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Rln3  -  relaxin 3

Mus musculus

Synonyms: Insl7, Insulin-like peptide 7, Insulin-like peptide INSL7, M3, Prorelaxin M3, ...
 
 
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Disease relevance of Rln3

  • Functional expression of mouse relaxin and mouse relaxin-3 in the lung from an Ebola virus glycoprotein-pseudotyped lentivirus via tracheal delivery [1].
 

High impact information on Rln3

  • The M3 protein encoded by murine gamma herpesvirus68 (gamma HV68) functions as an immune system saboteur by the engagement of chemoattractant cytokines, thereby altering host antiviral inflammatory responses [2].
  • T-cell responses to the M3 immune evasion protein of murid gammaherpesvirus 68 are partially protective and induced with lytic antigen kinetics [3].
  • Consistent with the distribution of RLX3 mRNA, neurons containing RLX3-like immunoreactivity (LI) were observed in the pontine nucleus incertus and the majority of these cells, which are known to express corticotropin-releasing factor receptor-1, were shown to express glutamic acid decarboxylase-65-immunoreactivity, suggesting a GABA phenotype [4].
  • Relaxin-3 in GABA projection neurons of nucleus incertus suggests widespread influence on forebrain circuits via G-protein-coupled receptor-135 in the rat [4].
  • The RLX3-positive network overlapped the regional distribution of GPCR135 mRNA and specific binding sites for an [(125)I]-GPCR135-selective, chimeric peptide [4].
 

Biological context of Rln3

 

Anatomical context of Rln3

  • To clarify the function of relaxin 3, we prepared recombinant human relaxin 3 using a mouse adrenocorticotrophic hormone (ACTH)-secreting cell line, AtT20 [5].
 

Associations of Rln3 with chemical compounds

  • Here we show that a specific proline (Pro 8*), located at the apex of the loop between the second and third transmembrane helices (M2-M3), can link binding to gating through a cis-trans isomerization of the protein backbone [6].
 

Regulatory relationships of Rln3

  • In the present study we explore whether GPCR142 is expressed in the mouse brain and whether it is likely to contribute to or interfere with the pharmacological evaluation of relaxin-3 ligands [7].
 

Other interactions of Rln3

 

Analytical, diagnostic and therapeutic context of Rln3

  • In ongoing studies to understand the physiological functions of RLX3, the distribution of RLX3-containing neuronal elements in rat brain was determined by immunohistochemistry, using an affinity-purified polyclonal antiserum raised against a conserved segment of the RLX3 C-peptide (AS-R3(85-101)) [4].
  • Ir-relaxin 3 was purified from the culture supernatant by a combination of various chromatographies [5].
  • After treatment with 5 microM forskolin for 3 days, the concentration of the ir-relaxin 3 in the culture supernatant reached 12 nM [5].
  • To detect a mature form of recombinant human relaxin 3, a competitive enzyme immunoassay (EIA) was developed using a monoclonal antibody (mAb; HK4-144-10), which was raised for the N-terminal peptide of human relaxin 3 A-chain [5].
  • DNA vaccination with the M3 gene, encoding an immune evasion molecule expressed during both the acute lytic and persistent phases of murid gammaherpesvirus 68 infection, yielded a significantly lower titer of virus in the lung than controls [3].

References

  1. Functional expression of mouse relaxin and mouse relaxin-3 in the lung from an Ebola virus glycoprotein-pseudotyped lentivirus via tracheal delivery. Silvertown, J.D., Walia, J.S., Summerlee, A.J., Medin, J.A. Endocrinology (2006) [Pubmed]
  2. Structural basis of chemokine sequestration by a herpesvirus decoy receptor. Alexander, J.M., Nelson, C.A., van Berkel, V., Lau, E.K., Studts, J.M., Brett, T.J., Speck, S.H., Handel, T.M., Virgin, H.W., Fremont, D.H. Cell (2002) [Pubmed]
  3. T-cell responses to the M3 immune evasion protein of murid gammaherpesvirus 68 are partially protective and induced with lytic antigen kinetics. Obar, J.J., Donovan, D.C., Crist, S.G., Silvia, O., Stewart, J.P., Usherwood, E.J. J. Virol. (2004) [Pubmed]
  4. Relaxin-3 in GABA projection neurons of nucleus incertus suggests widespread influence on forebrain circuits via G-protein-coupled receptor-135 in the rat. Ma, S., Bonaventure, P., Ferraro, T., Shen, P.J., Burazin, T.C., Bathgate, R.A., Liu, C., Tregear, G.W., Sutton, S.W., Gundlach, A.L. Neuroscience (2007) [Pubmed]
  5. Production of recombinant human relaxin 3 in AtT20 cells. Kizawa, H., Nishi, K., Ishibashi, Y., Harada, M., Asano, T., Ito, Y., Suzuki, N., Hinuma, S., Fujisawa, Y., Onda, H., Nishimura, O., Fujino, M. Regul. Pept. (2003) [Pubmed]
  6. Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel. Lummis, S.C., Beene, D.L., Lee, L.W., Lester, H.A., Broadhurst, R.W., Dougherty, D.A. Nature (2005) [Pubmed]
  7. G-Protein-Coupled Receptor (GPCR)-142 Does Not Contribute to Relaxin-3 Binding in the Mouse Brain: Further Support that Relaxin-3 Is the Physiological Ligand for GPCR135. Sutton, S.W., Bonaventure, P., Kuei, C., Nepomuceno, D., Wu, J., Zhu, J., Lovenberg, T.W., Liu, C. Neuroendocrinology (2005) [Pubmed]
 
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