Urokinase receptor: Difference between revisions

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Latest revision as of 21:18, 1 January 2019

The Urokinase receptor, also known as uPA receptor or uPAR or CD87 (Cluster of Differentiation 87), is a multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol (GPI) anchor. uPAR was originally identified as a saturable binding site for urokinase on the cell surface.

Molecular characteristics

uPAR consists of three different domains of the three-finger protein domain family, which also includes domains found in lymphocyte antigen 6 and in snake venom toxins of the three-finger toxin family, such as alpha-neurotoxins.^[1] All three three-finger domains are necessary for high affinity binding of the primary ligand, urokinase. It has been possible to express uPAR recombinantly in CHO-cells and S2 cells from Drosophila melanogaster. 4 out of 5 of the possible glycosylation sites are used in vivo giving the protein a molecular weight of 50-60 kDA. Recently the structure of uPAR was solved by X-ray crystallography in complex with a peptide antagonist^[2] and with its native ligand, urokinase.^[3]

Besides the primary ligand urokinase, uPAR interacts with several other proteins, among others: vitronectin, the uPAR associated protein (uPARAP) and the integrin family of membrane proteins.

Physiological significance

uPAR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. In order to be able to reorganize tissue, the old tissue must be able to be degraded. An important mechanism in this degradation is the proteolysis cascade initiated by the plasminogen activation system. uPAR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus uPAR seems to be an important player in the regulation of this process.

However the components of the plasminogen activation system have been found to be highly expressed in many malignant tumors, indicating that tumors are able to hijack the system, and use it in metastasis. Thus inhibitors of the various components of the plasminogen activation system have been sought as possible anticancer drugs.

uPAR has been involved in various other non-proteolytical processes related to cancer, such as cell migration, cell cycle regulation, and cell adhesion.

When uPA is bound to the receptor, there is cleavage between the GPI-anchor and the uPAR, releasing suPAR.^[4]

Interactions

Urokinase receptor has been shown to interact with LRP1.^[5]

References

↑ Kessler, Pascal; Marchot, Pascale; Silva, Marcela; Servent, Denis (August 2017). "The three-finger toxin fold: a multifunctional structural scaffold able to modulate cholinergic functions". Journal of Neurochemistry. 142: 7–18. doi:10.1111/jnc.13975.
↑ Llinas P, Le Du MH, Gårdsvoll H, Danø K, Ploug M, Gilquin B, Stura EA, Ménez A (May 2005). "Crystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptide". The EMBO Journal. 24 (9): 1655–63. doi:10.1038/sj.emboj.7600635. PMC 1142576. PMID 15861141.
↑ Huai Q, Mazar AP, Kuo A, Parry GC, Shaw DE, Callahan J, Li Y, Yuan C, Bian C, Chen L, Furie B, Furie BC, Cines DB, Huang M (February 2006). "Structure of human urokinase plasminogen activator in complex with its receptor". Science. 311 (5761): 656–9. doi:10.1126/science.1121143. PMID 16456079.
↑ Thunø M, Macho B, Eugen-Olsen J (2009). "suPAR: the molecular crystal ball". Disease Markers. 27 (3): 157–72. doi:10.3233/DMA-2009-0657. PMID 19893210.
↑ Czekay RP, Kuemmel TA, Orlando RA, Farquhar MG (May 2001). "Direct binding of occupied urokinase receptor (uPAR) to LDL receptor-related protein is required for endocytosis of uPAR and regulation of cell surface urokinase activity". Molecular Biology of the Cell. 12 (5): 1467–79. doi:10.1091/mbc.12.5.1467. PMC 34598. PMID 11359936.

External links

PLAUR+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

[kessler_2017-1] Kessler, Pascal; Marchot, Pascale; Silva, Marcela; Servent, Denis (August 2017). "The three-finger toxin fold: a multifunctional structural scaffold able to modulate cholinergic functions". Journal of Neurochemistry. 142: 7–18. doi:10.1111/jnc.13975.

[2] Llinas P, Le Du MH, Gårdsvoll H, Danø K, Ploug M, Gilquin B, Stura EA, Ménez A (May 2005). "Crystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptide". The EMBO Journal. 24 (9): 1655–63. doi:10.1038/sj.emboj.7600635. PMC 1142576. PMID 15861141.

[3] Huai Q, Mazar AP, Kuo A, Parry GC, Shaw DE, Callahan J, Li Y, Yuan C, Bian C, Chen L, Furie B, Furie BC, Cines DB, Huang M (February 2006). "Structure of human urokinase plasminogen activator in complex with its receptor". Science. 311 (5761): 656–9. doi:10.1126/science.1121143. PMID 16456079.

[4] Thunø M, Macho B, Eugen-Olsen J (2009). "suPAR: the molecular crystal ball". Disease Markers. 27 (3): 157–72. doi:10.3233/DMA-2009-0657. PMID 19893210.

[pmid11359936-5] Czekay RP, Kuemmel TA, Orlando RA, Farquhar MG (May 2001). "Direct binding of occupied urokinase receptor (uPAR) to LDL receptor-related protein is required for endocytosis of uPAR and regulation of cell surface urokinase activity". Molecular Biology of the Cell. 12 (5): 1467–79. doi:10.1091/mbc.12.5.1467. PMC 34598. PMID 11359936.

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[5]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+The '''Urokinase receptor''', also known as [[Urokinase|uPA]] receptor or uPAR or '''CD87''' ('''C'''luster of '''D'''ifferentiation '''87'''), is a multidomain [[glycoprotein]] tethered to the [[cell membrane]] with a [[GPI anchor|glycosylphosphotidylinositol]] (GPI) anchor. uPAR was originally identified as a saturable binding site for urokinase on the cell surface.
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = no
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB = {{PDB2|1ywh}}, {{PDB2|2fd6}}, {{PDB2|2i9b}}
- | Name = Plasminogen activator, urokinase receptor
- | HGNCid = 9053
- | Symbol = PLAUR
- | AltSymbols =; CD87; UPAR; URKR
- | OMIM = 173391
- | ECnumber =
- | Homologene = 48120
- | MGIid = 97612
- | GeneAtlas_image1 = PBB_GE_PLAUR_210845_s_at_tn.png
- | GeneAtlas_image2 = PBB_GE_PLAUR_211924_s_at_tn.png
- | GeneAtlas_image3 = PBB_GE_PLAUR_214866_at_tn.png
- | Function = {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0030377 |text = U-plasminogen activator receptor activity}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
- | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0019898 |text = extrinsic to membrane}}
- | Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0030162 |text = regulation of proteolysis}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 5329
-    | Hs_Ensembl = ENSG00000011422
-    | Hs_RefseqProtein = NP_001005376
-    | Hs_RefseqmRNA = NM_001005376
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 19
-    | Hs_GenLoc_start = 48842111
-    | Hs_GenLoc_end = 48866539
-    | Hs_Uniprot = Q03405
-    | Mm_EntrezGene = 18793
-    | Mm_Ensembl = ENSMUSG00000046223
-    | Mm_RefseqmRNA = NM_011113
-    | Mm_RefseqProtein = NP_035243
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 7
-    | Mm_GenLoc_start = 24171260
-    | Mm_GenLoc_end = 24184727
-    | Mm_Uniprot = Q3U2D1
-  }}
-}}
-The '''Urokinase receptor''', also known as [[Urokinase|uPA]] receptor or uPAR or '''CD87''' ('''C'''luster of '''D'''ifferentiation '''87'''), is multidomain [[glycoprotein]] tethered to the [[cell membrane]] with a [[glycosylphosphotidylinositol]] (GPI) anchor. uPAR was originally identified as a saturable binding site for urokinase on the cell surface.
 == Molecular characteristics ==
-uPAR consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. All three domains are necessary for high affinity binding of the primary ligand, urokinase. It has been possible to express uPAR recombinantly in [[Chinese Hamster Ovary cell|CHO-cell]]s and [[S2]] cells from ''[[Drosophila melanogaster]]''. 4 out of 5 of the possible [[glycosylation]] sites are used in vivo giving the [[protein]] a [[molecular weight]] of 50-60 kDA. Recently the structure of uPAR was solved by [[X-ray crystallography]] in complex with an [[peptide]] [[receptor antagonist|antagonist]]<ref>Crystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptide. Llinas P, Le Du MH, Gardsvoll H, Dano K, Ploug M, Gilquin B, Stura EA, Menez A. EMBO J. 2005 May 4;24(9):1655-63. Epub 2005 Apr 7. (full text article online: {{Entrez Pubmed|15861141}}).</ref> and with its native ligand, urokinase<ref>Structure of human urokinase plasminogen activator in complex with its receptor. Huai Q, Mazar AP, Kuo A, Parry GC, Shaw DE, Callahan J, Li Y, Yuan C, Bian C, Chen L, Furie B, Furie BC, Cines DB, Huang M., Science. 2006 Feb 3;311(5761):656-9. {{Entrez Pubmed|16456079}}).</ref>.
+uPAR consists of three different [[protein domain|domains]] of the [[three-finger protein]] domain family, which also includes domains found in [[LY6|lymphocyte antigen 6]] and in [[snake venom]] toxins of the [[three-finger toxin]] family, such as [[alpha-neurotoxin]]s.<ref name="kessler_2017">{{cite journal |last1=Kessler |first1=Pascal |last2=Marchot |first2=Pascale |last3=Silva |first3=Marcela |last4=Servent |first4=Denis |title=The three-finger toxin fold: a multifunctional structural scaffold able to modulate cholinergic functions |journal=Journal of Neurochemistry |date=August 2017 |volume=142 |pages=7–18 |doi=10.1111/jnc.13975}}</ref> All three three-finger domains are necessary for high affinity binding of the primary ligand, urokinase. It has been possible to express uPAR recombinantly in [[Chinese Hamster Ovary cell|CHO-cell]]s and [[Schneider 2 cells|S2]] cells from ''[[Drosophila melanogaster]]''. 4 out of 5 of the possible [[glycosylation]] sites are used in vivo giving the [[protein]] a [[molecular weight]] of 50-60 kDA. Recently the structure of uPAR was solved by [[X-ray crystallography]] in complex with a [[peptide]] [[receptor antagonist|antagonist]]<ref>{{cite journal | vauthors = Llinas P, Le Du MH, Gårdsvoll H, Danø K, Ploug M, Gilquin B, Stura EA, Ménez A | title = Crystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptide | journal = The EMBO Journal | volume = 24 | issue = 9 | pages = 1655–63 | date = May 2005 | pmid = 15861141 | pmc = 1142576 | doi = 10.1038/sj.emboj.7600635 }}</ref> and with its native ligand, urokinase.<ref>{{cite journal | vauthors = Huai Q, Mazar AP, Kuo A, Parry GC, Shaw DE, Callahan J, Li Y, Yuan C, Bian C, Chen L, Furie B, Furie BC, Cines DB, Huang M | title = Structure of human urokinase plasminogen activator in complex with its receptor | journal = Science | volume = 311 | issue = 5761 | pages = 656–9 | date = February 2006 | pmid = 16456079 | doi = 10.1126/science.1121143 | url = http://www.sciencemag.org/cgi/pmidlookup?view=short&pmid=16456079 }}</ref>
 Besides the primary [[ligand]] [[urokinase]], uPAR interacts with several other [[proteins]], among others: [[vitronectin]], the uPAR associated protein ([[uPARAP]]) and the [[integrin]] family of [[membrane proteins]].
 == Physiological significance ==
-uPAR is a part of the [[plasminogen activation system]], which in the healthy body is involved in tissue reorganization events such as [[mammary gland]] involution and [[wound healing]]. In order to be able to reorganize tissue it is important, that the old tissue can be degraded. An important mechanism in this degradation is the [[proteolysis]] cascade initiated by the [[plasminogen activation system]]. uPAR binds [[urokinase]] and thus restricts [[plasminogen]] activation to the immediate vicinity of the [[cell membrane]]. Thus uPAR seems to be an important player in the regulation of this process.
+uPAR is a part of the [[plasminogen]] activation system, which in the healthy body is involved in tissue reorganization events such as [[mammary gland]] involution and [[wound healing]]. In order to be able to reorganize tissue, the old tissue must be able to be degraded. An important mechanism in this degradation is the [[proteolysis]] cascade initiated by the plasminogen activation system. uPAR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus uPAR seems to be an important player in the regulation of this process.
-However the components of the [[plasminogen activation system]] have been found to be highly expressed in many [[malignant]] [[tumor]]s, indicating that tumors are able to [[wiktionary:Hijack|hijack]] the system, and use it in [[metastasis]]. Thus [[Enzyme inhibitor|inhibitor]]s of the various components of the plasminogen activation system has been sought as possible anticancer drugs.
+However the components of the plasminogen activation system have been found to be highly expressed in many [[malignant]] [[tumor]]s, indicating that tumors are able to hijack the system, and use it in [[metastasis]]. Thus [[Enzyme inhibitor|inhibitor]]s of the various components of the plasminogen activation system have been sought as possible anticancer drugs.
-uPAR has been involved in various other non-proteolytical processes related to cancer, such as [[cell migration]], [[cell cycle]] regulation and cell adhesion.
+uPAR has been involved in various other non-proteolytical processes related to cancer, such as [[cell migration]], [[cell cycle]] regulation, and cell adhesion.
+When uPA is bound to the receptor, there is cleavage between the GPI-anchor and the uPAR, releasing [[suPAR]].<ref>{{cite journal | vauthors = Thunø M, Macho B, Eugen-Olsen J | title = suPAR: the molecular crystal ball | journal = Disease Markers | volume = 27 | issue = 3 | pages = 157–72 | year = 2009 | pmid = 19893210 | doi = 10.3233/DMA-2009-0657 | url = http://iospress.metapress.com/openurl.asp?genre=article&issn=0278-0240&volume=27&issue=3&spage=157 }}</ref>
+== Interactions ==
+Urokinase receptor has been shown to [[Protein-protein interaction|interact]] with [[LRP1]].<ref name=pmid11359936>{{cite journal | vauthors = Czekay RP, Kuemmel TA, Orlando RA, Farquhar MG | title = Direct binding of occupied urokinase receptor (uPAR) to LDL receptor-related protein is required for endocytosis of uPAR and regulation of cell surface urokinase activity | journal = Molecular Biology of the Cell | volume = 12 | issue = 5 | pages = 1467–79 | date = May 2001 | pmid = 11359936 | pmc = 34598 | doi = 10.1091/mbc.12.5.1467 }}</ref>
 == See also ==
@@ Line 69: / Line 27: @@
 * [[Plasminogen activation system]]
 * [[Urokinase]]
+* [[suPAR]]
 == References ==
-{{reflist|2}}
+{{reflist}}
-==Further reading==
+== Further reading ==
 {{refbegin | 2}}
-*Structure-Function Relationships in the Interaction Between the Urokinase-Type Plasminogen Activator and its Receptor. Ploug, M. Curr Pharm Des. 2003;9(19):1499-528. PMID 12871065.
+* {{cite journal | vauthors = Ploug M | title = Structure-function relationships in the interaction between the urokinase-type plasminogen activator and its receptor | journal = Current Pharmaceutical Design | volume = 9 | issue = 19 | pages = 1499–528 | year = 2003 | pmid = 12871065 | doi = 10.2174/1381612033454630 | url = http://www.benthamdirect.org/pages/content.php?CPD/2003/00000009/00000019/0003B.SGM }}
-{{PBB_Further_reading
+* {{cite journal | vauthors = Kjøller L | title = The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility | journal = Biological Chemistry | volume = 383 | issue = 1 | pages = 5–19 | date = January 2002 | pmid = 11928822 | doi = 10.1515/BC.2002.002 }}
-| citations =
+* {{cite journal | vauthors = Chavakis T, Kanse SM, May AE, Preissner KT | title = Haemostatic factors occupy new territory: the role of the urokinase receptor system and kininogen in inflammation | journal = Biochemical Society Transactions | volume = 30 | issue = 2 | pages = 168–73 | date = April 2002 | pmid = 12023845 | doi = 10.1042/BST0300168 }}
-*{{cite journal  | author=Kjøller L |title=The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility. |journal=Biol. Chem. |volume=383 |issue= 1 |pages= 5-19 |year= 2003 |pmid= 11928822 |doi=  }}
+* {{cite journal | vauthors = Ploug M, Gårdsvoll H, Jørgensen TJ, Lønborg Hansen L, Danø K | title = Structural analysis of the interaction between urokinase-type plasminogen activator and its receptor: a potential target for anti-invasive cancer therapy | journal = Biochemical Society Transactions | volume = 30 | issue = 2 | pages = 177–83 | date = April 2002 | pmid = 12023847 | doi = 10.1042/BST0300177 }}
-*{{cite journal  | author=Chavakis T, Kanse SM, May AE, Preissner KT |title=Haemostatic factors occupy new territory: the role of the urokinase receptor system and kininogen in inflammation. |journal=Biochem. Soc. Trans. |volume=30 |issue= 2 |pages= 168-73 |year= 2002 |pmid= 12023845 |doi= 10.1042/ }}
+* {{cite journal | vauthors = Alfano M, Sidenius N, Blasi F, Poli G | title = The role of urokinase-type plasminogen activator (uPA)/uPA receptor in HIV-1 infection | journal = Journal of Leukocyte Biology | volume = 74 | issue = 5 | pages = 750–6 | date = November 2003 | pmid = 12960238 | doi = 10.1189/jlb.0403176 }}
-*{{cite journal  | author=Ploug M, Gårdsvoll H, Jørgensen TJ, ''et al.'' |title=Structural analysis of the interaction between urokinase-type plasminogen activator and its receptor: a potential target for anti-invasive cancer therapy. |journal=Biochem. Soc. Trans. |volume=30 |issue= 2 |pages= 177-83 |year= 2002 |pmid= 12023847 |doi= 10.1042/ }}
+* {{cite journal | vauthors = Alfano D, Franco P, Vocca I, Gambi N, Pisa V, Mancini A, Caputi M, Carriero MV, Iaccarino I, Stoppelli MP | title = The urokinase plasminogen activator and its receptor: role in cell growth and apoptosis | journal = Thrombosis and Haemostasis | volume = 93 | issue = 2 | pages = 205–11 | date = February 2005 | pmid = 15711734 | doi = 10.1160/TH04-09-0592 }}
-*{{cite journal  | author=Alfano M, Sidenius N, Blasi F, Poli G |title=The role of urokinase-type plasminogen activator (uPA)/uPA receptor in HIV-1 infection. |journal=J. Leukoc. Biol. |volume=74 |issue= 5 |pages= 750-6 |year= 2004 |pmid= 12960238 |doi= 10.1189/jlb.0403176 }}
-*{{cite journal  | author=Alfano D, Franco P, Vocca I, ''et al.'' |title=The urokinase plasminogen activator and its receptor: role in cell growth and apoptosis. |journal=Thromb. Haemost. |volume=93 |issue= 2 |pages= 205-11 |year= 2005 |pmid= 15711734 |doi= 10.1267/THRO05020205 }}
-}}
 {{refend}}
-==External links==
+== External links ==
 * {{MeshName|PLAUR+protein,+human}}
+{{PDB Gallery|geneid=5329}}
 {{Clusters of differentiation}}
 [[Category:Clusters of differentiation]]
-{{WikiDoc Sources}}

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1-50	CD1 a-c 1A 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51-100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101-150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151-200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201-250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251-300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301-350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

Urokinase receptor: Difference between revisions

Latest revision as of 21:18, 1 January 2019

Contents

Molecular characteristics

Physiological significance

Interactions

See also

References

Further reading

External links

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