View source for Luteinizing hormone/choriogonadotropin receptor

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{{Short description|Transmembrane receptor found in humans}}
{{Infobox gene}}

The '''luteinizing hormone/choriogonadotropin receptor''' ('''LHCGR'''), also '''lutropin/choriogonadotropin receptor''' ('''LCGR''') or '''luteinizing hormone receptor''' ('''LHR'''), is a [[transmembrane receptor]] found predominantly in the [[ovary]] and [[testis]], but also many extragonadal organs such as the [[uterus]] and [[breast]]s. The receptor interacts with both [[luteinizing hormone]] (LH) and chorionic gonadotropins (such as [[Human chorionic gonadotropin|hCG]] in humans) and represents a [[G protein-coupled receptor]] (GPCR). Its activation is necessary for the hormonal functioning during reproduction.

== LHCGR gene ==
The [[Human genetics|gene]] for the LHCGR is found on [[chromosome 2]] p21 in humans, close to the [[FSH receptor]] gene. It consists of 70&nbsp;kbp (versus 54&nbsp;kpb for the FSHR).<ref name="FSHR">{{cite journal | vauthors = Simoni M, Gromoll J, Nieschlag E | title = The follicle-stimulating hormone receptor: biochemistry, molecular biology, physiology, and pathophysiology | journal = Endocrine Reviews | volume = 18 | issue = 6 | pages = 739–773 | date = December 1997 | pmid = 9408742 | doi = 10.1210/edrv.18.6.0320 | doi-access = free }}</ref> The gene is similar to the gene for the FSH receptor and the TSH receptor.

== Receptor structure ==
The LHCGR consists of 674 amino acids and has a molecular mass of about 85–95&nbsp;kDA based on the extent of glycosylation.<ref name="LHCGR">{{cite journal | vauthors = Ascoli M, Fanelli F, Segaloff DL | title = The lutropin/choriogonadotropin receptor, a 2002 perspective | journal = Endocrine Reviews | volume = 23 | issue = 2 | pages = 141–174 | date = April 2002 | pmid = 11943741 | doi = 10.1210/edrv.23.2.0462 | doi-access = free }}</ref>

Like other GPCRs, the LHCG receptor possess seven membrane-spanning domains or [[transmembrane helix|transmembrane helices]].<ref name="pmid9558473">{{cite journal | vauthors = Dufau ML | title = The luteinizing hormone receptor | journal = Annual Review of Physiology | volume = 60 | pages = 461–496 | year = 1998 | pmid = 9558473 | doi = 10.1146/annurev.physiol.60.1.461 }}</ref> The extracellular domain  of the receptor is heavily  [[Glycosylation|glycosylated]]. These transmembrane domains contain two highly conserved [[cysteine]] residues, which build [[disulfide bond]]s to stabilize the receptor structure. The transmembrane part is highly homologous with other members of the rhodopsin family of GPCRs.<ref name="pmid24001578">{{cite journal | vauthors = Jiang X, Dias JA, He X | title = Structural biology of glycoprotein hormones and their receptors: insights to signaling | journal = Molecular and Cellular Endocrinology | volume = 382 | issue = 1 | pages = 424–451 | date = January 2014 | pmid = 24001578 | doi = 10.1016/j.mce.2013.08.021 | doi-access = free }}</ref>  The C-terminal domain is intracellular and brief, rich in [[serine]] and [[threonine]] residues for possible [[phosphorylation]].

== Ligand binding and signal transduction ==
Upon binding of LH to the external part of the membrane spanning receptor, a [[signal transduction|transduction of the signal]] takes place. This process results in the activation of a [[heterotrimeric G protein]]. Binding of LH to the receptor shifts its [[Chemical conformation|conformation]]. The activated receptor promotes the binding of [[Guanosine triphosphate|GTP]] to the G protein and its subsequent activation. After binding GTP, the G protein heterotrimer detaches from the receptor and disassembles. The alpha-subunit Gs binds [[adenylate cyclase]] and activates the [[Cyclic adenosine monophosphate|cAMP]] system.<ref name="pmid9833610">{{cite journal | vauthors = Ryu KS, Gilchrist RL, Koo YB, Ji I, Ji TH | title = Gene, interaction, signal generation, signal divergence and signal transduction of the LH/CG receptor | journal = International Journal of Gynaecology and Obstetrics | volume = 60 | issue = Suppl 1 | pages = S9-20 | date = April 1998 | pmid = 9833610 | doi = 10.1016/S0020-7292(98)80001-5 | s2cid = 4798893 }}</ref>

It is believed that a receptor molecule exists in a conformational equilibrium between active and inactive states. The binding of LH (or CG) to the receptor shifts the equilibrium towards the active form of the receptor. For a cell to respond to LH only a small percentage (≈1%) of receptor sites need to be activated.

=== Phosphorylation by cAMP-dependent protein kinases ===
Cyclic AMP-dependent protein kinases ([[protein kinase A]]) are activated by the signal cascade originated by the activation of the G protein Gs by the LHCG-receptor. Activated Gs binds the enzyme adenylate cyclase and this leads to the production of [[cyclic AMP]] (cAMP). Cyclin AMP-dependent protein kinases are present as [[tetrameric protein|tetramer]]s with two regulatory subunits and two catalytic subunits. Upon binding of cAMP to the regulatory subunits, the catalytic units are released and initiate the phosphorylation of proteins leading to the physiologic action. Cyclic AMP is degraded by [[phosphodiesterase]] and release 5’AMP. One of the targets of protein kinase A is the Cyclic AMP Response Element Binding Protein, [[CREB]], which binds [[DNA]] in the [[cell nucleus]] via direct interactions with specific DNA sequences called [[cyclic AMP response element]]s (CRE); this process results in the activation or inactivation of [[gene transcription]].<ref name="FSHR" />

The signal is amplified by the involvement of cAMP and the resulting phosphorylation. The process is modified by [[prostaglandin]]s. Other cellular regulators that participate are the intracellular calcium concentration regulated by [[phospholipase C]] activation, [[nitric oxide]], and other growth factors.

Other pathways of signaling exist for the LHCGR.<ref name="LHCGR" />

== Action ==
[[File:Steroidogenesis.svg|thumb|Luteinizing hormone up-regulates cholesterol side chain cleaving enzyme in sensitive tissues, the first step of all human steroidogenesis. |389x389px]]The LHCG receptor's main function is the regulation of [[steroidogenesis]]. This is accomplished by increasing the intracellular levels of the enzyme [[Cholesterol side-chain cleavage enzyme|cholesterol side chain cleaving enzyme]], a member of the [[cytochrome P450]] family. This leads to increased conversion of cholesterol into androgen precursors required to make many steroid hormones, including testosterone and estrogens.<ref>{{cite journal | vauthors = Dufau ML, Cigorraga S, Baukal AJ, Sorrell S, Bator JM, Neubauer JF, Catt KJ | title = Androgen biosynthesis in Leydig cells after testicular desensitization by luteinizing hormone-releasing hormone and human chorionic gonadotropin | journal = Endocrinology | volume = 105 | issue = 6 | pages = 1314–1321 | date = December 1979 | pmid = 227658 | doi = 10.1210/endo-105-6-1314 }}</ref>

=== Ovary ===
In the ovary, the LHCG receptor is necessary for follicular maturation and ovulation, as well as luteal function. Its  expression requires appropriate hormonal stimulation by [[Follicle-stimulating hormone|FSH]] and [[estradiol]]. The LHCGR is present on [[granulosa cells]], [[theca]] cells, [[luteal]] cells, and interstitial cells<ref name="LHCGR"/> The LCGR is restimulated by increasing levels of [[chorionic gonadotropin]]s in case a [[pregnancy]] is developing. In turn, luteal function is prolonged and the endocrine milieu is supportive of the nascent pregnancy.

=== Testis ===
In the male the LHCGR has been identified on the [[Leydig cell]]s that are critical for [[testosterone]] production, and  support [[spermatogenesis]].

Normal LHCGR functioning is critical for male fetal development, as the fetal Leydig cells produce androstenedione which is converted to testosterone in fetal Sertoli cells to induce masculinization.

=== Extragonadal ===
LHCGR have been found in many types of extragonadal tissues, and the physiologic role of some has remained largely unexplored. Thus receptors have been found in the [[uterus]], [[sperm]], [[seminal vesicles]], [[prostate]], [[skin]], [[breast]], [[adrenal]]s, [[thyroid]], neural [[retina]], [[neuroendocrine]] cells, and (rat) [[brain]].<ref name="LHCGR"/><!--section: III. Expression of the LHR-->

== Receptor regulation ==
[[Image:7TM receptor.png|thumb|326x326px|The seven transmembrane α-helix structure of a G protein-coupled receptor such as LHCGR]]

=== Upregulation ===
[[Upregulation]] refers to the increase in the number of receptor sites on the membrane. Estrogen and FSH upregulate LHCGR sites in preparation for [[ovulation]]. After ovulation, the luteinized ovary  maintains LHCGR s that allow activation in case there is an implantation. Upregulation in males requires gene transcription to synthesize LH receptors within the cell cytoplasm. Some reasons as to why downregulated LH receptors are not upregulated are: lack of gene transcription, lack of RNA to protein conversion and lack of cell membrane targeted shipments from Golgi.

=== Desensitization ===
The LHCGRs become desensitized when exposed to LH  for some time.  A key reaction of this downregulation is the [[phosphorylation]] of the intracellular (or [[cytoplasm]]ic) receptor domain by [[protein kinase]]s. This process uncouples Gs protein from the LHCGR.

=== Downregulation ===
[[Downregulation]] refers to the decrease in the number of receptor molecules. This is usually the result of receptor [[endocytosis]]. In this process, the bound LCGR-hormone complex binds [[arrestin]] and concentrates in [[clathrin coated pit]]s. Clathrin coated pits recruit [[dynamin]] and pinch off from the cell surface, becoming [[clathrin-coated vesicle]]s.  Clathrin-coated vesicles are processed into [[endosome]]s, some of which are recycled to the cell surface while others are targeted to [[lysosomes]]. Receptors targeted to lysosomes are degraded. Use of long-acting agonists will downregulate the receptor population by promoting their endocytosis.

=== Modulators ===
Antibodies to LHCGR can interfere with LHCGR activity.

== LHCGR antagonists and agonists ==
In 2019, the discovery of potent, and selective antagonists of the Luteinizing Hormone Receptor (BAY-298 and BAY-899) were reported which were able to reduce sex hormone levels ''in vivo''.<ref>{{cite journal | vauthors = Wortmann L, Lindenthal B, Muhn P, Walter A, Nubbemeyer R, Heldmann D, Sobek L, Morandi F, Schrey AK, Moosmayer D, Günther J, Kuhnke J, Koppitz M, Lücking U, Röhn U, Schäfer M, Nowak-Reppel K, Kühne R, Weinmann H, Langer G | title = Discovery of BAY-298 and BAY-899: Tetrahydro-1,6-naphthyridine-Based, Potent, and Selective Antagonists of the Luteinizing Hormone Receptor Which Reduce Sex Hormone Levels in Vivo | journal = Journal of Medicinal Chemistry | volume = 62 | issue = 22 | pages = 10321–10341 | date = November 2019 | pmid = 31670515 | doi = 10.1021/acs.jmedchem.9b01382 | s2cid = 204967109 | doi-access = free }}</ref> The latter fulfils the quality criteria for a 'Donated Chemical Probe' as defined by the [[Structural Genomics Consortium]].<ref>{{Cite web |title=Donated Chemical Probes |url=https://www.thesgc.org/donated-chemical-probes |website=thesgc.org |access-date=July 31, 2023}}</ref>

A series of thienopyr(im)idine-based compounds<ref>{{cite journal | vauthors = van Straten NC, Schoonus-Gerritsma GG, van Someren RG, Draaijer J, Adang AE, Timmers CM, Hanssen RG, van Boeckel CA | title = The first orally active low molecular weight agonists for the LH receptor: thienopyr(im)idines with therapeutic potential for ovulation induction | journal = ChemBioChem | volume = 3 | issue = 10 | pages = 1023–1026 | date = October 2002 | pmid = 12362369 | doi = 10.1002/1439-7633(20021004)3:10<1023::AID-CBIC1023>3.0.CO;2-9 | s2cid = 8732411 }}</ref> leading to optimized Org 43553 were described as the first Luteinizing Hormone Receptor agonists.<ref>{{cite journal | vauthors = Heitman LH, Oosterom J, Bonger KM, Timmers CM, Wiegerinck PH, Ijzerman AP | title = [3H]Org 43553, the first low-molecular-weight agonistic and allosteric radioligand for the human luteinizing hormone receptor | journal = Molecular Pharmacology | volume = 73 | issue = 2 | pages = 518–524 | date = February 2008 | pmid = 17989351 | doi = 10.1124/mol.107.039875 | hdl-access = free | s2cid = 34584880 | hdl = 1887/3209412 }}</ref><ref>{{cite journal | vauthors = van de Lagemaat R, Timmers CM, Kelder J, van Koppen C, Mosselman S, Hanssen RG | title = Induction of ovulation by a potent, orally active, low molecular weight agonist (Org 43553) of the luteinizing hormone receptor | journal = Human Reproduction | volume = 24 | issue = 3 | pages = 640–648 | date = March 2009 | pmid = 19088107 | doi = 10.1093/humrep/den412 | doi-access = free }}</ref>

== LHCGR abnormalities ==
Loss-of-function mutations in females can lead to [[infertility]]. In 46, XY individuals severe inactivation can cause male [[pseudohermaphroditism]], as fetal Leydig cells during may not respond and thus interfere with masculinization.<ref name="pmid10714363">{{cite journal | vauthors = Wu SM, Chan WY | title = Male pseudohermaphroditism due to inactivating luteinizing hormone receptor mutations | journal = Archives of Medical Research | volume = 30 | issue = 6 | pages = 495–500 | year = 1999 | pmid = 10714363 | doi = 10.1016/S0188-4409(99)00074-0 | doi-access = free }}</ref> Less severe inactivation can result in [[hypospadias]] or a [[micropenis]].<ref name="LHCGR"/>

== History ==
[[Alfred G. Gilman]]  and [[Martin Rodbell]] received the 1994 [[Nobel Prize in Medicine and Physiology]] for the discovery of the G Protein System.

==Interactions ==
Luteinizing hormone/choriogonadotropin receptor has been shown to [[Protein-protein interaction|interact]] with [[GIPC1]].<ref name=pmid14507927>{{cite journal | vauthors = Hirakawa T, Galet C, Kishi M, Ascoli M | title = GIPC binds to the human lutropin receptor (hLHR) through an unusual PDZ domain binding motif, and it regulates the sorting of the internalized human choriogonadotropin and the density of cell surface hLHR | journal = The Journal of Biological Chemistry | volume = 278 | issue = 49 | pages = 49348–49357 | date = December 2003 | pmid = 14507927 | doi = 10.1074/jbc.M306557200 | doi-access = free }}</ref>

== References ==
{{Reflist|2}}

== Further reading ==
{{refbegin | 2}}
* {{cite journal | vauthors = Ji TH, Ryu KS, Gilchrist R, Ji I | title = Interaction, signal generation, signal divergence, and signal transduction of LH/CG and the receptor | journal = Recent Progress in Hormone Research | volume = 52 | pages = 431–53; discussion 454 | year = 1997 | pmid = 9238862 }}
* {{cite journal | vauthors = Dufau ML | title = The luteinizing hormone receptor | journal = Annual Review of Physiology | volume = 60 | pages = 461–496 | year = 1998 | pmid = 9558473 | doi = 10.1146/annurev.physiol.60.1.461 }}
* {{cite journal | vauthors = Ascoli M, Fanelli F, Segaloff DL | title = The lutropin/choriogonadotropin receptor, a 2002 perspective | journal = Endocrine Reviews | volume = 23 | issue = 2 | pages = 141–174 | date = April 2002 | pmid = 11943741 | doi = 10.1210/edrv.23.2.0462 | doi-access = free }}
* {{cite journal | vauthors = Amsterdam A, Hanoch T, Dantes A, Tajima K, Strauss JF, Seger R | title = Mechanisms of gonadotropin desensitization | journal = Molecular and Cellular Endocrinology | volume = 187 | issue = 1–2 | pages = 69–74 | date = February 2002 | pmid = 11988313 | doi = 10.1016/S0303-7207(01)00701-8 | s2cid = 23625847 }}
* {{cite journal | vauthors = Fanelli F, Puett D | title = Structural aspects of luteinizing hormone receptor: information from molecular modeling and mutagenesis | journal = Endocrine | volume = 18 | issue = 3 | pages = 285–293 | date = August 2002 | pmid = 12450321 | doi = 10.1385/ENDO:18:3:285 | s2cid = 24739956 | hdl = 11380/584273 | hdl-access = free }}
* {{cite journal | vauthors = Latronico AC, Segaloff DL | title = Insights learned from L457(3.43)R, an activating mutant of the human lutropin receptor | journal = Molecular and Cellular Endocrinology | volume = 260-262 | pages = 287–293 | date = January 2007 | pmid = 17055147 | pmc = 1785107 | doi = 10.1016/j.mce.2005.11.053 }}
* {{cite journal | vauthors = Nagayama Y, Russo D, Wadsworth HL, Chazenbalk GD, Rapoport B | title = Eleven amino acids (Lys-201 to Lys-211) and 9 amino acids (Gly-222 to Leu-230) in the human thyrotropin receptor are involved in ligand binding | journal = The Journal of Biological Chemistry | volume = 266 | issue = 23 | pages = 14926–14930 | date = August 1991 | pmid = 1651314 | doi = 10.1016/S0021-9258(18)98566-2 | doi-access = free }}
* {{cite journal | vauthors = Jia XC, Oikawa M, Bo M, Tanaka T, Ny T, Boime I, Hsueh AJ | title = Expression of human luteinizing hormone (LH) receptor: interaction with LH and chorionic gonadotropin from human but not equine, rat, and ovine species | journal = Molecular Endocrinology | volume = 5 | issue = 6 | pages = 759–768 | date = June 1991 | pmid = 1922095 | doi = 10.1210/mend-5-6-759 | doi-access = free }}
* {{cite journal | vauthors = Minegishi T, Nakamura K, Takakura Y, Miyamoto K, Hasegawa Y, Ibuki Y, Igarashi M, Minegishi T | title = Cloning and sequencing of human LH/hCG receptor cDNA | journal = Biochemical and Biophysical Research Communications | volume = 172 | issue = 3 | pages = 1049–1054 | date = November 1990 | pmid = 2244890 | doi = 10.1016/0006-291X(90)91552-4 | author8 = Minegish T [corrected to Minegishi T }}
* {{cite journal | vauthors = Rousseau-Merck MF, Misrahi M, Atger M, Loosfelt H, Milgrom E, Berger R | title = Localization of the human luteinizing hormone/choriogonadotropin receptor gene (LHCGR) to chromosome 2p21 | journal = Cytogenetics and Cell Genetics | volume = 54 | issue = 1–2 | pages = 77–79 | year = 1991 | pmid = 2249480 | doi = 10.1159/000132962 }}
* {{cite journal | vauthors = Xie YB, Wang H, Segaloff DL | title = Extracellular domain of lutropin/choriogonadotropin receptor expressed in transfected cells binds choriogonadotropin with high affinity | journal = The Journal of Biological Chemistry | volume = 265 | issue = 35 | pages = 21411–21414 | date = December 1990 | pmid = 2254302 | doi = 10.1016/S0021-9258(18)45750-X | doi-access = free }}
* {{cite journal | vauthors = Frazier AL, Robbins LS, Stork PJ, Sprengel R, Segaloff DL, Cone RD | title = Isolation of TSH and LH/CG receptor cDNAs from human thyroid: regulation by tissue specific splicing | journal = Molecular Endocrinology | volume = 4 | issue = 8 | pages = 1264–1276 | date = August 1990 | pmid = 2293030 | doi = 10.1210/mend-4-8-1264 | hdl-access = free | doi-access = free | hdl = 21.11116/0000-0000-7844-D }}
* {{cite journal | vauthors = Keutmann HT, Charlesworth MC, Mason KA, Ostrea T, Johnson L, Ryan RJ | title = A receptor-binding region in human choriogonadotropin/lutropin beta subunit | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 7 | pages = 2038–2042 | date = April 1987 | pmid = 3470775 | pmc = 304579 | doi = 10.1073/pnas.84.7.2038 | doi-access = free | bibcode = 1987PNAS...84.2038K }}
* {{cite journal | vauthors = Jiang X, Dreano M, Buckler DR, Cheng S, Ythier A, Wu H, Hendrickson WA, el Tayar N | title = Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions | journal = Structure | volume = 3 | issue = 12 | pages = 1341–1353 | date = December 1995 | pmid = 8747461 | doi = 10.1016/S0969-2126(01)00272-6 | doi-access = free }}
* {{cite journal | vauthors = Atger M, Misrahi M, Sar S, Le Flem L, Dessen P, Milgrom E | title = Structure of the human luteinizing hormone-choriogonadotropin receptor gene: unusual promoter and 5' non-coding regions | journal = Molecular and Cellular Endocrinology | volume = 111 | issue = 2 | pages = 113–123 | date = June 1995 | pmid = 7556872 | doi = 10.1016/0303-7207(95)03557-N | s2cid = 25479294 }}
* {{cite journal | vauthors = Latronico AC, Anasti J, Arnhold IJ, Mendonça BB, Domenice S, Albano MC, Zachman K, Wajchenberg BL, Tsigos C | title = A novel mutation of the luteinizing hormone receptor gene causing male gonadotropin-independent precocious puberty | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 80 | issue = 8 | pages = 2490–2494 | date = August 1995 | pmid = 7629248 | doi = 10.1210/jcem.80.8.7629248 }}
* {{cite journal | vauthors = Shenker A, Laue L, Kosugi S, Merendino JJ, Minegishi T, Cutler GB | title = A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty | journal = Nature | volume = 365 | issue = 6447 | pages = 652–654 | date = October 1993 | pmid = 7692306 | doi = 10.1038/365652a0 | s2cid = 4307732 | bibcode = 1993Natur.365..652S }}
* {{cite journal | vauthors = Yano K, Saji M, Hidaka A, Moriya N, Okuno A, Kohn LD, Cutler GB | title = A new constitutively activating point mutation in the luteinizing hormone/choriogonadotropin receptor gene in cases of male-limited precocious puberty | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 80 | issue = 4 | pages = 1162–1168 | date = April 1995 | pmid = 7714085 | doi = 10.1210/jcem.80.4.7714085 }}
* {{cite journal | vauthors = Kremer H, Kraaij R, Toledo SP, Post M, Fridman JB, Hayashida CY, van Reen M, Milgrom E, Ropers HH, Mariman E | title = Male pseudohermaphroditism due to a homozygous missense mutation of the luteinizing hormone receptor gene | journal = Nature Genetics | volume = 9 | issue = 2 | pages = 160–164 | date = February 1995 | pmid = 7719343 | doi = 10.1038/ng0295-160 | hdl-access = free | s2cid = 8678536 | hdl = 2066/20602 }}
* {{cite journal | vauthors = Kosugi S, Van Dop C, Geffner ME, Rabl W, Carel JC, Chaussain JL, Mori T, Merendino JJ, Shenker A | title = Characterization of heterogeneous mutations causing constitutive activation of the luteinizing hormone receptor in familial male precocious puberty | journal = Human Molecular Genetics | volume = 4 | issue = 2 | pages = 183–188 | date = February 1995 | pmid = 7757065 | doi = 10.1093/hmg/4.2.183 }}
* {{cite journal | vauthors = Kremer H, Mariman E, Otten BJ, Moll GW, Stoelinga GB, Wit JM, Jansen M, Drop SL, Faas B, Ropers HH | title = Cosegregation of missense mutations of the luteinizing hormone receptor gene with familial male-limited precocious puberty | journal = Human Molecular Genetics | volume = 2 | issue = 11 | pages = 1779–1783 | date = November 1993 | pmid = 8281137 | doi = 10.1093/hmg/2.11.1779 }}
{{refend}}

== External links ==
* {{cite web | url = http://www.iuphar-db.org/GPCR/ReceptorDisplayForward?receptorID=2987 | title = Glycoprotein Hormone Receptors: LH | work = IUPHAR Database of Receptors and Ion Channels | publisher = International Union of Basic and Clinical Pharmacology | access-date = 2006-07-20 | archive-date = 2021-01-18 | archive-url = https://web.archive.org/web/20210118042810/https://www.iuphar-db.org/GPCR/ReceptorDisplayForward?receptorID=2987 | url-status = dead }}
*[https://web.archive.org/web/20061016214005/http://gris.ulb.ac.be/ GRIS: Glycoprotein-hormone Receptor Information System]
*{{MeshName|LH-hCG+Receptors}}

{{G protein-coupled receptors}}
{{Neuropeptide receptors}}
{{GnRH and gonadotropins}}
{{GnRH and gonadotropin receptor modulators}}

{{DEFAULTSORT:Luteinizing hormone choriogonadotropin receptor}}

[[Category:G protein-coupled receptors]]
[[Category:Gonadotropin-releasing hormone and gonadotropins]]
[[Category:Signal transduction]]