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=== Aiding gastrointestinal function ===
=== Aiding gastrointestinal function ===
{{cleanup|section|reason=this section contains weasel words|date=June 2012}}
{{cleanup|section|reason=this section contains jargon|date=June 2012}}
Studies link glutamine-enriched diets with maintenance of [[Enterocyte|gut barrier]] function and cell differentiation.<ref>{{cite doi|10.1177/014860719902300516}}</ref> Glutamine may help to protect the lining of the gastrointestinal tract or mucosa. It has been suggested that people who have inflammatory bowel disease IBD (ulcerative colitis and Crohn' s disease) may not have enough glutamine. However, two clinical trials found that taking glutamine supplements did not improve symptoms of Crohn' s disease.<ref>{{cite pmid|10630444}}</ref>
Glutamine-enriched diets have been linked with maintenance of [[Enterocyte|gut barrier]] function and cell differentiation,<ref>{{cite doi|10.1177/014860719902300516}}</ref> suggesting that glutamine may help to protect the lining of the gastrointestinal tract or mucosa. It has been suggested{{By whom}} that people who have [[inflammatory bowel disease]] (ulcerative colitis and Crohn' s disease) may not have enough glutamine. However, two clinical trials found that taking glutamine supplements did not improve symptoms of Crohn' s disease.<ref>{{cite pmid|10630444}}</ref>


==See also==
==See also==

Revision as of 01:35, 21 September 2012

"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
Names
IUPAC name
Glutamine
Other names
2-Amino-4-carbamoylbutanoic acid; (levo)glutamide
Identifiers
3D model (JSmol)
Abbreviations Gln, Q
ChEBI
ChEMBL
ChemSpider
ECHA InfoCard 100.000.266 Edit this at Wikidata
KEGG
UNII
  • InChI=1S/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10) checkY
    Key: ZDXPYRJPNDTMRX-UHFFFAOYSA-N checkY
  • InChI=1/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10)
    Key: ZDXPYRJPNDTMRX-UHFFFAOYAL
  • O=C(N)CCC(N)C(=O)O
Properties
C5H10N2O3
Molar mass 146.146 g·mol−1
Melting point 185–186 °C decomp.
soluble
+6.5º (H2O, c = 2)
Supplementary data page
Glutamine (data page)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
☒N verify (what is checkY☒N ?)

Glutamine (abbreviated as Gln or Q) is one of the 20 amino acids encoded by the standard genetic code. It is not recognized as an essential amino acid but may become conditionally essential in certain situations, including intensive athletic training or certain gastrointestinal disorders.[citation needed] 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.[2]

Structure

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

Functions

Glutamine plays a role in a variety of biochemical functions including:

Producing and consuming organs

Producers

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.[6] 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.[2]

Consumers

The most eager consumers of glutamine are the cells of intestines,[2] the kidney cells for the acid base balance, activated immune cells[7] and many cancer cells.[5] In respect to the last point mentioned, different glutamine analogues such as DON, Azaserine or Acivicin are tested as anti-cancer drugs.

Examples for the usage of glutamine

In catabolic states of injury and illness, glutamine becomes conditionally-essential (requiring intake from food or supplements).[8] 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.[8][unreliable source?] Glutamine is also marketed as a supplement used for muscle growth in weightlifting, bodybuilding, endurance, and other sports. Evidence indicates that glutamine when orally loaded may increase plasma HGH levels by stimulating the anterior pituitary gland.[9] In biological research, L-glutamine is commonly added to the media in cell culture.[10]

Aiding recovery after surgery

It is also known that glutamine has various 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 that 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 had no glutamine within their dietary regimen, all without any side-effects.[11]

Nutrition

Occurrences in nature

Glutamine is the most abundant naturally occurring, non-essential amino acid in the human body and one of the few amino acids that can directly cross the blood–brain barrier.[12] 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.[8]

Dietary sources

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.[8]

Aiding gastrointestinal function

Glutamine-enriched diets have been linked with maintenance of gut barrier function and cell differentiation,[13] suggesting that glutamine may help to protect the lining of the gastrointestinal tract or mucosa. It has been suggested[by whom?] that people who have inflammatory bowel disease (ulcerative colitis and Crohn' s disease) may not have enough glutamine. However, two clinical trials found that taking glutamine supplements did not improve symptoms of Crohn' s disease.[14]

See also

References

  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. ^ a b c d Brosnan JT (2003). "Interorgan amino acid transport and its regulation". J. Nutr. 133 (6 Suppl 1): 2068S–2072S. PMID 12771367. {{cite journal}}: Unknown parameter |month= ignored (help)
  3. ^ 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.{{cite book}}: CS1 maint: multiple names: authors list (link)
  4. ^ Attention: This template ({{cite doi}}) is deprecated. To cite the publication identified by doi:10.1002/bies.20063, please use {{cite journal}} (if it was published in a bona fide academic journal, otherwise {{cite report}} with |doi=10.1002/bies.20063 instead.
  5. ^ a b Attention: This template ({{cite doi}}) is deprecated. To cite the publication identified by doi:10.1083/jcb.200703099, please use {{cite journal}} (if it was published in a bona fide academic journal, otherwise {{cite report}} with |doi=10.1083/jcb.200703099 instead.
  6. ^ Attention: This template ({{cite doi}}) is deprecated. To cite the publication identified by doi:10.1590/S0100-879X2003000200002, please use {{cite journal}} (if it was published in a bona fide academic journal, otherwise {{cite report}} with |doi=10.1590/S0100-879X2003000200002 instead.
  7. ^ Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 11533304, please use {{cite journal}} with |pmid=11533304 instead.
  8. ^ a b c d "Glutamine". University of Maryland Medical Center. 2011-05-24. Retrieved 2012-06-24.
  9. ^ Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 7733028, please use {{cite journal}} with |pmid=7733028 instead.
  10. ^ 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...
  11. ^ Attention: This template ({{cite doi}}) is deprecated. To cite the publication identified by doi:10.1097/00000658-199802000-00022, please use {{cite journal}} (if it was published in a bona fide academic journal, otherwise {{cite report}} with |doi=10.1097/00000658-199802000-00022 instead.
  12. ^ Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 9580550, please use {{cite journal}} with |pmid=9580550 instead.
  13. ^ Attention: This template ({{cite doi}}) is deprecated. To cite the publication identified by doi:10.1177/014860719902300516, please use {{cite journal}} (if it was published in a bona fide academic journal, otherwise {{cite report}} with |doi=10.1177/014860719902300516 instead.
  14. ^ Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 10630444, please use {{cite journal}} with |pmid=10630444 instead.
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