Glutamine

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"Gln" redirects here. For other uses, see GLN (disambiguation).
L-Glutamine
Skeletal formula of the L-isomer
Ball-and-stick model of the L-isomer as a zwitterion
Identifiers
Abbreviations Gln, Q
CAS number 56-85-9 YesY
PubChem 738
ChemSpider 718 YesY
UNII 0RH81L854J YesY
EC-number 200-292-1
KEGG C00303 YesY
ChEBI CHEBI:28300 YesY
ChEMBL CHEMBL930 N
IUPHAR ligand 723
ATC code A16AA03
Jmol-3D images Image 1
Properties[1]
Molecular formula C5H10N2O3
Molar mass 146.14 g mol−1
Melting point decomposes around 185°C
Solubility in water soluble
Chiral rotation [α]D +6.5º (H2O, c = 2)
Supplementary data page
Structure and
properties
n, εr, etc.
Thermodynamic
data
Phase behaviour
Solid, liquid, gas
Spectral data UV, IR, NMR, MS
Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
 N (verify) (what is: YesY/N?)
Infobox references

Glutamine (abbreviated as Gln or Q, and often called L-glutamine) is one of the 20 amino acids encoded by the standard genetic code. It is considered a conditionally essential amino acid.[2] Its side-chain is an amide formed by replacing the side-chain hydroxyl of glutamic acid with an amine functional group, making it the amide of glutamic acid. Its codons are CAA and CAG. In human blood, glutamine is the most abundant free amino acid, with a concentration of about 500–900 µmol/l.[3]

Structure[edit]

Glutamine zwitterionic forms at neutral pH: L-glutamine (left) and D-glutamine

Functions[edit]

Glutamine plays a role in a variety of biochemical functions:

Producing and consuming organs[edit]

Producers[edit]

Glutamine is synthesized by the enzyme glutamine synthetase from glutamate and ammonia. The most relevant glutamine-producing tissue is the muscle mass, accounting for about 90% of all glutamine synthesized. Glutamine is also released, in small amounts, by the lung and the brain.[7] Although the liver is capable of relevant glutamine synthesis, its role in glutamine metabolism is more regulatory than producing, since the liver takes up large amounts of glutamine derived from the gut.[3]

Consumers[edit]

The most eager consumers of glutamine are the cells of intestines,[3] the kidney cells for the acid-base balance, activated immune cells,[8] and many cancer cells.[6] In respect to the last point mentioned, different glutamine analogues, such as DON, Azaserine or Acivicin, are tested as anticancer drugs.

Examples for the usage of glutamine[edit]

In catabolic states of injury and illness, glutamine becomes conditionally essential (requiring intake from food or supplements).[9] Glutamine has been studied extensively over the past 10–15 years, and has been shown to be useful in treatment of injuries, trauma, burns, and treatment-related side effects of cancer, as well as in wound healing for postoperative patients. Glutamine is also marketed as a supplement used for muscle growth in weightlifting, bodybuilding, endurance, and other sports. Evidence indicates glutamine, when orally loaded, may increase plasma HGH levels by stimulating the anterior pituitary gland.[10] In biological research, L-glutamine is commonly added to the media in cell culture.[11][12] However, the high level of glutamine in the culture media may inhibit other amino acid transport activities.[13]

Aiding recovery after surgery[edit]

Glutamine is also known to have various side effects in reducing healing time after operations. Hospital-stay times after abdominal surgery can be reduced by providing parenteral nutrition regimens containing high amounts of glutamine to patients. Clinical trials have revealed patients on supplementation regimens containing glutamine have improved nitrogen balances, generation of cysteinyl-leukotrienes from polymorphonuclear neutrophil granulocytes, and improved lymphocyte recovery and intestinal permeability (in postoperative patients), in comparison to those that have no glutamine within their dietary regimen, all without any side effects.[14]

Nutrition[edit]

Occurrences in nature[edit]

Glutamine is the most abundant naturally occurring, nonessential amino acid in the human body, and one of the few amino acids that can directly cross the blood–brain barrier.[15] In the body, it is found circulating in the blood, as well as stored in the skeletal muscles. It becomes conditionally essential (requiring intake from food or supplements) in states of illness or injury.[9]

Dietary sources[edit]

Dietary sources of L-glutamine include beef, chicken, fish, eggs, milk, dairy products, wheat, cabbage, beets, beans, spinach, and parsley. Small amounts of free L-glutamine are also found in vegetable juices.[9]

See also[edit]

References[edit]

  1. ^ Weast, Robert C., ed. (1981). CRC Handbook of Chemistry and Physics (62nd ed.). Boca Raton, FL: CRC Press. p. C-311. ISBN 0-8493-0462-8. .
  2. ^ Dietary Reference Intakes: The Essential Guide to Nutrient Requirements, published by the Institute of Medicine's Food and Nutrition Board, currently available online at http://fnic.nal.usda.gov/dietary-guidance/dietary-reference-intakes/dri-reports
  3. ^ a b c d Brosnan, John T. (June 2003). "Interorgan amino acid transport and its regulation". J. Nutr. 133 (6 Suppl 1): 2068S–2072S. PMID 12771367. open access publication - free to read
  4. ^ Hall, John E.; Guyton, Arthur C. (2006). Textbook of medical physiology (11th ed.). St. Louis, Mo: Elsevier Saunders. p. 393. ISBN 0-7216-0240-1. 
  5. ^ Aledo, J. C. (2004). "Glutamine breakdown in rapidly dividing cells: Waste or investment?". BioEssays 26 (7): 778–785. doi:10.1002/bies.20063. PMID 15221859.  edit
  6. ^ a b Yuneva, M.; Zamboni, N.; Oefner, P.; Sachidanandam, R.; Lazebnik, Y. (2007). "Deficiency in glutamine but not glucose induces MYC-dependent apoptosis in human cells". The Journal of Cell Biology 178 (1): 93–105. doi:10.1083/jcb.200703099. PMC 2064426. PMID 17606868.  edit
  7. ^ Newsholme, P.; Lima, M. M. R.; Procopio, J.; Pithon-Curi, T. C.; Doi, S. Q.; Bazotte, R. B.; Curi, R. (2003). "Glutamine and glutamate as vital metabolites". Brazilian Journal of Medical and Biological Research 36 (2): 153–163. doi:10.1590/S0100-879X2003000200002. PMID 12563517.  edit
  8. ^ Newsholme, P. (2001). "Why is L-glutamine metabolism important to cells of the immune system in health, postinjury, surgery or infection?". The Journal of nutrition 131 (9 Suppl): 2515S–2522S; discussion 2522S–4S. PMID 11533304.  edit
  9. ^ a b c "Glutamine". Medical Reference Guide. University of Maryland Medical Center. 2011-05-24. Archived from the original on 2009-12-09. Retrieved 2014-03-03. 
  10. ^ Welbourne, T. C. (1995). "Increased plasma bicarbonate and growth hormone after an oral glutamine load". The American journal of clinical nutrition 61 (5): 1058–1061. PMID 7733028.  edit
  11. ^ Thilly, William G. (1986). Mammalian cell technology. London: Butterworths. p. 110. ISBN 0-409-90029-X. Retrieved 2012-06-22. "13 amino acids in Eagle's popular culture medium...are arginine, cyst(e)ine, glutamine..." 
  12. ^ Yang H, Roth CM, Ierapetritou MG. (2011) Analysis of amino acid supplementation effects on hepatocyte cultures using flux balance analysis, OMICS, A Journal of Integrative Biology, 15(7-8): 449–460.
  13. ^ Yang H, Ierapetritou MG, Roth CM. (2010) Effects of amino acid transport limitations on cultured hepatocytes, Biophysical Chemistry, 152(1-3):89-98.
  14. ^ Morlion, B. J.; Stehle, P.; Wachtler, P.; Siedhoff, H. P.; Köller, M.; König, W.; Fürst, P.; Puchstein, C. (1998). "Total Parenteral Nutrition with Glutamine Dipeptide After Major Abdominal Surgery". Annals of Surgery 227 (2): 302–308. doi:10.1097/00000658-199802000-00022. PMC 1191250. PMID 9488531.  edit
  15. ^ Lee, W. J.; Hawkins, R. A.; Viña, J. R.; Peterson, D. R. (1998). "Glutamine transport by the blood-brain barrier: A possible mechanism for nitrogen removal". The American journal of physiology 274 (4 Pt 1): C1101–C1107. PMID 9580550.  edit

External links[edit]