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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

GPHB5  -  glycoprotein hormone beta 5

Homo sapiens

Synonyms: B5, GPB5, Glycoprotein hormone beta-5, Thyrostimulin subunit beta, ZLUT1
 
 
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Disease relevance of GPHB5

 

High impact information on GPHB5

  • Those restriction fragments characteristic of the GPA 3' and GPB 5' ends were absent from the SAT homozygote and showed reduced intensity in SAT heterozygotes [2].
  • However, neither transgenic overexpression of GPHA2 nor deletion of GPHB5 produces an overt phenotype in mice [1].
  • Based on unique sequence similarity to the alpha- and beta-subunits of glycoprotein hormones, they were named glycoprotein-alpha2 (GPA2) and glycoprotein-beta5 (GPB5), respectively [3].
  • To explore the function of thyrostimulin in the rat, we have cloned rat GPA2 and GPB5, reconstituted the heterodimers in vitro, and confirmed that rat thyrostimulin activates TSHR with an affinity similar to that of TSH [4].
  • Furthermore, the levels of GPB5 remain constant during the estrus cycle, while those of GPA2 vary [4].
 

Anatomical context of GPHB5

  • A quantitative analysis showed that the co-localization of GPA2 and GPB5 is restricted in the rat to the eye and the testis [4].
  • Subsequently, it was demonstrated that GPA2 and GPB5 form a heterodimeric hormone, thyrostimulin/OGH, capable of activating TSHR in vivoand the thyroid axis in transgenic mice [5].
 

Associations of GPHB5 with chemical compounds

  • Based on comparative genomic searches, we isolated the fly orthologs for human GPA2 and GPB5, each consisting of 10 cysteine residues likely involved in cystine-knot formation [6].
 

Analytical, diagnostic and therapeutic context of GPHB5

  • RT-PCR analyses in Drosophila melanogaster demonstrated the expression of GPA2 and GPB5 at different developmental stages [6].
  • PCR analysis using a panel of human cDNAs from 14 different tissues demonstrated that GPB5 is similar to other beta-subunits showing restricted tissue expression, mainly in pituitary and brain [3].
  • In situ hybridization of the pituitary showed that while GPA2 is expressed in the anterior lobe, GPB5 is not detected in any of the lobes [4].

References

  1. A glycoprotein hormone expressed in corticotrophs exhibits unique binding properties on thyroid-stimulating hormone receptor. Okada, S.L., Ellsworth, J.L., Durnam, D.M., Haugen, H.S., Holloway, J.L., Kelley, M.L., Lewis, K.E., Ren, H., Sheppard, P.O., Storey, H.M., Waggie, K.S., Wolf, A.C., Yao, L.Y., Webster, P.J. Mol. Endocrinol. (2006) [Pubmed]
  2. Glycophorin SAT of the human erythrocyte membrane is specified by a hybrid gene reciprocal to glycophorin Dantu gene. Huang, C.H., Reid, M.E., Okubo, Y., Daniels, G.L., Blumenfeld, O.O. Blood (1995) [Pubmed]
  3. Evolution of glycoprotein hormone subunit genes in bilateral metazoa: identification of two novel human glycoprotein hormone subunit family genes, GPA2 and GPB5. Hsu, S.Y., Nakabayashi, K., Bhalla, A. Mol. Endocrinol. (2002) [Pubmed]
  4. Differential expression of the thyrostimulin subunits, glycoprotein alpha2 and beta5 in the rat pituitary. Nagasaki, H., Wang, Z., Jackson, V.R., Lin, S., Nothacker, H.P., Civelli, O. J. Mol. Endocrinol. (2006) [Pubmed]
  5. Conservation of the heterodimeric glycoprotein hormone subunit family proteins and the LGR signaling system from nematodes to humans. Park, J.I., Semyonov, J., Chang, C.L., Hsu, S.Y. Endocrine (2005) [Pubmed]
  6. Heterodimeric fly glycoprotein hormone-alpha2 (GPA2) and glycoprotein hormone-beta5 (GPB5) activate fly leucine-rich repeat-containing G protein-coupled receptor-1 (DLGR1) and stimulation of human thyrotropin receptors by chimeric fly GPA2 and human GPB5. Sudo, S., Kuwabara, Y., Park, J.I., Hsu, S.Y., Hsueh, A.J. Endocrinology (2005) [Pubmed]
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