User:Powell Cat/Prohormone
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A prohormone is a committed precursor of a hormone comprised of peptide hormones synthesized together, having a minimal hormonal effect by itself but can travel the blood stream as a hormone in an inactivated form, ready to be activated later in the cell by post-translational modification.[1][2]
The body naturally produces prohormones as a way to regulate hormone expression, making them an optimal storage and transportation unit for inactive hormones. Once prohormones are needed to be expressed, prohormone convertase, a protein, cleaves the prohormones and separates them into one or more active hormones.[3]
Examples of natural, human prohormones include proinsulin and pro-opiomelanocortin.
Many prohormones are labeled as anabolic steroid precursors, used as ergogenic or anabolic agents for muscle growth.[4] A commonly consumed example of said precursors are androstenedione and androstenediol, both of which currently are banned substances in the United States.[4][5]
Structure
Prohormones vary considerably in length and design, as do peptide hormones, but their base structure is the same.
Function
Prohormone
Prohormones allow for transport and storage of usually-active proteins as inactive peptide chains
- example: natural vitamin D is a prohormone[6]
- converts prohormone to hormone via endoproteolytic cleavage, allowing for removal of extended amino acid residues that hinder the inactive proteins from being active[3]
- allows for regulation of hormone content in the body as when in inactive form, they have minimal effect on the body
For peptide hormones, the conversion process from prohormone to hormone (pro-protein to protein) typically occurs after being exported to the endoplasmic reticulum and often requires multiple processing enzymes.[7] Proamylin, which is cosecreted with proinsulin, requires the above three factors and an amidating monooxygenase to convert itself to an active hormone.[8] Some pro-protein precursors, such as preproinsulin, also go through this process, with the added step of removing a signal peptide by signal peptidases, to convert said precursors into prohormones.[7]
Uses
Prohormone supplements
- health risk
- relatively unknown
- list of side effects
- most banned in the U.S.
See also
References
Granados, Jorge; Gillum, Trevor L.; Christmas, Kevin M.; Kuennen, Matthew R. (2014-03-01). "Prohormone supplement 3β-hydroxy-5α-androst-1-en-17-one enhances resistance training gains but impairs user health". Journal of Applied Physiology. 116 (5): 560–569. doi:10.1152/japplphysiol.00616.2013. ISSN 8750-7587
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- ^ Friedman, Theodore C.; Cool, David R. (2004-01-01), Martini, Luciano (ed.), "Prohormones", Encyclopedia of Endocrine Diseases, New York: Elsevier, pp. 91–98, doi:10.1016/b0-12-475570-4/01074-x, ISBN 978-0-12-475570-3, retrieved 2021-12-04
- ^ Miller, Benjamin Frank (1997). Miller-Keane Encyclopedia & dictionary of medicine, nursing & allied health. Claire Brackman Keane (6th ed.). Philadelphia: Saunders. ISBN 0-7216-6278-1. OCLC 36465055.
- ^ a b Dhanvantari, Savita; Cawley, Niamh X.; Loh, Y. Peng (2004-01-01), Martini, Luciano (ed.), "Prohormone Convertases", Encyclopedia of Endocrine Diseases, New York: Elsevier, pp. 84–90, ISBN 978-0-12-475570-3, retrieved 2021-12-09
- ^ a b Powers, Michael E. (2002). "The Safety and Efficacy of Anabolic Steroid Precursors: What is the Scientific Evidence?". Journal of Athletic Training. 37 (3): 300–305. ISSN 1062-6050. PMID 16558675.
- ^ Pitts, Joseph R. (2014-12-18). "Text - H.R.4771 - 113th Congress (2013-2014): Designer Anabolic Steroid Control Act of 2014". www.congress.gov. Retrieved 2021-12-09.
- ^ Demer, Linda L.; Hsu, Jeffrey J.; Tintut, Yin (2018-05-25). "Steroid Hormone Vitamin D". Circulation Research. 122 (11): 1576–1585. doi:10.1161/CIRCRESAHA.118.311585. PMC 6122607. PMID 29798901.
{{cite journal}}: CS1 maint: PMC format (link) - ^ a b Alberts, Bruce (2002). Molecular biology of the cell. Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (4th ed ed.). New York: Garland Science. ISBN 0-8153-3218-1. OCLC 48122761.
{{cite book}}:|edition=has extra text (help) - ^ "Amylin Proprotein Processing Generates Progressively More Amyloidogenic Peptides that Initially Sample the Helical State". Biochemistry. 47: 9900–9910. August 19, 2008 – via American Chemical Society.