen vinyl-ether bond to yield aldehydes. In turn, the latter reacted with a fuchsine-sulfurous acid stain used in this nuclear staining method and gave rise to colored compounds inside the cytoplasm of the cells. Plasmalogens were named based on the fact that these colored compounds were present in the "plasmal" or inside of the cell.

File:Plasmalogen-synthesis-pathway.png

Biosynthesis of plasmalogens begins with association of peroxisomal matrix enzymes GNPAT (glycerone phosphate acyl transferase) and AGPS (alkyl-glycerone phosphate synthase)

on the luminal side of the peroxisomal membrane.{{cite journal |vauthors=Brites P, Waterham HR, Wanders RJ |title=Functions and biosynthesis of plasmalogens in health and disease |journal=Biochim Biophys Acta |volume=1636 |issue=2–3 |pages=219–31 |date=March 2004 |pmid=15164770 |doi=10.1016/j.bbalip.2003.12.010 }}

These two enzymes can interact with each other to increase efficiency. Therefore, fibroblasts without AGPS activity have a reduced GNPAT level and activity.{{cite journal |vauthors=Biermann J, Just WW, Wanders RJ, Van Den Bosch H |title=Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes |journal=Eur J Biochem |volume=261 |issue=2 |pages=492–9 |date=April 1999 |pmid=10215861 |doi=10.1046/j.1432-1327.1999.00295.x |doi-access=free }}{{cite journal |vauthors=Hardeman D, van den Bosch H |title=Topography of ether phospholipid biosynthesis |journal=Biochim Biophys Acta |volume=1006 |issue=1 |pages=1–8 |date=November 1989 |pmid=2804060 |doi=10.1016/0005-2760(89)90315-9 }}

The first step of the biosynthesis is catalyzed by GNPAT. This enzyme acylates dihydroxyacetone phosphate at the sn-1 position. This is followed by the exchange of the acyl group for an alkyl group by AGPS.{{cite journal |vauthors=Brown AJ, Snyder F |title=Alkyldihydroxyacetone-P synthase. Solubilization, partial purification, new assay method, and evidence for a ping-pong mechanism |journal=J Biol Chem |volume=257 |issue=15 |pages=8835–9 |date=August 1982 |doi=10.1016/S0021-9258(18)34205-4 |pmid=7096336 |doi-access=free }}

The 1-alkyl-DHAPdihydroxyacetone phosphate is then reduced to 1-O-alkyl-2-hydroxy-sn-glycerophosphate (GPA) by an acyl/alkyl-dihydroxyacetone phosphate reductase located in both peroxisomal and endoplasmatic reticulum membranes.{{cite journal |vauthors=James PF, Lake AC, Hajra AK, Larkins LK, Robinson M, Buchanan FG, Zoeller RA |title=An animal cell mutant with a deficiency in acyl/alkyl-dihydroxyacetone-phosphate reductase activity. Effects on the biosynthesis of ether-linked and diacyl glycerolipids |journal=J Biol Chem |volume=272 |issue=38 |pages=23540–6 |date=September 1997 |pmid=9295290 |doi=10.1074/jbc.272.38.23540 |doi-access= free}}

All other modifications occur in the endoplasmatic reticulum. There an acyl group is placed at the sn-2 position by an alkyl/acyl GPA acyltransferase and the phosphate group is removed by a phosphatidic acid phosphatase to form 1-O-alkyl-2-acyl-sn-glycerol.

Using CDP-ethanolamine a phosphotransferase forms 1-O-alkyl-2-acyl-sn-GPEtn. After dehydrogenation at the 1- and 2-positions of the

alkyl group by an electron transport system and plasmanylethanolamine desaturase the vinyl ether bond of plasmalogens is finally formed. The protein corresponding to plasmanylethanolamine desaturase has been identified and is called CarF in bacteria and PEDS1 (TMEM189) in humans (and animals).{{cite journal |vauthors=Gallego-García A, Monera-Girona AJ, Pajares-Martínez E, Bastida-Martínez E, Pérez-Castaño R, Iniesta AA, Fontes M, Padmanabhan S, Elías-Arnanz M |title=A bacterial light response reveals an orphan desaturase for human plasmalogen synthesis |date=2019 |journal=Science |volume=366 |issue=6461 |pages=128–132 |doi=10.1126/science.aay1436 |pmid=31604315|bibcode=2019Sci...366..128G |s2cid=203717749 |doi-access=free }}{{cite journal |last1=Werner |first1=ER |last2=Keller |first2=MA |last3=Sailer |first3=S |last4=Lackner |first4=K |last5=Koch |first5=J |last6=Hermann |first6=M |last7=Coassin |first7=S |last8=Golderer |first8=G |last9=Werner-Felmayer |first9=G |last10=Zoeller |first10=RA |last11=Hulo |first11=N |last12=Berger |first12=J |last13=Watschinger |first13=K |title=The TMEM189 gene encodes plasmanylethanolamine desaturase which introduces the characteristic vinyl ether double bond into plasmalogens. |journal=Proceedings of the National Academy of Sciences of the United States of America |date=7 April 2020 |volume=117 |issue=14 |pages=7792–7798 |doi=10.1073/pnas.1917461117 |pmid=32209662|pmc=7149458 |doi-access=free |bibcode=2020PNAS..117.7792W }}

Plasmenylcholine is formed from 1-O-alkyl-2-acyl-sn-glycerol by choline phosphotransferase. As there is no plasmenylcholine desaturase choline plasmalogens can be formed only after hydrolysis of ethanolamine plasmalogens to 1-O-(1Z-alkenyl)-2-acyl-sn-glycerol that can be modified by choline phosphotransferase and CDP choline.{{cite journal |vauthors=Lee TC |title=Biosynthesis and possible biological functions of plasmalogens |journal=Biochim Biophys Acta |volume=1394 |issue=2–3 |pages=129–45 |date=November 1998 |pmid=9795186 |doi=10.1016/s0005-2760(98)00107-6 }}{{cite journal|last1=Braverman|first1=NE|last2=Moser|first2=AB|title=Functions of plasmalogen lipids in health and disease.|journal=Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease|date=September 2012|volume=1822|issue=9|pages=1442–52|doi=10.1016/j.bbadis.2012.05.008|pmid=22627108|doi-access=}}

Peroxisome biogenesis disorders are autosomal recessive disorders often characterized by impaired plasmalogen biosynthesis. In these cases, the peroxisomal enzyme GNPAT, necessary for the initial steps of plasmalogen biosynthesis, is mislocalized to the cytoplasm where it is inactive. In addition, genetic mutations in the GNPAT or AGPS genes can result in plasmalogen deficiencies, which lead to the development of rhizomelic chondrodysplasia punctata (RCDP) type 2 or 3, respectively.{{Cite journal

| last1 = Wanders | first1 = R.

| last2 = Waterham | first2 = H.

| title = Peroxisomal disorders: the single peroxisomal enzyme deficiencies

| journal = Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

| volume = 1763

| issue = 12

| pages = 1707–20

| year = 2006

| doi = 10.1016/j.bbamcr.2006.08.010

| pmid=17055078

| doi-access = free

}} In such cases, both copies of the GNPAT or AGPS gene must be mutated in order for disease to manifest. Unlike the peroxisome biogenesis disorders, other aspects of peroxisome assembly in RCDP2 and RCDP3 patients are normal as is their ability to metabolize very long chain fatty acids. Individuals with severe plasmalogen deficiencies frequently show abnormal neurological development, skeletal malformation, impaired respiration, and cataracts.

{{cite journal |vauthors=Braverman NE, Steinberg SJ, Fallatah W, et al |veditors=Adam MP, Ardinger HH, Pagon RA, et al |title=Rhizomelic Chondrodysplasia Punctata Type 1 |journal=GeneReviews® [Internet] |publisher=University of Washington |id=NBK1270 |pmid=20301447 |date=2020 |url=https://www.ncbi.nlm.nih.gov/books/NBK1270/}}

Deficits in plasmalogen levels contribute to pathology in Zellweger syndrome.

Plasmalogen-knockout mice show similar alterations like arrest of spermatogenesis, development of cataract and defects in central nervous system myelination.{{cite journal |vauthors=Rodemer C, Thai TP, Brugger B, Kaercher T, Werner H, Nave KA, Wieland F, Gorgas K, Just WW |title=Inactivation of ether lipid biosynthesis causes male infertility, defects in eye development and optic nerve hypoplasia in mice |journal=Hum Mol Genet |volume=12 |issue=15 |pages=1881–95 |date=August 2003 |pmid=12874108 |doi=10.1093/hmg/ddg191 |doi-access=free }}

Plasmalogen alkyl chains have been shown to promote or inhibit the cell death from ferroptosis, depending on their degree of saturation.{{Cite journal|last1=Zou|first1=Yilong|last2=Henry|first2=Whitney S.|last3=Ricq|first3=Emily L.|last4=Graham|first4=Emily T.|last5=Phadnis|first5=Vaishnavi V.|last6=Maretich|first6=Pema|last7=Paradkar|first7=Sateja|last8=Boehnke|first8=Natalie|last9=Deik|first9=Amy A.|last10=Reinhardt|first10=Ferenc|last11=Eaton|first11=John K.|date=September 2020|title=Plasticity of ether lipids promotes ferroptosis susceptibility and evasion|journal=Nature|volume=585|issue=7826|pages=603–8|doi=10.1038/s41586-020-2732-8 |pmc=8051864|pmid=32939090|bibcode=2020Natur.585..603Z}}{{cite journal |vauthors=Xin S, Mueller C, Pfeiffer S, Kraft VA, Merl-Pham J, Bao X, Feederle R, Jin X, Hauck SM, Schmitt-Kopplin P, Schick JA |title=MS4A15 drives ferroptosis resistance through calcium-restricted lipid remodeling |journal=Cell Death Differ |volume=29 |issue=3 |pages=670–686 |date=March 2022 |pmid=34663908 |doi=10.1038/s41418-021-00883-z |pmc=8901757 |s2cid=239025829 }}

During inflammation, neutrophil-derived myeloperoxidase produces hypochlorous acid, which causes oxidative chlorination of plasmalogens at the sn-1 chain by reacting with the vinyl ether bond.{{Cite journal|last1=Albert|first1=Carolyn J.|last2=Crowley|first2=Jan R.|last3=Hsu|first3=Fong-Fu|last4=Thukkani|first4=Arun K.|last5=Ford|first5=David A.|date=2001-06-29|title=Reactive Chlorinating Species Produced by Myeloperoxidase Target the Vinyl Ether Bond of Plasmalogens IDENTIFICATION OF 2-CHLOROHEXADECANAL|journal=Journal of Biological Chemistry|language=en|volume=276|issue=26|pages=23733–41|doi=10.1074/jbc.M101447200 |pmid=11301330|doi-access=free}} Several researchers are currently investigating the impact of chlorinated lipids on pathology.

The lack of good methods to assay plasmalogen has created difficulties for scientists to assess how plasmalogen might be involved in human diseases other than RCDP and Zellweger spectrum, in which the involvement is certain. There is some evidence in humans that low plasmalogens are involved in the pathology of bronchopulmonary dysplasia, which is an important complication of premature birth. One study showed that plasmalogen levels are reduced in people with COPD who smoked compared with non-smokers.

There is some evidence from humans and animals that there are reduced levels of plasmalogens in the brain in neurodegenerative disorders including Alzheimer disease, Parkinson's disease, Niemann–Pick disease, type C, Down syndrome, and multiple sclerosis, it is not clear if this is causal or correlative. A study with mice concluded that plasmalogens can eliminate aging-associated synaptic defects.{{Cite journal |title=Plasmalogens Eliminate Aging-Associated Synaptic Defects and Microglia-Mediated Neuroinflammation in Mice |journal=Front. Mol. Biosci. |year=2022 |doi=10.3389/fmolb.2022.815320|doi-access=free |last1=Gu |first1=Jinxin |last2=Chen |first2=Lixue |last3=Sun |first3=Ran |last4=Wang |first4=Jie-Li |last5=Wang |first5=Juntao |last6=Lin |first6=Yingjun |last7=Lei |first7=Shuwen |last8=Zhang |first8=Yang |last9=Lv |first9=Dan |last10=Jiang |first10=Faqin |last11=Deng |first11=Yuru |last12=Collman |first12=James P. |last13=Fu |first13=Lei |volume=9 |page=815320 |pmid=35281262 |pmc=8906368 }}

More recently, population studies have also associated lower circulating plasmalogen levels with cardiometabolic disease. {{Cite journal |last1=Meikle |first1=Peter J. |last2=Wong |first2=Gerard |last3=Barlow |first3=Christopher K. |last4=Weir |first4=Jacquelyn M. |last5=Greeve |first5=Melissa A. |last6=MacIntosh |first6=Gemma L. |last7=Almasy |first7=Laura |last8=Comuzzie |first8=Anthony G. |last9=Mahaney |first9=Michael C. |last10=Kowalczyk |first10=Adam |last11=Haviv |first11=Izhac |last12=Grantham |first12=Narelle |last13=Magliano |first13=Dianna J. |last14=Jowett |first14=Jeremy B. M. |last15=Zimmet |first15=Paul |date=2013-09-27 |editor-last=Maya-Monteiro |editor-first=Clarissa Menezes |title=Plasma Lipid Profiling Shows Similar Associations with Prediabetes and Type 2 Diabetes |journal=PLOS ONE |language=en |volume=8 |issue=9 |pages=e74341 |doi=10.1371/journal.pone.0074341 |doi-access=free |issn=1932-6203 |pmc=3785490 |pmid=24086336|bibcode=2013PLoSO...874341M }}{{Cite journal |last1=Meikle |first1=Peter J. |last2=Wong |first2=Gerard |last3=Tsorotes |first3=Despina |last4=Barlow |first4=Christopher K. |last5=Weir |first5=Jacquelyn M. |last6=Christopher |first6=Michael J. |last7=MacIntosh |first7=Gemma L. |last8=Goudey |first8=Benjamin |last9=Stern |first9=Linda |last10=Kowalczyk |first10=Adam |last11=Haviv |first11=Izhak |last12=White |first12=Anthony J. |last13=Dart |first13=Anthony M. |last14=Duffy |first14=Stephen J. |last15=Jennings |first15=Garry L. |date=November 2011 |title=Plasma Lipidomic Analysis of Stable and Unstable Coronary Artery Disease |url=https://www.ahajournals.org/doi/10.1161/ATVBAHA.111.234096 |journal=Arteriosclerosis, Thrombosis, and Vascular Biology |language=en |volume=31 |issue=11 |pages=2723–2732 |doi=10.1161/ATVBAHA.111.234096 |issn=1079-5642}}{{Cite journal |last1=Sutter |first1=Iryna |last2=Klingenberg |first2=Roland |last3=Othman |first3=Alaa |last4=Rohrer |first4=Lucia |last5=Landmesser |first5=Ulf |last6=Heg |first6=Dierik |last7=Rodondi |first7=Nicolas |last8=Mach |first8=Francois |last9=Windecker |first9=Stephan |last10=Matter |first10=Christian M. |last11=Lüscher |first11=Thomas F. |last12=von Eckardstein |first12=Arnold |last13=Hornemann |first13=Thorsten |date=March 2016 |title=Decreased phosphatidylcholine plasmalogens – A putative novel lipid signature in patients with stable coronary artery disease and acute myocardial infarction |url=https://linkinghub.elsevier.com/retrieve/pii/S002191501630003X |journal=Atherosclerosis |language=en |volume=246 |pages=130–140 |doi=10.1016/j.atherosclerosis.2016.01.003|pmid=26773473 }}{{Cite journal |last1=Tonks |first1=Katherine T. |last2=Coster |first2=Adelle CF |last3=Christopher |first3=Michael J. |last4=Chaudhuri |first4=Rima |last5=Xu |first5=Aimin |last6=Gagnon-Bartsch |first6=Johann |last7=Chisholm |first7=Donald J. |last8=James |first8=David E. |last9=Meikle |first9=Peter J. |last10=Greenfield |first10=Jerry R. |last11=Samocha-Bonet |first11=Dorit |date=April 2016 |title=Skeletal muscle and plasma lipidomic signatures of insulin resistance and overweight/obesity in humans |journal=Obesity |language=en |volume=24 |issue=4 |pages=908–916 |doi=10.1002/oby.21448 |issn=1930-7381 |pmc=6585800 |pmid=26916476}} Animal studies have also demonstrated lower cardiac plasmalogen levels under settings of dilated cardiomyopathy{{Cite journal |last1=Tham |first1=Yow Keat |last2=Huynh |first2=Kevin |last3=Mellett |first3=Natalie A. |last4=Henstridge |first4=Darren C. |last5=Kiriazis |first5=Helen |last6=Ooi |first6=Jenny Y.Y. |last7=Matsumoto |first7=Aya |last8=Patterson |first8=Natalie L. |last9=Sadoshima |first9=Junichi |last10=Meikle |first10=Peter J. |last11=McMullen |first11=Julie R. |date=March 2018 |title=Distinct lipidomic profiles in models of physiological and pathological cardiac remodeling, and potential therapeutic strategies |url=https://linkinghub.elsevier.com/retrieve/pii/S1388198117302366 |journal=Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids |language=en |volume=1863 |issue=3 |pages=219–234 |doi=10.1016/j.bbalip.2017.12.003|pmid=29217479 }}{{Cite journal |last=Belkin |first=Teleah G. |last2=Masterman |first2=Emma I. |last3=Yildiz |first3=Gunes S. |last4=Kiriazis |first4=Helen |last5=Mellett |first5=Natalie A. |last6=Cross |first6=Jonathon |last7=Grigolon |first7=Kyah |last8=Dogra |first8=Akshima |last9=Donner |first9=Daniel |last10=Chooi |first10=Roger |last11=Liang |first11=Amy |last12=Kompa |first12=Andrew R. |last13=Sadoshima |first13=Junichi |last14=Edgley |first14=Amanda J. |last15=Greening |first15=David W. |date=2025-03-01 |title=An optimized plasmalogen modulating dietary supplement provides greater protection in a male than female mouse model of dilated cardiomyopathy |url=https://linkinghub.elsevier.com/retrieve/pii/S2772976124000631 |journal=Journal of Molecular and Cellular Cardiology Plus |volume=11 |pages=100273 |doi=10.1016/j.jmccpl.2024.100273 |issn=2772-9761|doi-access=free |pmc=11708127 }} and myocardial infarction.{{Cite journal |last1=Montero-Bullon |first1=Javier-Fernando |last2=Aveiro |first2=Susana S. |last3=Melo |first3=Tânia |last4=Martins-Marques |first4=Tânia |last5=Lopes |first5=Diana |last6=Neves |first6=Bruna |last7=Girão |first7=Henrique |last8=Rosário M Domingues |first8=M. |last9=Domingues |first9=Pedro |date=September 2021 |title=Cardiac phospholipidome is altered during ischemia and reperfusion in an ex vivo rat model |journal=Biochemistry and Biophysics Reports |language=en |volume=27 |pages=101037 |doi=10.1016/j.bbrep.2021.101037 |pmc=8207217 |pmid=34169155}}

In addition to mammals, plasmalogens are also found in invertebrates and single cell organisms protozoans. Among bacteria they have been found in many anaerobic species including Clostridia, Megasphaera, and Veillonella. Among aerobic bacteria, plasmalogens occur in myxobacteria, and their plasmanylethanolamine desaturase (CarF) required to generate the vinyl ether bond, and hence plasmalogen, is conserved as TMEM189 in humans (and animals). Plasmalogens have been shown to have a complex evolutionary history based on the fact that their biosynthetic pathways differ in aerobic and anaerobic organisms.{{Cite journal

| last1 = Goldfine | first1 = H.

| title = The appearance, disappearance and reappearance of plasmalogens in evolution

| doi = 10.1016/j.plipres.2010.07.003

| journal = Progress in Lipid Research

| volume = 49

| issue = 4

| pages = 493–498

| year = 2010

| pmid = 20637230

| url = https://zenodo.org/record/1197344

}}

Recently, it has been demonstrated that the red blood cells of humans and great apes (chimpanzees, gorillas and orangutans) have differences in their plasmalogen composition. Total RBC plasmalogen levels were found to be lower in humans than in chimpanzees, or gorillas, but higher than in orangutans. Gene expression data from all these species caused the authors to speculate that other human and great ape cells and tissues differ in plasmalogen levels. Although the consequences of these potential differences are unknown, cross-species differences in tissue plasmalogens could influence organ functions and multiple biological processes.

Plasmalogens form a major component in the cell membranes of deep-sea animals like the comb jelly, enhancing molecular resistance to high pressure.{{Cite journal |last=Winnikoff |first=Jacob R. |last2=Milshteyn |first2=Daniel |last3=Vargas-Urbano |first3=Sasiri J. |last4=Pedraza-Joya |first4=Miguel A. |last5=Armando |first5=Aaron M. |last6=Quehenberger |first6=Oswald |last7=Sodt |first7=Alexander |last8=Gillilan |first8=Richard E. |last9=Dennis |first9=Edward A. |last10=Lyman |first10=Edward |last11=Haddock |first11=Steven H. D. |last12=Budin |first12=Itay |date=2024-06-28 |title=Homeocurvature adaptation of phospholipids to pressure in deep-sea invertebrates |url=https://www.science.org/doi/10.1126/science.adm7607 |journal=Science |language=en |volume=384 |issue=6703 |pages=1482–1488 |doi=10.1126/science.adm7607 |issn=0036-8075|pmc=11593575 }}

• Ether lipid

{{Reflist}}

• {{MeshName|Plasmalogens}}

{{Phospholipids}}

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