Editing Amyloid (section)

==Non-disease and functional amyloids==
Many examples of non-pathological amyloid with a well-defined physiological role have been identified in various organisms, including [[Homo sapiens|human]]. These may be termed as functional or physiological or native amyloid.<ref name="pmid18487849">{{cite journal | vauthors = Hammer ND, Wang X, McGuffie BA, Chapman MR | title = Amyloids: friend or foe? | journal = Journal of Alzheimer's Disease | volume = 13 | issue = 4 | pages = 407–19 | date = May 2008 | pmid = 18487849 | pmc = 2674399 | doi = 10.3233/JAD-2008-13406 | url = http://iospress.metapress.com/openurl.asp?genre=article&issn=1387-2877&volume=13&issue=4&spage=407 | url-status = dead | archive-url = https://archive.today/20130103210811/http://iospress.metapress.com/openurl.asp?genre=article&issn=1387-2877&volume=13&issue=4&spage=407 | archive-date = 2013-01-03 }}</ref><ref name="pmid17412596">{{cite journal | vauthors = Fowler DM, Koulov AV, Balch WE, Kelly JW | title = Functional amyloid--from bacteria to humans | journal = Trends in Biochemical Sciences | volume = 32 | issue = 5 | pages = 217–24 | date = May 2007 | pmid = 17412596 | doi = 10.1016/j.tibs.2007.03.003 }}</ref><ref name="pmid28498720"/>
* Functional amyloid in [[Homo sapiens|''Homo sapiens'']]:
** Intralumenal domain of melanocyte protein [[PMEL (gene)|PMEL]]<ref name="pmid16300414">{{cite journal | vauthors = Fowler DM, Koulov AV, Alory-Jost C, Marks MS, Balch WE, Kelly JW | title = Functional amyloid formation within mammalian tissue | journal = PLOS Biology | volume = 4 | issue = 1 | pages = e6 | date = January 2006 | pmid = 16300414 | pmc = 1288039 | doi = 10.1371/journal.pbio.0040006 | doi-access = free }}</ref>
** Peptide/protein hormones stored as amyloids within endocrine secretory granules<ref>{{cite journal | vauthors = Maji SK, Perrin MH, Sawaya MR, Jessberger S, Vadodaria K, Rissman RA, Singru PS, Nilsson KP, Simon R, Schubert D, Eisenberg D, Rivier J, Sawchenko P, Vale W, Riek R | display-authors = 6 | title = Functional amyloids as natural storage of peptide hormones in pituitary secretory granules | journal = Science | volume = 325 | issue = 5938 | pages = 328–32 | date = July 2009 | pmid = 19541956 | pmc = 2865899 | doi = 10.1126/science.1173155 | bibcode = 2009Sci...325..328M }}</ref>
** Receptor-interacting serine/threonine-protein kinase 1/3 ([[RIP1 (protein)|RIP1]]/[[RIP3]])<ref name="pmid22817896">{{cite journal | vauthors = Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H | display-authors = 6 | title = The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis | journal = Cell | volume = 150 | issue = 2 | pages = 339–50 | date = July 2012 | pmid = 22817896 | pmc = 3664196 | doi = 10.1016/j.cell.2012.06.019 }}</ref>
** Fragments of [[prostatic acid phosphatase]] and [[semenogelin]]s<ref name="pmid24691351">{{cite journal | vauthors = Usmani SM, Zirafi O, Müller JA, Sandi-Monroy NL, Yadav JK, Meier C, Weil T, Roan NR, Greene WC, Walther P, Nilsson KP, Hammarström P, Wetzel R, Pilcher CD, Gagsteiger F, Fändrich M, Kirchhoff F, Münch J | display-authors = 6 | title = Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen | journal = Nature Communications | volume = 5 | pages = 3508 | date = April 2014 | pmid = 24691351 | pmc = 4129123 | doi = 10.1038/ncomms4508 | bibcode = 2014NatCo...5.3508U }}</ref>
* Functional amyloid in other organisms:
** [[Pilus#Curli|Curli]] [[Fimbria (bacteriology)|fibrils]] produced by ''[[E. coli]],'' ''[[Salmonella]], ''and a few other members of the [[Enterobacteriales]] (Csg). The genetic elements ([[operons]]) encoding the curli system are phylogenetic widespread and can be found in at least four bacterial phyla.<ref>{{cite journal | vauthors = Dueholm MS, Albertsen M, Otzen D, Nielsen PH | title = Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure | journal = PLOS ONE | volume = 7 | issue = 12 | pages = e51274 | year = 2012 | pmid = 23251478 | pmc = 3521004 | doi = 10.1371/journal.pone.0051274 | veditors = Webber MA | bibcode = 2012PLoSO...751274D | doi-access = free }}</ref> This suggest that many more bacteria may express curli fibrils.
** GvpA, forming the walls of particular [[Gas vesicle]]s, i.e. the buoyancy organelles of aquatic archaea and eubacteria<ref>{{cite journal | vauthors = Bayro MJ, Daviso E, Belenky M, Griffin RG, Herzfeld J | title = An amyloid organelle, solid-state NMR evidence for cross-β assembly of gas vesicles | journal = The Journal of Biological Chemistry | volume = 287 | issue = 5 | pages = 3479–84 | date = January 2012 | pmid = 22147705 | pmc = 3271001 | doi = 10.1074/jbc.M111.313049 | doi-access = free }}</ref>
** Fap fibrils in various species of ''[[Pseudomonas]]''<ref>{{cite journal | vauthors = Dueholm MS, Petersen SV, Sønderkær M, Larsen P, Christiansen G, Hein KL, Enghild JJ, Nielsen JL, Nielsen KL, Nielsen PH, Otzen DE | display-authors = 6 | title = Functional amyloid in Pseudomonas | journal = Molecular Microbiology | volume = 77 | issue = 4 | pages = 1009–20 | date = August 2010 | pmid = 20572935 | doi = 10.1111/j.1365-2958.2010.07269.x | s2cid = 205368641 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Dueholm MS, Søndergaard MT, Nilsson M, Christiansen G, Stensballe A, Overgaard MT, Givskov M, Tolker-Nielsen T, Otzen DE, Nielsen PH | display-authors = 6 | title = Expression of Fap amyloids in Pseudomonas aeruginosa, P. fluorescens, and P. putida results in aggregation and increased biofilm formation | journal = MicrobiologyOpen | volume = 2 | issue = 3 | pages = 365–82 | date = June 2013 | pmid = 23504942 | pmc = 3684753 | doi = 10.1002/mbo3.81 }}</ref>
** Chaplins from ''[[Streptomyces coelicolor]]''<ref name="pmid12832396">{{cite journal | vauthors = Claessen D, Rink R, de Jong W, Siebring J, de Vreugd P, Boersma FG, Dijkhuizen L, Wosten HA | display-authors = 6 | title = A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils | journal = Genes & Development | volume = 17 | issue = 14 | pages = 1714–26 | date = July 2003 | pmid = 12832396 | pmc = 196180 | doi = 10.1101/gad.264303 }}</ref>
** [[Spidroin]] from ''[[Trichonephila edulis]]'' ([[spider]]) ([[Spider silk]])<ref name="pmid12180993">{{cite journal | vauthors = Kenney JM, Knight D, Wise MJ, Vollrath F | title = Amyloidogenic nature of spider silk | journal = European Journal of Biochemistry | volume = 269 | issue = 16 | pages = 4159–63 | date = August 2002 | pmid = 12180993 | doi = 10.1046/j.1432-1033.2002.03112.x | doi-access = free }}</ref>
** [[Hydrophobin]]s from [[Neurospora crassa]] and other fungi<ref name="pmid11250193">{{cite journal | vauthors = Mackay JP, Matthews JM, Winefield RD, Mackay LG, Haverkamp RG, Templeton MD | title = The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures | journal = Structure | volume = 9 | issue = 2 | pages = 83–91 | date = February 2001 | pmid = 11250193 | doi = 10.1016/s0969-2126(00)00559-1 | doi-access = free }}</ref>
** Fungal cell adhesion proteins forming cell surface amyloid regions with greatly increased binding strength<ref>{{cite journal | vauthors = Garcia MC, Lee JT, Ramsook CB, Alsteens D, Dufrêne YF, Lipke PN | title = A role for amyloid in cell aggregation and biofilm formation | journal = PLOS ONE | volume = 6 | issue = 3 | pages = e17632 | date = March 2011 | pmid = 21408122 | pmc = 3050909 | doi = 10.1371/journal.pone.0017632 | bibcode = 2011PLoSO...617632G | doi-access = free }}</ref><ref>{{cite journal | vauthors = Lipke PN, Garcia MC, Alsteens D, Ramsook CB, Klotz SA, Dufrêne YF | title = Strengthening relationships: amyloids create adhesion nanodomains in yeasts | journal = Trends in Microbiology | volume = 20 | issue = 2 | pages = 59–65 | date = February 2012 | pmid = 22099004 | pmc = 3278544 | doi = 10.1016/j.tim.2011.10.002 }}</ref>
** Environmental [[biofilm]]s according to staining with amyloid specific dyes and antibodies.<ref>{{cite journal | vauthors = Larsen P, Nielsen JL, Dueholm MS, Wetzel R, Otzen D, Nielsen PH | title = Amyloid adhesins are abundant in natural biofilms | journal = Environmental Microbiology | volume = 9 | issue = 12 | pages = 3077–90 | date = December 2007 | pmid = 17991035 | doi = 10.1111/j.1462-2920.2007.01418.x | bibcode = 2007EnvMi...9.3077L }}</ref>
** Tubular sheaths encasing [[Methanosaeta]] thermophila filaments<ref>{{cite journal | vauthors = Dueholm MS, Larsen P, Finster K, Stenvang MR, Christiansen G, Vad BS, Bøggild A, Otzen DE, Nielsen PH | display-authors = 6 | title = The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids | journal = The Journal of Biological Chemistry | volume = 290 | issue = 33 | pages = 20590–600 | date = August 2015 | pmid = 26109065 | pmc = 4536462 | doi = 10.1074/jbc.M115.654780 | doi-access = free }}</ref>
* Functional amyloid acting as prions
** Several [[yeast prions]] are based on an infectious amyloid, e.g. [PSI+] ([[Sup35p]]); [URE3] ([[Ure2p]]); [PIN+] or [RNQ+] (Rnq1p); [SWI1+] (Swi1p) and [OCT8+] (Cyc8p)
** Prion HET-s from ''[[Podospora anserina]]''<ref name="pmid9275200">{{cite journal | vauthors = Coustou V, Deleu C, Saupe S, Begueret J | title = The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 18 | pages = 9773–8 | date = September 1997 | pmid = 9275200 | pmc = 23266 | doi = 10.1073/pnas.94.18.9773 | bibcode = 1997PNAS...94.9773C | doi-access = free }}</ref>
** Neuron-specific isoform of CPEB from ''[[Aplysia californica]]'' (marine snail)<ref name="pmid14697205">{{cite journal | vauthors = Si K, Lindquist S, Kandel ER | title = A neuronal isoform of the aplysia CPEB has prion-like properties | journal = Cell | volume = 115 | issue = 7 | pages = 879–91 | date = December 2003 | pmid = 14697205 | doi = 10.1016/s0092-8674(03)01020-1 | s2cid = 3060439 | doi-access = free }}</ref>