Procorticotrophin-releasing hormone: endoproteolytic processing and differential release of its derived peptides within AtT20 cells

@article{Perone1998ProcorticotrophinreleasingHE,
  title={Procorticotrophin-releasing hormone: endoproteolytic processing and differential release of its derived peptides within AtT20 cells},
  author={Marcelo J. Perone and C. A Murray and Oscar A. Brown and S. Gibson and Alex D. White and Elizabeth A. Linton and Anthony V. Perkins and P. R. Lowenstein and Maria Graciela Castro},
  journal={Molecular and Cellular Endocrinology},
  year={1998},
  volume={142},
  pages={191-202}
}

Prothyrotropin-releasing Hormone Targets Its Processing Products to Different Vesicles of the Secretory Pathway*

The data show that pro-TRH-derived peptides are differentially sorted within the secretory pathway and that the initial cleavage in the trans-Golgi network is key to this process.

Corticotropin and Corticotropin-Releasing Hormone

The results demonstrate that the HSV1 recombinant vector expressing the fulllength CRH precursor molecule constitutes an excellent delivery system for both cell lines and postmitotic neurons in vitro, which has enabled the study of targeting, endoproteolytic processing and biological activity of this neuropeptide precursor.

Processing of procorticotropin-releasing hormone (pro-CRH): molecular forms of CRH in normal and preeclamptic pregnancy.

The studies using maternal plasma indicate that CRH(1-41) is the only one of the pro-CRH fragments studied to be maintained in significant amounts in the maternal circulation and also the only fragment studied for which a specific plasma binding protein exists.

Corticotropin releasing hormone and proopiomelanocortin involvement in the cutaneous response to stress.

Cutaneous expression of the CRH/POMC system is highly organized, encoding mediators and receptors similar to the hypothalamic-pituitary-adrenal (HPA) axis, that in the skin is expressed as a highly localized response which neutralizes noxious stimuli and attendant immune reactions.

The Cell Biology Neuropeptide Hormones

This chapter discusses the discovery and chemical characterization of the first identified hypothalamic releasing factor, thyrotropin-releasing hormone (pyroGlu-His-ProNH2), which provided ultimate confirmation for the founding principles of neuroendocrinology which resulted later in the discovery of other releasing factor peptides.

Generation of a Recombinant Herpes Simplex Virus Type 1 Expressing the Rat Corticotropin- Releasing Hormone Precursor: Endoproteolytic Processing, Intracellular Targeting and Biological Activity

The results demonstrate that the HSV1 recombinant vector expressing the full-length CRH precursor molecule constitutes an excellent delivery system for both cell lines and postmitotic neurons in vitro, which has enabled the study of targeting, endoproteolytic processing and biological activity of this neuropeptide precursor.

Characterization of a cDNA encoding a novel avian hypothalamic neuropeptide exerting an inhibitory effect on gonadotropin release.

GnIH is a hypothalamic factor responsible for the negative regulation of gonadotropin secretion and the presence of a novel RFamide peptide family containing a C-terminal -LPXRF-NH(2) sequence has been revealed.

Cutaneous expression of corticotropin‐releasing hormone (CRH), urocortin, and CRH receptors

  • A. SlominskiJ. Wortsman E. Wei
  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2001
The cutaneous CRH/POMC expression is highly reactive to common stressors such as immune cytokines, ultraviolet radiation, cutaneous pathology, or even the physiological changes associated with the hair cycle phase, and similar to its central analog, the local expression and action of CRH / POMC elements appear to be highly organized and entrained, representing general mechanism of cutaneous response to stressful stimuli.

Advances in understanding corticotrophin-releasing hormone gene expression.

In AtT20 cells multiple response elements coordinate a response to cAMP and glucocorticoids while in placental cells the CRE acts in isolation, which lead to responses that meet specific physiological needs.

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The results suggest that the endogenous CRH produced by the transfected R1 and R4 cells may cause down-regulation of their CRH receptors, and thus exogenous CRH cannot cause further stimulation of ACTH release in these cells.

Expression of Biologically Active Procorticotrophin‐Releasing Hormone (proCRH) in Stably Transfected CHO‐K1 Cells: Characterization of Nuclear proCRH

Both the cytoplasmic and nuclear species of IR‐CRH displayed an apparent molecular weight of approximately 19 kDa, consistent with the size of the uncleaved CRH precursor molecule.

Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT-20 cells.

In AtT-20 and rat pituitary cells, processing of POMC through at least two endo- and exoproteolytic cleavage steps and alpha-amidation of joining peptide begin in the trans Golgi subcompartment, it is concluded that this Golgi cisterna as well as secretion granules contain the active enzymes necessary for proteolytic processing and alpha -amidation.

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