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Prolactin receptor

January 01, 1970

The prolactin receptor (PRLR) is a type I cytokine receptor[1] encoded in humans by the PRLR gene on chromosome 5p13-14. It is the receptor for prolactin (PRL). The PRLR can also bind to and be activated by growth hormone (GH) and human placental lactogen (hPL). The PRLR is expressed in the mammary glands, pituitary gland, and other tissues. It plays an important role in lobuloalveolar development of the mammary glands during pregnancy and in lactation.

Prolactin Receptor
Identifiers
SymbolPRLR
NCBI gene5618
HGNC9446
OMIM176761
PDB1RW5
RefSeqNM_000949
UniProtP16471
Other data
LocusChr. 5 p13-p12
Search for
StructuresSwiss-model
DomainsInterPro

Structure edit

The prolactin receptor (PRLR) is a membrane-bound protein of the cytokine receptor superfamily. In humans, it is encoded by a single gene which contains 11 exons and is located on chromosome 5.[2] PRLR expression can be found in several tissues such as the gonads, breast, uterus, heart, liver, kidney, brain, immune cells, as well as adrenal and pituitary glands.

Several PRLR isoforms have been described in different tissues. These have varying lengths and cytoplasmic domain composition, but share identical extracellular domains, which are the regions binding to PRLR.

Diversity of PRLR is a result of transcription initiation in different sites of the PRLR promoter region. Additionally, post-translational modifications, like alternative splicing are the events that result in the different isoforms that allow for all the different actions of prolactin in the body.[3]

Signaling edit

The PRLR is a class 1 cytokine receptor that uses messenger pathways to control cell proliferation, migration, intracellular ion concentration and inhibit programmed cell death (apoptosis).[4][5] PRLRs also have functions in the second messenger cascades, including:

  • JAK-STAT pathway – the STAT protein family has been shown to have a key transduction role in cytokine receptor signalling; this pathway is initiated following the activation of PRLRs.[6] Although there have been 4 STAT proteins identified as transducer molecules of PRLR, STAT5 is recognised as the most important transducer of PRLR isoforms, with a role in inhibiting regulation of gene transcription.
  • Ras-Raf-MAPK – initiated by PRLR activation. Phosphotyrosine residues on PRLR act as binding sites for adapter proteins – these connect PRLR to the Ras/Raf/MAP kinase cascade
  • JAK-RUSH pathway [7][8]
  • PI3K/AKT/mTOR pathway[9]

Function edit

Expression of the PRLR protein is found within cells of the mammary glands[10] in accordance with its role in lactation, but also is the subject of attention for its diverse and emerging roles by its expression in adipose tissue,[11] pancreatic islet cell proliferation,[12] and immune responses.[13] The PRLR has been found to be essential for lobuloalveolar maturation of the mammary glands during pregnancy, as evidenced by the fact that PRLR knockout mice show severely impaired development of lobuloalveolar structures.[14][15] Disruption of PRLR signaling pathways have been linked to tumorigenesis and breast cancer development.[16]

Ligands edit

Agonists edit

Antagonists edit

Prolactin receptor antagonists such as Del1-9-G129R-hPRL have been developed.[18][19][20][21][22]

Dopamine agonists are currently the most common methods used for treating hyperprolactinemia. However, since dopamine agonists only negatively regulate prolactin production from the pituitary gland, a few studies have tried to develop prolactin receptor antagonists for potentially treating the dopamine-resistant local hyperprolactinemia.[18][23] Δ1–9-G129R-hPRL is one of the prolactin receptor antagonists been studied. Δ1–9-G129R-hPRL as a mutant (inactivated) form of prolactin which exerts its antagonist effect by competing with prolactin to bind with prolactin receptors; thereby, inhibiting the agonist effects of prolactin on prolactin receptors.[18] Besides molecular antagonists, antibodies can also potentially be used to inhibit prolactin receptor signaling. LFA102 is a monoclonal antibody that has been studied and tested for disrupting prolactin receptor's signaling in breast cancers and prostate cancers.[24] Although LFA102 has been proved sufficient to reduce prolactin receptor signaling based on in vitro and in vivo (mouse) studies, LFA102 likely has low effects on limiting tumor growth (breast and prostate cancer) as shown in phase I clinical trials.[24][25]

Prolactin receptor dysfunction edit

PRLR dysfunction has been seen to positively regulate the proliferation of malignant cells in breast cancer. Defects on prolactin receptor signalling can trigger tumour activity, rather than suppress. Signal control is monitored by a variety of genes, and the PRLR gene has been identified in the tissue of metastatic primary breast cancer cells.[26] The defect in the gene is thought to have built a resistance to chemotherapy, and has lost the ability to regulate the apoptosis of cells with mutated DNA.[27] This signalling defect then fails to promote the cellular differentiation, and promotes the upstream survival of the cancerous cells. In breast cancer, the survival of the breast epithelial cells resemble the malignant cells, characteristically known to have an increased proliferative rate.[28]

See also edit

References edit

  1. ^ Brooks CL (August 2012). "Molecular mechanisms of prolactin and its receptor". review. Endocrine Reviews. 33 (4): 504–25. doi:10.1210/er.2011-1040. PMC 3410225. PMID 22577091.
  2. ^ Brooks CL (August 2012). "Molecular mechanisms of prolactin and its receptor". Endocrine Reviews. 33 (4): 504–25. doi:10.1210/er.2011-1040. PMC 3410225. PMID 22577091.
  3. ^ Minh Hung H, Dieu Hang T, Nguyen MT (June 2019). "Structural Investigation of Human Prolactin Receptor Transmembrane Domain Homodimerization in a Membrane Environment through Multiscale Simulations". The Journal of Physical Chemistry B. 123 (23): 4858–4866. doi:10.1021/acs.jpcb.9b01986. PMID 31099581. S2CID 157056703.
  4. ^ Dandawate P, Kaushik G, Ghosh C, Standing D, Ali Sayed AA, Choudhury S, et al. (April 2020). "Diphenylbutylpiperidine Antipsychotic Drugs Inhibit Prolactin Receptor Signaling to Reduce Growth of Pancreatic Ductal Adenocarcinoma in Mice". Gastroenterology. 158 (5): 1433–1449.e27. doi:10.1053/j.gastro.2019.11.279. PMC 7103550. PMID 31786131.
  5. ^ Trott JF, Schennink A, Petrie WK, Manjarin R, VanKlompenberg MK, Hovey RC (May 2012). "Triennial Lactation Symposium: Prolactin: The multifaceted potentiator of mammary growth and function". Journal of Animal Science. 90 (5): 1674–86. doi:10.2527/jas.2011-4682. PMID 22205663.
  6. ^ Freeman ME, Kanyicska B, Lerant A, Nagy G (October 2000). "Prolactin: structure, function, and regulation of secretion". Physiological Reviews. 80 (4): 1523–631. doi:10.1152/physrev.2000.80.4.1523. PMID 11015620.
  7. ^ Helmer RA, Panchoo M, Dertien JS, Bhakta SM, Hewetson A, Chilton BS (August 2010). "Prolactin-induced Jak2 phosphorylation of RUSH: a key element in Jak/RUSH signaling". Molecular and Cellular Endocrinology. 325 (1–2): 143–9. doi:10.1016/j.mce.2010.05.010. PMC 2902710. PMID 20562009.
  8. ^ Helmer RA, Dertien JS, Chilton BS (May 2011). "Prolactin induces Jak2 phosphorylation of RUSHY195". Molecular and Cellular Endocrinology. 338 (1–2): 79–83. doi:10.1016/j.mce.2011.03.009. PMID 21457752. S2CID 36530259.
  9. ^ Clevenger CV, Furth PA, Hankinson SE, Schuler LA (February 2003). "The role of prolactin in mammary carcinoma". Endocrine Reviews. 24 (1): 1–27. doi:10.1210/er.2001-0036. PMC 1698952. PMID 12588805.
  10. ^ Baran N, Kelly PA, Binart N (April 2002). "Characterization of a prolactin-regulated gene in reproductive tissues using the prolactin receptor knockout mouse model". primary. Biology of Reproduction. 66 (4): 1210–8. doi:10.1095/biolreprod66.4.1210. PMID 11906943. S2CID 22649010.
  11. ^ Viengchareun S, Servel N, Fève B, Freemark M, Lombès M, Binart N (February 2008). "Prolactin receptor signaling is essential for perinatal brown adipocyte function: a role for insulin-like growth factor-2". primary. PLOS ONE. 3 (2): e1535. Bibcode:2008PLoSO...3.1535V. doi:10.1371/journal.pone.0001535. PMC 2212135. PMID 18253483.
  12. ^ Arumugam R, Fleenor D, Freemark M (August 2014). "Knockdown of prolactin receptors in a pancreatic beta cell line: effects on DNA synthesis, apoptosis, and gene expression". primary. Endocrine. 46 (3): 568–76. doi:10.1007/s12020-013-0073-1. PMC 3984618. PMID 24114406.
  13. ^ Dogusan Z, Book ML, Verdood P, Yu-Lee LY, Hooghe-Peters EL (September 2000). "Prolactin activates interferon regulatory factor-1 expression in normal lympho-hemopoietic cells". primary. European Cytokine Network. 11 (3): 435–42. PMID 11022129.
  14. ^ Horseman ND (6 December 2012). Prolactin. Springer Science & Business Media. pp. 227–. ISBN 978-1-4615-1683-5.
  15. ^ Bland KI, Copeland EM (9 September 2009). The Breast: Comprehensive Management of Benign and Malignant Diseases. Elsevier Health Sciences. pp. 44–45. ISBN 978-1-4377-1121-9.
  16. ^ Nouhi Z, Chughtai N, Hartley S, Cocolakis E, Lebrun JJ, Ali S (February 2006). "Defining the role of prolactin as an invasion suppressor hormone in breast cancer cells". Cancer Research. 66 (3): 1824–32. doi:10.1158/0008-5472.CAN-05-2292. PMID 16452244.
  17. ^ Bernichtein S, Kinet S, Jeay S, Llovera M, Madern D, Martial JA, et al. (September 2001). "S179D-human PRL, a pseudophosphorylated human PRL analog, is an agonist and not an antagonist". Endocrinology. 142 (9): 3950–63. doi:10.1210/endo.142.9.8369. PMID 11517174.
  18. ^ a b c Goffin V, Touraine P, Culler MD, Kelly PA (October 2006). "Drug Insight: prolactin-receptor antagonists, a novel approach to treatment of unresolved systemic and local hyperprolactinemia?". Nature Clinical Practice. Endocrinology & Metabolism. 2 (10): 571–81. doi:10.1038/ncpendmet0270. PMID 17024156. S2CID 21368033.
  19. ^ Jomain JB, Tallet E, Broutin I, Hoos S, van Agthoven J, Ducruix A, et al. (November 2007). "Structural and thermodynamic bases for the design of pure prolactin receptor antagonists: X-ray structure of Del1-9-G129R-hPRL". The Journal of Biological Chemistry. 282 (45): 33118–31. doi:10.1074/jbc.M704364200. PMID 17785459.
  20. ^ Jacobson EM, Hugo ER, Tuttle TR, Papoian R, Ben-Jonathan N (November 2010). "Unexploited therapies in breast and prostate cancer: blockade of the prolactin receptor". Trends in Endocrinology and Metabolism. 21 (11): 691–8. doi:10.1016/j.tem.2010.08.004. PMC 2967606. PMID 20846877.
  21. ^ Hansen MJ, Olsen JG, Bernichtein S, O'Shea C, Sigurskjold BW, Goffin V, Kragelund BB (2011). "Development of prolactin receptor antagonists with reduced pH-dependence of receptor binding". Journal of Molecular Recognition. 24 (4): 533–47. doi:10.1002/jmr.1064. PMID 20842635. S2CID 32885400.
  22. ^ Ferraris J, Bernichtein S, Pisera D, Goffin V (2013). "Use of prolactin receptor antagonist to better understand prolactin regulation of pituitary homeostasis". Neuroendocrinology. 98 (3): 171–9. doi:10.1159/000354701. hdl:11336/8384. PMID 23969780.
  23. ^ Karayazi Atıcı Ö, Govindrajan N, Lopetegui-González I, Shemanko CS (June 2021). "Prolactin: A hormone with diverse functions from mammary gland development to cancer metastasis". Seminars in Cell & Developmental Biology. 114: 159–170. doi:10.1016/j.semcdb.2020.10.005. PMID 33109441. S2CID 225100290.
  24. ^ a b Abramicheva PA, Smirnova OV (April 2019). "Prolactin Receptor Isoforms as the Basis of Tissue-Specific Action of Prolactin in the Norm and Pathology". Biochemistry. Biokhimiia. 84 (4): 329–345. doi:10.1134/S0006297919040011. PMID 31228925. S2CID 129945003.
  25. ^ Goffin V, Touraine P (September 2015). "The prolactin receptor as a therapeutic target in human diseases: browsing new potential indications". Expert Opinion on Therapeutic Targets. 19 (9): 1229–44. doi:10.1517/14728222.2015.1053209. PMID 26063597. S2CID 31029607.
  26. ^ Bernard V, Young J, Binart N (June 2019). "Prolactin - a pleiotropic factor in health and disease". Nature Reviews. Endocrinology. 15 (6): 356–365. doi:10.1038/s41574-019-0194-6. PMID 30899100. S2CID 84846294.
  27. ^ Shemanko CS (November 2016). "Prolactin receptor in breast cancer: marker for metastatic risk". Journal of Molecular Endocrinology. 57 (4): R153–R165. doi:10.1530/JME-16-0150. PMID 27658959.
  28. ^ McHale K, Tomaszewski JE, Puthiyaveettil R, Livolsi VA, Clevenger CV (May 2008). "Altered expression of prolactin receptor-associated signaling proteins in human breast carcinoma". Modern Pathology. 21 (5): 565–71. doi:10.1038/modpathol.2008.7. PMID 18246042. S2CID 205199390.

External links edit

January 01, 1970
prolactin, receptor, prolactin, receptor, prlr, type, cytokine, receptor, encoded, humans, prlr, gene, chromosome, 5p13, receptor, prolactin, prlr, also, bind, activated, growth, hormone, human, placental, lactogen, prlr, expressed, mammary, glands, pituitary,. The prolactin receptor PRLR is a type I cytokine receptor 1 encoded in humans by the PRLR gene on chromosome 5p13 14 It is the receptor for prolactin PRL The PRLR can also bind to and be activated by growth hormone GH and human placental lactogen hPL The PRLR is expressed in the mammary glands pituitary gland and other tissues It plays an important role in lobuloalveolar development of the mammary glands during pregnancy and in lactation Prolactin ReceptorIdentifiersSymbolPRLRNCBI gene5618HGNC9446OMIM176761PDB1RW5RefSeqNM 000949UniProtP16471Other dataLocusChr 5 p13 p12Search forStructuresSwiss modelDomainsInterProContents 1 Structure 2 Signaling 3 Function 4 Ligands 4 1 Agonists 4 2 Antagonists 5 Prolactin receptor dysfunction 6 See also 7 References 8 External linksStructure editThe prolactin receptor PRLR is a membrane bound protein of the cytokine receptor superfamily In humans it is encoded by a single gene which contains 11 exons and is located on chromosome 5 2 PRLR expression can be found in several tissues such as the gonads breast uterus heart liver kidney brain immune cells as well as adrenal and pituitary glands Several PRLR isoforms have been described in different tissues These have varying lengths and cytoplasmic domain composition but share identical extracellular domains which are the regions binding to PRLR Diversity of PRLR is a result of transcription initiation in different sites of the PRLR promoter region Additionally post translational modifications like alternative splicing are the events that result in the different isoforms that allow for all the different actions of prolactin in the body 3 Signaling editThe PRLR is a class 1 cytokine receptor that uses messenger pathways to control cell proliferation migration intracellular ion concentration and inhibit programmed cell death apoptosis 4 5 PRLRs also have functions in the second messenger cascades including JAK STAT pathway the STAT protein family has been shown to have a key transduction role in cytokine receptor signalling this pathway is initiated following the activation of PRLRs 6 Although there have been 4 STAT proteins identified as transducer molecules of PRLR STAT5 is recognised as the most important transducer of PRLR isoforms with a role in inhibiting regulation of gene transcription Ras Raf MAPK initiated by PRLR activation Phosphotyrosine residues on PRLR act as binding sites for adapter proteins these connect PRLR to the Ras Raf MAP kinase cascade JAK RUSH pathway 7 8 PI3K AKT mTOR pathway 9 Function editExpression of the PRLR protein is found within cells of the mammary glands 10 in accordance with its role in lactation but also is the subject of attention for its diverse and emerging roles by its expression in adipose tissue 11 pancreatic islet cell proliferation 12 and immune responses 13 The PRLR has been found to be essential for lobuloalveolar maturation of the mammary glands during pregnancy as evidenced by the fact that PRLR knockout mice show severely impaired development of lobuloalveolar structures 14 15 Disruption of PRLR signaling pathways have been linked to tumorigenesis and breast cancer development 16 Ligands editAgonists edit Prolactin Growth hormone Human placental lactogen Placental growth hormone S179D hPRL 17 Antagonists edit Prolactin receptor antagonists such as Del1 9 G129R hPRL have been developed 18 19 20 21 22 Dopamine agonists are currently the most common methods used for treating hyperprolactinemia However since dopamine agonists only negatively regulate prolactin production from the pituitary gland a few studies have tried to develop prolactin receptor antagonists for potentially treating the dopamine resistant local hyperprolactinemia 18 23 D1 9 G129R hPRL is one of the prolactin receptor antagonists been studied D1 9 G129R hPRL as a mutant inactivated form of prolactin which exerts its antagonist effect by competing with prolactin to bind with prolactin receptors thereby inhibiting the agonist effects of prolactin on prolactin receptors 18 Besides molecular antagonists antibodies can also potentially be used to inhibit prolactin receptor signaling LFA102 is a monoclonal antibody that has been studied and tested for disrupting prolactin receptor s signaling in breast cancers and prostate cancers 24 Although LFA102 has been proved sufficient to reduce prolactin receptor signaling based on in vitro and in vivo mouse studies LFA102 likely has low effects on limiting tumor growth breast and prostate cancer as shown in phase I clinical trials 24 25 Prolactin receptor dysfunction editPRLR dysfunction has been seen to positively regulate the proliferation of malignant cells in breast cancer Defects on prolactin receptor signalling can trigger tumour activity rather than suppress Signal control is monitored by a variety of genes and the PRLR gene has been identified in the tissue of metastatic primary breast cancer cells 26 The defect in the gene is thought to have built a resistance to chemotherapy and has lost the ability to regulate the apoptosis of cells with mutated DNA 27 This signalling defect then fails to promote the cellular differentiation and promotes the upstream survival of the cancerous cells In breast cancer the survival of the breast epithelial cells resemble the malignant cells characteristically known to have an increased proliferative rate 28 See also editProlactin modulator Hypothalamic pituitary prolactin axisReferences edit Brooks CL August 2012 Molecular mechanisms of prolactin and its receptor review Endocrine Reviews 33 4 504 25 doi 10 1210 er 2011 1040 PMC 3410225 PMID 22577091 Brooks CL August 2012 Molecular mechanisms of prolactin and its receptor Endocrine Reviews 33 4 504 25 doi 10 1210 er 2011 1040 PMC 3410225 PMID 22577091 Minh Hung H Dieu Hang T Nguyen MT June 2019 Structural Investigation of Human Prolactin Receptor Transmembrane Domain Homodimerization in a Membrane Environment through Multiscale Simulations The Journal of Physical Chemistry B 123 23 4858 4866 doi 10 1021 acs jpcb 9b01986 PMID 31099581 S2CID 157056703 Dandawate P Kaushik G Ghosh C Standing D Ali Sayed AA Choudhury S et al April 2020 Diphenylbutylpiperidine Antipsychotic Drugs Inhibit Prolactin Receptor Signaling to Reduce Growth of Pancreatic Ductal Adenocarcinoma in Mice Gastroenterology 158 5 1433 1449 e27 doi 10 1053 j gastro 2019 11 279 PMC 7103550 PMID 31786131 Trott JF Schennink A Petrie WK Manjarin R VanKlompenberg MK Hovey RC May 2012 Triennial Lactation Symposium Prolactin The multifaceted potentiator of mammary growth and function Journal of Animal Science 90 5 1674 86 doi 10 2527 jas 2011 4682 PMID 22205663 Freeman ME Kanyicska B Lerant A Nagy G October 2000 Prolactin structure function and regulation of secretion Physiological Reviews 80 4 1523 631 doi 10 1152 physrev 2000 80 4 1523 PMID 11015620 Helmer RA Panchoo M Dertien JS Bhakta SM Hewetson A Chilton BS August 2010 Prolactin induced Jak2 phosphorylation of RUSH a key element in Jak RUSH signaling Molecular and Cellular Endocrinology 325 1 2 143 9 doi 10 1016 j mce 2010 05 010 PMC 2902710 PMID 20562009 Helmer RA Dertien JS Chilton BS May 2011 Prolactin induces Jak2 phosphorylation of RUSHY195 Molecular and Cellular Endocrinology 338 1 2 79 83 doi 10 1016 j mce 2011 03 009 PMID 21457752 S2CID 36530259 Clevenger CV Furth PA Hankinson SE Schuler LA February 2003 The role of prolactin in mammary carcinoma Endocrine Reviews 24 1 1 27 doi 10 1210 er 2001 0036 PMC 1698952 PMID 12588805 Baran N Kelly PA Binart N April 2002 Characterization of a prolactin regulated gene in reproductive tissues using the prolactin receptor knockout mouse model primary Biology of Reproduction 66 4 1210 8 doi 10 1095 biolreprod66 4 1210 PMID 11906943 S2CID 22649010 Viengchareun S Servel N Feve B Freemark M Lombes M Binart N February 2008 Prolactin receptor signaling is essential for perinatal brown adipocyte function a role for insulin like growth factor 2 primary PLOS ONE 3 2 e1535 Bibcode 2008PLoSO 3 1535V doi 10 1371 journal pone 0001535 PMC 2212135 PMID 18253483 Arumugam R Fleenor D Freemark M August 2014 Knockdown of prolactin receptors in a pancreatic beta cell line effects on DNA synthesis apoptosis and gene expression primary Endocrine 46 3 568 76 doi 10 1007 s12020 013 0073 1 PMC 3984618 PMID 24114406 Dogusan Z Book ML Verdood P Yu Lee LY Hooghe Peters EL September 2000 Prolactin activates interferon regulatory factor 1 expression in normal lympho hemopoietic cells primary European Cytokine Network 11 3 435 42 PMID 11022129 Horseman ND 6 December 2012 Prolactin Springer Science amp Business Media pp 227 ISBN 978 1 4615 1683 5 Bland KI Copeland EM 9 September 2009 The Breast Comprehensive Management of Benign and Malignant Diseases Elsevier Health Sciences pp 44 45 ISBN 978 1 4377 1121 9 Nouhi Z Chughtai N Hartley S Cocolakis E Lebrun JJ Ali S February 2006 Defining the role of prolactin as an invasion suppressor hormone in breast cancer cells Cancer Research 66 3 1824 32 doi 10 1158 0008 5472 CAN 05 2292 PMID 16452244 Bernichtein S Kinet S Jeay S Llovera M Madern D Martial JA et al September 2001 S179D human PRL a pseudophosphorylated human PRL analog is an agonist and not an antagonist Endocrinology 142 9 3950 63 doi 10 1210 endo 142 9 8369 PMID 11517174 a b c Goffin V Touraine P Culler MD Kelly PA October 2006 Drug Insight prolactin receptor antagonists a novel approach to treatment of unresolved systemic and local hyperprolactinemia Nature Clinical Practice Endocrinology amp Metabolism 2 10 571 81 doi 10 1038 ncpendmet0270 PMID 17024156 S2CID 21368033 Jomain JB Tallet E Broutin I Hoos S van Agthoven J Ducruix A et al November 2007 Structural and thermodynamic bases for the design of pure prolactin receptor antagonists X ray structure of Del1 9 G129R hPRL The Journal of Biological Chemistry 282 45 33118 31 doi 10 1074 jbc M704364200 PMID 17785459 Jacobson EM Hugo ER Tuttle TR Papoian R Ben Jonathan N November 2010 Unexploited therapies in breast and prostate cancer blockade of the prolactin receptor Trends in Endocrinology and Metabolism 21 11 691 8 doi 10 1016 j tem 2010 08 004 PMC 2967606 PMID 20846877 Hansen MJ Olsen JG Bernichtein S O Shea C Sigurskjold BW Goffin V Kragelund BB 2011 Development of prolactin receptor antagonists with reduced pH dependence of receptor binding Journal of Molecular Recognition 24 4 533 47 doi 10 1002 jmr 1064 PMID 20842635 S2CID 32885400 Ferraris J Bernichtein S Pisera D Goffin V 2013 Use of prolactin receptor antagonist to better understand prolactin regulation of pituitary homeostasis Neuroendocrinology 98 3 171 9 doi 10 1159 000354701 hdl 11336 8384 PMID 23969780 Karayazi Atici O Govindrajan N Lopetegui Gonzalez I Shemanko CS June 2021 Prolactin A hormone with diverse functions from mammary gland development to cancer metastasis Seminars in Cell amp Developmental Biology 114 159 170 doi 10 1016 j semcdb 2020 10 005 PMID 33109441 S2CID 225100290 a b Abramicheva PA Smirnova OV April 2019 Prolactin Receptor Isoforms as the Basis of Tissue Specific Action of Prolactin in the Norm and Pathology Biochemistry Biokhimiia 84 4 329 345 doi 10 1134 S0006297919040011 PMID 31228925 S2CID 129945003 Goffin V Touraine P September 2015 The prolactin receptor as a therapeutic target in human diseases browsing new potential indications Expert Opinion on Therapeutic Targets 19 9 1229 44 doi 10 1517 14728222 2015 1053209 PMID 26063597 S2CID 31029607 Bernard V Young J Binart N June 2019 Prolactin a pleiotropic factor in health and disease Nature Reviews Endocrinology 15 6 356 365 doi 10 1038 s41574 019 0194 6 PMID 30899100 S2CID 84846294 Shemanko CS November 2016 Prolactin receptor in breast cancer marker for metastatic risk Journal of Molecular Endocrinology 57 4 R153 R165 doi 10 1530 JME 16 0150 PMID 27658959 McHale K Tomaszewski JE Puthiyaveettil R Livolsi VA Clevenger CV May 2008 Altered expression of prolactin receptor associated signaling proteins in human breast carcinoma Modern Pathology 21 5 565 71 doi 10 1038 modpathol 2008 7 PMID 18246042 S2CID 205199390 External links editProlactin receptor at the U S National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Prolactin receptor amp oldid 1191043965, wikipedia, wiki, book, books, library,

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