The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review: 

TRGJP  -  T cell receptor gamma joining P

Homo sapiens

Synonyms: JP, TCRGJP
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on TRGJP

  • After reduction with dithiothreitol this material was recovered in an elution volume identical to that of purified hJP and corresponding to a mol wt of ca. 3000 [1].
  • This result was corroborated using HPLC purification to determine both amidated and glycine-extended forms of JP [2].
  • Plasma IR-JP had circadian variations and responded to the metyrapone test in a manner strictly similar to that of ACTH and lipotropins (LPHs) [3].
  • Normal male volunteers at 0800 h had plasma IR-JP values ranging from undetectable (< 6 pmol/L) to 28 pmol/L; all values were suppressed by the overnight 1 mg dexamethasone test [3].
  • The other two variants were identified as human JP with a free cysteine residue and human JP dimer and accounted for 35% and 15%, respectively, of the total purified [4].
 

Biological context of TRGJP

 

Anatomical context of TRGJP

  • We have examined the response of aldosterone to beta-endorphin (beta-End) and joining peptide (JP) and compared these with the response to ACTH using eight cell suspensions prepared from human adrenal glands [6].
 

Associations of TRGJP with chemical compounds

  • The predominant form of human JP, accounting for about 50% of the total purified, was found to be conjugated to glutathione through the lone cysteine residue at position 9 [4].
  • Furthermore, JP stimulated aldosterone biosynthesis (41 +/- 16 fmol/10(4) cells above basal; p < 0.05), only at the highest concentration used, 10(-6) M [6].
  • JP (10(-10) M) inhibited ACTH-stimulated cortisol production so that the mean values fell to 5186 +/- 2588 and also inhibited DHEA production, from 240 +/- 48 to 180 +/- 33 pmol/10(6) cells [7].
  • These results suggest that the relative production of androgen to cortisol is greater in response to beta-End and JP than in response to ACTH [7].
  • NPP and ACTH, but not JP, enhanced LH release concentration-dependently [8].
 

Analytical, diagnostic and therapeutic context of TRGJP

  • The joining peptide (JP) and the N-terminal peptide of proopiomelanocortin (NPP) were isolated from an acid-acetone extract of the distal lobe of the pituitary of the bullfrog, Rana catesbeiana, and purified by gel filtration and reverse-phase high performance liquid chromatography [5].
  • Northern blot analysis showed that the probe derived from JP-GAL hybridized to a single 2.6 kb RNA [9].
  • Labeling and immunoprecipitation experiments confirmed that three proopiomelanocortin (POMC)-derived peptides, the N-terminal peptide of POMC (NPP), joining peptide (JP) and adrenocorticotropic hormone (ACTH), were released by the bullfrog (Rana catesbeiana) anterior pituitary [8].

References

  1. Human joining peptide: a proopiomelanocortin product secreted as a homodimer. Bertagna, X., Camus, F., Lenne, F., Girard, F., Luton, J.P. Mol. Endocrinol. (1988) [Pubmed]
  2. Biosynthesis of amidated joining peptide from pro-adrenocorticotropin-endorphin. Cullen, E.I., Mains, R.E. Mol. Endocrinol. (1987) [Pubmed]
  3. Plasma immunoreactive joining peptide in man: a new marker of proopiomelanocortin processing and corticotroph function. Phlipponneau, M., Lenne, F., Proeschel, M.F., Girard, F., Luton, J.P., Bertagna, X. J. Clin. Endocrinol. Metab. (1993) [Pubmed]
  4. Isolation and characterization of three forms of joining peptide from adult human pituitaries: lack of adrenal androgen-stimulating activity. Robinson, P., Bateman, A., Mulay, S., Spencer, S.J., Jaffe, R.B., Solomon, S., Bennett, H.P. Endocrinology (1991) [Pubmed]
  5. Purification and characterization of joining peptide and N-terminal peptide of proopiomelanocortin from the pars distalis of the bullfrog pituitary. Iwamuro, S., Hayashi, H., Delbende, C., Vaudry, H., Kikuyama, S. Peptides (1992) [Pubmed]
  6. Non-ACTH POMC fragments stimulate aldosterone production by human adrenal cells in vitro. Molloy, E.S., Clarke, D.M., Fearon, U.M., Cunningham, S.K., McKenna, T.J. Steroids (1998) [Pubmed]
  7. The steroidogenic effects of beta-endorphin and joining peptide: a potential role in the modulation of adrenal androgen production. Clarke, D., Fearon, U., Cunningham, S.K., McKenna, T.J. J. Endocrinol. (1996) [Pubmed]
  8. Stimulation by proopiomelanocortin-derived peptides of LH release by bullfrog dispersed anterior pituitary cells. Aida, T., Oguchi, A., Iwamuro, S., Yamamoto, K., Kikuyama, S. Zool. Sci. (1997) [Pubmed]
  9. Molecular cloning of beta-galactosidase from Japanese pear (Pyrus pyrifolia) and its gene expression with fruit ripening. Tateishi, A., Inoue, H., Shiba, H., Yamaki, S. Plant Cell Physiol. (2001) [Pubmed]
 
WikiGenes - Universities