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       #Post#: 3100--------------------------------------------------
       Understanding Androgen Receptor (AR)
       By: Road2HardCoreIron Date: March 28, 2023, 2:11 pm
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       The androgen receptor (AR), also known as NR3C4 (nuclear
       receptor subfamily 3, group C, member 4), is a type of nuclear
       receptor[9] that is activated by binding any of the androgenic
       hormones, including testosterone and dihydrotestosterone,[10] in
       the cytoplasm and then translocating into the nucleus. The
       androgen receptor is most closely related to the progesterone
       receptor, and progestins in higher dosages can block the
       androgen receptor.[11][12]
       The main function of the androgen receptor is as a DNA-binding
       transcription factor that regulates gene expression;[13]
       however, the androgen receptor has other functions as well.[14]
       Androgen-regulated genes are critical for the development and
       maintenance of the male sexual phenotype.
       Function
       Effect on development
       In some cell types, testosterone interacts directly with
       androgen receptors, whereas, in others, testosterone is
       converted by 5-alpha-reductase to dihydrotestosterone, an even
       more potent agonist for androgen receptor activation.[15]
       Testosterone appears to be the primary androgen
       receptor-activating hormone in the Wolffian duct, whereas
       dihydrotestosterone is the main androgenic hormone in the
       urogenital sinus, urogenital tubercle, and hair follicles.[16]
       Testosterone is therefore responsible primarily for the
       development of male primary sexual characteristics, whilst
       dihydrotestosterone is responsible for secondary male
       characteristics.
       Androgens cause slow maturation of the bones, but more of the
       potent maturation effect comes from the estrogen produced by
       aromatization of androgens. Steroid users of teen age may find
       that their growth had been stunted by androgen and/or estrogen
       excess. People with too little sex hormones can be short during
       puberty but end up taller as adults as in androgen insensitivity
       syndrome or estrogen insensitivity syndrome.[17]
       Knockout-mice studies have shown that the androgen receptor is
       essential for normal female fertility, being required for
       development and full functionality of the ovarian follicles and
       ovulation, working through both intra-ovarian and neuroendocrine
       mechanisms.[18]
       Maintenance of male skeletal integrity
       Via the androgen receptor, androgens play a key role in the
       maintenance of male skeletal integrity. The regulation of this
       integrity by androgen receptor (AR) signaling can be attributed
       to both osteoblasts and osteocytes.[19]
       Role in females
       The AR plays a role in regulating female sexual, somatic, and
       behavioral functions. Experimental data using AR knockout female
       mice, provides evidence that the promotion of cardiac growth,
       kidney hypertrophy, cortical bone growth and regulation of
       trabecular bone structure is a result of DNA-binding-dependent
       actions of the AR in females.
       Moreover, the importance of understanding female androgen
       receptors lies in their role in several genetic disorders
       including androgen insensitivity syndrome (AIS). Complete (CAIS)
       and partial (PAIS) which are a result of mutations in the genes
       that code for AR. These mutations cause the inactivation of AR
       due to mutations conferring resistance to circulating
       testosterone, with more than 400 different AR mutations
       reported.[citation needed]
       Mechanism of action
       Genomic
       The primary mechanism of action for androgen receptors is direct
       regulation of gene transcription. The binding of an androgen to
       the androgen receptor results in a conformational change in the
       receptor that, in turn, causes dissociation of heat shock
       proteins, transport from the cytosol into the cell nucleus, and
       dimerization. The androgen receptor dimer binds to a specific
       sequence of DNA known as a hormone response element. Androgen
       receptors interact with other proteins in the nucleus, resulting
       in up- or down-regulation of specific gene transcription.[20]
       Up-regulation or activation of transcription results in
       increased synthesis of messenger RNA, which, in turn, is
       translated by ribosomes to produce specific proteins. One of the
       known target genes of androgen receptor activation is the
       insulin-like growth factor 1 receptor (IGF-1R).[21] Thus,
       changes in levels of specific proteins in cells is one way that
       androgen receptors control cell behavior.
       One function of androgen receptor that is independent of direct
       binding to its target DNA sequence is facilitated by recruitment
       via other DNA-binding proteins. One example is serum response
       factor, a protein that activates several genes that cause muscle
       growth.[22]
       Androgen receptor is modified by post-translational modification
       through acetylation,[23] which directly promotes AR-mediated
       transactivation, apoptosis[24] and contact-independent growth of
       prostate cancer cells.[25] AR acetylation is induced by
       androgens[26] and determines recruitment into chromatin.[27] The
       AR acetylation site is a key target of NAD-dependent and
       TSA-dependent histone deacetylases[28] and long non-coding
       RNA.[29]
       Non-genomic
       More recently, androgen receptors have been shown to have a
       second mode of action. As has been also found for other steroid
       hormone receptors such as estrogen receptors, androgen receptors
       can have actions that are independent of their interactions with
       DNA.[14][30] Androgen receptors interact with certain signal
       transduction proteins in the cytoplasm. Androgen binding to
       cytoplasmic androgen receptors can cause rapid changes in cell
       function independent of changes in gene transcription, such as
       changes in ion transport. Regulation of signal transduction
       pathways by cytoplasmic androgen receptors can indirectly lead
       to changes in gene transcription, for example, by leading to
       phosphorylation of other transcription factors.
       Genetics
       Gene
       In humans, the androgen receptor is encoded by the AR gene
       located on the X chromosome at Xq11–12.[31][32]
       Deficiencies
       At least 165 disease-causing mutations in this gene have been
       discovered. [33] The androgen insensitivity syndrome, formerly
       known as testicular feminization, is caused by a mutation in the
       androgen receptor gene on the X chromosome (locus:
       Xq11–Xq12).[34] The androgen receptor seems to affect neuron
       physiology and is defective in Kennedy's disease.[35][36] In
       addition, point mutations and trinucleotide repeat polymorphisms
       have been linked to a number of additional disorders.[37]
       CAG repeats
       The AR gene contains CAG repeats that affect receptor function,
       where fewer repeats leads to increased receptor sensitivity to
       circulating androgens and more repeats leads to decreased
       receptor sensitivity. Studies have shown that racial variation
       in CAG repeats exists,[38][39] with African-Americans having
       fewer repeats than non-Hispanic white Americans.[38] The racial
       trends in CAG repeats parallels the incidence and mortality of
       prostate cancer in these groups.
       Mutations
       The enhancer and the gene encoding for these receptors contain
       recurrent mutations, such as structural rearrangements and copy
       number changes, acquired in the progression of metastatic
       castration-resistant prostate cancer (mCRPC) treatment with
       therapy targeting these receptors (abiraterone, enzalutamide),
       make the disease progression determined by the androgen receptor
       genotype.[40]
       Structure
       Structural domains of the two isoforms (AR-A and AR-B) of the
       human androgen receptor. Numbers above the bars refer to the
       amino acid residues that separate the domains starting from the
       N-terminus (left) to C-terminus (right). NTD = N-terminal
       domain, DBD = DNA-binding domain, LBD = ligand-binding domain,
       AF = activation function.
       Isoforms
       Two isoforms of the androgen receptor (A and B) have been
       identified:[41]
       AR-A – 87 kDa; N-terminus truncated (lacks the first 187 amino
       acids), which results from in vitro proteolysis.[42]
       AR-B – 110 kDa; full length
       Domains
       Like other nuclear receptors, the androgen receptor is modular
       in structure and is composed of the following functional domains
       labeled A through F:[43]
       A/B) – N-terminal regulatory domain contains:[44]
       activation function 1 (AF-1) between residues 101 and 370
       required for full ligand-activated transcriptional activity
       activation function 5 (AF-5) between residues 360–485 is
       responsible for the constitutive activity (activity without
       bound ligand)
       dimerization surface involving residues 1–36 (containing the
       FXXLF motif; where F = phenylalanine, L = leucine, and X = any
       amino acid residue) and 370–494, both of which interact with the
       ligand binding domain (LBD) in an intramolecular[45][46][47]
       head-to-tail interaction[48][49][50]
       C) – DNA binding domain (DBD)
       D) – Hinge region; flexible region that connects the DBD with
       the LBD; along with the DBD, contains a ligand dependent nuclear
       localization signal[51]
       E) – Ligand binding domain (LBD) containing
       activation function 2 (AF-2), responsible for agonist induced
       activity (activity in the presence of bound agonist)
       AF-2 binds either the N-terminal FXXFL motif intramolecularly or
       coactivator proteins (containing the LXXLL or preferably FXXFL
       motifs)[50]
       A ligand dependent nuclear export signal[52]
       F) – C-terminal domain
       Splice variants
       AR-V7 is an androgen receptor splice variant that can be
       detected in circulating tumor cells of metastatic prostate
       cancer patients[53][54] and is predictive of resistance to some
       drugs.[55]
       Clinical significance
       High expression in androgen receptor has been linked to
       aggression and sex drive by affecting the HPA and HPG axis[56]
       Aberrant androgen receptor coregulator activity may contribute
       to the progression of prostate cancer.[57][40]
       Ligands
       vte Affinities[a][58]
       Compound
       Metribolone
       Dihydrotestosterone
       Cyproterone acetate
       Bicalutamide
       Nilutamide
       Hydroxyflutamide
       Flutamide
       Notes:
       At androgen receptors; measured in human prostate tissue.
       Relative to Metribolone, which is by definition 100%
       Agonists
       Endogenous androgens (e.g., testosterone, dihydrotestosterone,
       androstenedione, androstenediol, dehydroepiandrosterone)
       Synthetic androgens (e.g., methyltestosterone, metandienone,
       nandrolone, trenbolone, oxandrolone, stanozolol)
       Mixed
       Selective androgen receptor modulators (e.g., andarine,
       enobosarm)
       Antagonists
       Steroidal antiandrogens (e.g., cyproterone acetate,
       chlormadinone acetate, spironolactone, oxendolone)
       Nonsteroidal antiandrogens (e.g., flutamide, nilutamide,
       bicalutamide, enzalutamide, apalutamide, RU-58841)
       N-Terminal domain antiandrogens (e.g., bisphenol A, EPI-001,
       ralaniten, JN compounds)[59]
       As a drug target
       The AR is an important therapeutic target in prostate cancer.
       Thus many different antiandrogens have been developed, primarily
       targeting the ligand-binding domain of the protein.[60] AR
       ligands can either be classified based on their structure
       (steroidal or nonsteroidal) or based on their ability to
       activate or inhibit transcription (agonists or antagonists).[61]
       Inhibitors that target alternative functional domains
       (N-terminal domain, DNA-binding domain) of the protein are still
       under development.[59]
       Drug resistance
       Alteration of ARs may lead to treatment resistance (castration
       resistance) in prostate cancer as there may be missense
       mutations of the ligand binding domain, amplifications of the
       gene coding for this receptor or in its enhancer, mostly,
       suggesting the presence of different subclones with different
       genotypes of these receptors.[40]
       Interactions
       Androgen receptor has been shown to interact with:
       AKT1,[62]
       BAG1,[63][64][65]
       Beta-catenin,[66][67][68][69][70][71]
       BRCA1,[72][73]
       C-jun,[74]
       Calmodulin 1,[75]
       Caveolin 1,[76]
       CDK9,[77]
       COX5B,[78]
       CREB-binding protein,[79][80][81][82]
       Cyclin D1,[83][84][85][86]
       Cyclin-dependent kinase 7,[87]
       DACH1,[88]
       Death associated protein 6,[89]
       L-DOPA,[90]
       EFCAB6,[91]
       Epidermal growth factor receptor,[92][93]
       FOXO1,[94]
       GAPDH,[95]
       Gelsolin,[96]
       GNB2L1,[97]
       GSK3B,[98]
       HDAC1,[99]
       HSP90AA1,[100][101]
       HTATIP,[99]
       MAGEA11,[102][103]
       MED1,[104]
       MYST2,[105]
       NCOA1,[67][106][107]
       NCOA2,[66][81][102][108][109]
       NCOA3,[108][110][111]
       NCOA4,[62][109][112][113][114][115][116][117][118]
       NCOA6,[119]
       NCOR2,[66][120][121]
       NONO,[81]
       p300,[122]
       PA2G4,[123]
       PAK6,[124][125]
       PATZ1,[126]
       PIAS2,[127][128]
       PRPF6,[129]
       PTEN,[130]
       RAD9A,[131]
       RANBP9,[132]
       RCHY1,[133]
       Retinoblastoma protein,[134][135]
       RNF14,[109][112][136][137]
       RNF4,[126][138][139]
       SART3,[140]
       SIRT1,[28]
       SMAD3,[141][142][143]
       Small heterodimer partner,[144]
       Src,[130][145][146]
       SRY,[147]
       STAT3,[148][149]
       SVIL,[150]
       Testicular receptor 2,[151]
       Testicular receptor 4,[152]
       TGFB1I1,[112][153]
       TMF1,[154]
       TRIM68,[155]
       UBE2I,[66][67][156][157][158][159]
       UXT,[160] and
       ZMIZ1.[161]
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