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Gamma-glutamyltransferase

January 01, 1970

Gamma-glutamyltransferase (also γ-glutamyltransferase, GGT, gamma-GT, gamma-glutamyl transpeptidase;[1] EC 2.3.2.2) is a transferase (a type of enzyme) that catalyzes the transfer of gamma-glutamyl functional groups from molecules such as glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate).[1][2]: 268  GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione as well as drug and xenobiotic detoxification.[3] Other lines of evidence indicate that GGT can also exert a pro-oxidant role, with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology.[4] This transferase is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker.

Gamma-glutamyl transpeptidase
Identifiers
SymbolG_glu_transpept
PfamPF01019
InterProIPR000101
PROSITEPDOC00404
Membranome274
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Gamma-glutamyltransferase
Identifiers
EC no.2.3.2.2
CAS no.9046-27-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
gamma-glutamyltransferase 1
Identifiers
SymbolGGT1
Alt. symbolsGGT
NCBI gene2678
HGNC4250
OMIM231950
RefSeqNM_001032364
UniProtP19440
Other data
EC number2.3.2.2
LocusChr. 22 q11.1-11.2
Search for
StructuresSwiss-model
DomainsInterPro
gamma-glutamyltransferase 2
Identifiers
SymbolGGT2
Alt. symbolsGGT
NCBI gene2679
HGNC4251
OMIM137181
RefSeqNM_002058
UniProtP36268
Other data
EC number2.3.2.2
LocusChr. 22 q11.1-11.2
Search for
StructuresSwiss-model
DomainsInterPro

Nomenclature edit

The name γ-glutamyltransferase is preferred by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.[5][2] The Expert Panel on Enzymes of the International Federation of Clinical Chemistry also used this name.[6][2] The older name is gamma-glutamyl transpeptidase (GGTP).[2]

Function edit

GGT is present in the cell membranes of many tissues, including the kidneys, bile duct, pancreas, gallbladder, spleen, heart, brain, and seminal vesicles.[7] It is involved in the transfer of amino acids across the cellular membrane[8] and leukotriene metabolism.[9] It is also involved in glutathione metabolism by transferring the glutamyl moiety to a variety of acceptor molecules including water, certain L-amino acids, and peptides, leaving the cysteine product to preserve intracellular homeostasis of oxidative stress.[10][11] This general reaction is:

(5-L-glutamyl)-peptide + an amino acid ⇌ peptide + 5-L-glutamyl amino acid

Biochemistry edit

In prokaryotes and eukaryotes, GGT consists of two polypeptide chains, a heavy and a light subunit, processed from a single chain precursor by an autocatalytic cleavage.[12] The active site of GGT is known to be located in the light subunit.[citation needed]

Co-translational N-glycosylation serves a significant role in the proper autocatalytic cleavage and proper folding of GGT. Single site mutations at asparagine residues were shown to result in a functionally active yet slightly less thermally stable version of the enzyme in vitro, while knockout of all asparagine residues resulted in an accumulation of the uncleaved, propeptide form of the enzyme.[12]

Clinical significance edit

"GGT test" redirects here. For the test known as GTT, see Glucose tolerance test.

GGT is predominantly used as a diagnostic marker for liver disease.[citation needed] Elevated serum GGT activity can be found in diseases of the liver, biliary system, pancreas and kidneys.[13][14] Latent elevations in GGT are typically seen in patients with chronic viral hepatitis infections often taking 12 months or more to present.[citation needed]

Individual test results should always be interpreted using the reference range from the laboratory that performed the test, though example reference ranges are 15–85 IU/L for men, and 5–55 IU/L for women.[15] GGT is similar to alkaline phosphatase (ALP) in detecting disease of the biliary tract. Indeed, the two markers correlate well, though there are conflicting data about whether GGT has better sensitivity.[16][17] In general, ALP is still the first test for biliary disease. The main value of GGT is in verifying that ALP elevations are, in fact, due to biliary disease; ALP can also be increased in certain bone diseases, but GGT is not.[17]

Alcohol use edit

GGT is elevated by ingestion of large quantities of alcohol (needs reference) However, determination of high levels of total serum GGT activity is not specific to alcohol intoxication,[18] and the measurement of selected serum forms of the enzyme offer more specific information.[19] Isolated elevation or disproportionate elevation compared to other liver enzymes (such as ALT or alanine transaminase) can indicate harmful alcohol use or alcoholic liver disease,[20] and can indicate excess alcohol consumption up to 3 or 4 weeks prior to the test.[citation needed] The mechanism for this elevation is unclear. Alcohol might increase GGT production by inducing hepatic microsomal production, or it might cause the leakage of GGT from hepatocytes.[21]

Xenobiotics edit

Numerous drugs can raise GGT levels, including barbiturates and phenytoin.[22] GGT elevation has also been occasionally reported following nonsteroidal anti-inflammatory drugs (including aspirin), St. John's wort and kava.[23]

Cardiovascular disease edit

More recently, slightly elevated serum GGT has also been found to correlate with cardiovascular diseases and is under active investigation as a cardiovascular risk marker. GGT in fact accumulates in atherosclerotic plaques,[24] suggesting a potential role in pathogenesis of cardiovascular diseases,[25] and circulates in blood in the form of distinct protein aggregates,[19] some of which appear to be related to specific pathologies such as metabolic syndrome, alcohol addiction and chronic liver disease.

Elevated levels of GGT can also be due to congestive heart failure.[26]

Neoplasms edit

GGT is expressed in high levels in many different tumors. It is known to accelerate tumor growth and to increase resistance to cisplatin in tumors.[27]

Examples edit

Human proteins that belong to this family include GGT1, GGT2, GGT6, GGTL3, GGTL4, GGTLA1 and GGTLA4.

References edit

  1. ^ a b Tate SS, Meister A (1985). "[50] γ-Glutamyl transpeptidase from kidney". gamma-Glutamyl transpeptidase from kidney. Methods in Enzymology. Vol. 113. pp. 400–19. doi:10.1016/S0076-6879(85)13053-3. ISBN 978-0-12-182013-8. PMID 2868390.
  2. ^ a b c d Whitfield JB (August 2001). "Gamma glutamyl transferase". Critical Reviews in Clinical Laboratory Sciences. 38 (4): 263–355. doi:10.1080/20014091084227. PMID 11563810. S2CID 1070555.
  3. ^ Courtay C, Oster T, Michelet F, Visvikis A, Diederich M, Wellman M, Siest G (June 1992). "Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues". Biochemical Pharmacology. 43 (12): 2527–33. doi:10.1016/0006-2952(92)90140-E. PMID 1378736.
  4. ^ Dominici S, Paolicchi A, Corti A, Maellaro E, Pompella A (2005). "Prooxidant Reactions Promoted by Soluble and Cell-Bound γ-Glutamyltransferase Activity". Prooxidant reactions promoted by soluble and cell-bound gamma-glutamyltransferase activity. Methods in Enzymology. Vol. 401. pp. 484–501. doi:10.1016/S0076-6879(05)01029-3. ISBN 978-0-12-182806-6. PMID 16399404.
  5. ^ "EC 2.3.2.2". International Union of Biochemistry and Molecular Biology. 2011. Retrieved 9 October 2016.
  6. ^ Shaw LM, Strømme JH, London JL, Theodorsen L (December 1983). "International Federation of Clinical Chemistry. Scientific Committee, Analytical Section. Expert Panel on Enzymes. IFCC methods for measurement of enzymes. Part 4. IFCC methods for gamma-glutamyltransferase [(gamma-glutamyl)-peptide: amino acid gamma-glutamyltransferase, EC 2.3.2.2]. IFCC Document, Stage 2, Draft 2, 1983-01 with a view to an IFCC Recommendation". Clinica Chimica Acta; International Journal of Clinical Chemistry. 135 (3): 315F–338F. doi:10.1016/0009-8981(83)90291-7. PMID 6141014.
  7. ^ Goldberg DM (1980). "Structural, functional, and clinical aspects of gamma-glutamyltransferase". CRC Critical Reviews in Clinical Laboratory Sciences. 12 (1): 1–58. doi:10.3109/10408368009108725. PMID 6104563.
  8. ^ Meister A (August 1974). "The gamma-glutamyl cycle. Diseases associated with specific enzyme deficiencies". Annals of Internal Medicine. 81 (2): 247–53. doi:10.7326/0003-4819-81-2-247. PMID 4152527.
  9. ^ Raulf M, Stüning M, König W (May 1985). "Metabolism of leukotrienes by L-gamma-glutamyl-transpeptidase and dipeptidase from human polymorphonuclear granulocytes". Immunology. 55 (1): 135–47. PMC 1453575. PMID 2860060.
  10. ^ Schulman JD, Goodman SI, Mace JW, Patrick AD, Tietze F, Butler EJ (July 1975). "Glutathionuria: inborn error of metabolism due to tissue deficiency of gamma-glutamyl transpeptidase". Biochemical and Biophysical Research Communications. 65 (1): 68–74. doi:10.1016/S0006-291X(75)80062-3. PMID 238530.
  11. ^ Yokoyama H (June 2007). "[Gamma glutamyl transpeptidase (gammaGTP) in the era of metabolic syndrome]". Nihon Arukōru Yakubutsu Igakkai Zasshi = Japanese Journal of Alcohol Studies & Drug Dependence (in Japanese). 42 (3): 110–24. PMID 17665541.
  12. ^ a b West MB, Wickham S, Quinalty LM, Pavlovicz RE, Li C, Hanigan MH (19 August 2011). "Autocatalytic cleavage of human gamma-glutamyl transpeptidase is highly dependent on N-glycosylation at asparagine 95". The Journal of Biological Chemistry. 286 (33): 28876–28888. doi:10.1074/jbc.M111.248823. ISSN 1083-351X. PMC 3190695. PMID 21712391.
  13. ^ Fine A, McIntosh WB (May 1975). "Elevation of Serum Gamma-Glutamyl Transpeptidase in End-Stage Chronic Renal Failure". Scottish Medical Journal. 20 (3): 113–115. doi:10.1177/003693307502000309. ISSN 0036-9330. PMID 242073. S2CID 23177210.
  14. ^ Endre ZH, Pickering JW, Walker RJ, Devarajan P, Edelstein CL, Bonventre JV, Frampton CM, Bennett MR, Ma Q, Sabbisetti VS, Vaidya VS, Walcher AM, Shaw GM, Henderson SJ, Nejat M, Schollum JB, George PM (2 May 2011). "Improved performance of urinary biomarkers of acute kidney injury in the critically ill by stratification for injury duration and baseline renal function". Kidney International. 79 (10): 1119–1130. doi:10.1038/ki.2010.555. ISSN 0085-2538. PMC 3884688. PMID 21307838.
  15. ^ Mannion CM (2012). General Laboratory Manual (PDF). Department of Pathology, Hackensack University Medical Centre. p. 129. Retrieved 20 February 2014.
  16. ^ Betro MG, Oon RC, Edwards JB (November 1973). "Gamma-glutamyl transpeptidase in diseases of the liver and bone". American Journal of Clinical Pathology. 60 (5): 672–8. doi:10.1093/ajcp/60.5.672. PMID 4148049.
  17. ^ a b Lum G, Gambino SR (April 1972). "Serum gamma-glutamyl transpeptidase activity as an indicator of disease of liver, pancreas, or bone". Clinical Chemistry. 18 (4): 358–62. doi:10.1093/clinchem/18.4.358. PMID 5012259.
  18. ^ Lamy J, Baglin MC, Ferrant JP, Weill J (1974). "Determination de la gamma-glutamyl transpeptidase senque des ethyliques a la suite du sevrage". Clin Chim Acta. 56 (2): 169–73. doi:10.1016/0009-8981(74)90225-3. PMID 4154814.
  19. ^ a b Franzini M, Bramanti E, Ottaviano V, Ghiri E, Scatena F, Barsacchi R, Pompella A, Donato L, Emdin M, Paolicchi A (March 2008). "A high performance gel filtration chromatography method for gamma-glutamyltransferase fraction analysis". Analytical Biochemistry. 374 (1): 1–6. doi:10.1016/j.ab.2007.10.025. hdl:11382/3163. PMID 18023410.
  20. ^ Kaplan MM, Matloff DS, Selinger MJ, Quaroni EG (1985). "Biochemical basis for serum enzyme abnormalities in alcoholic liver disease". In Chang NC, Chao HM (eds.). Early identification of alcohol abuse, Proceedings of a workshop October 31–November 1, 1983. Rockville, Maryland: National Institute on Alcohol Abuse and Alcoholism. pp. 186–198. LCCN 84601128. Research Monograph No. 17.
  21. ^ Barouki R, Chobert MN, Finidori J, Aggerbeck M, Nalpas B, Hanoune J (1983). "Ethanol effects in a rat hepatoma cell line: induction of gamma-glutamyltransferase". Hepatology. 3 (3): 323–9. doi:10.1002/hep.1840030308. PMID 6132864. S2CID 84080031.
  22. ^ Rosalki SB, Tarlow D, Rau D (August 1971). "Plasma gamma-glutamyl transpeptidase elevation in patients receiving enzyme-inducing drugs". Lancet. 2 (7720): 376–7. doi:10.1016/S0140-6736(71)90093-6. PMID 4105075.
  23. ^ "Kava Uses, Benefits & Dosage". Herbal Database. Drugs.com.
  24. ^ Emdin M, Pompella A, Paolicchi A (October 2005). "Gamma-glutamyltransferase, atherosclerosis, and cardiovascular disease: triggering oxidative stress within the plaque". Circulation. 112 (14): 2078–80. doi:10.1161/CIRCULATIONAHA.105.571919. PMID 16203922.
  25. ^ Pompella A, Emdin M, Passino C, Paolicchi A (2004). "The significance of serum gamma-glutamyltransferase in cardiovascular diseases". Clinical Chemistry and Laboratory Medicine. 42 (10): 1085–91. doi:10.1515/CCLM.2004.224. PMID 15552264. S2CID 4248204.
  26. ^ Ruttmann E, Brant LJ, Concin H, Diem G, Rapp K, Ulmer H (October 2005). "Gamma-glutamyltransferase as a risk factor for cardiovascular disease mortality: an epidemiological investigation in a cohort of 163,944 Austrian adults". Circulation. 112 (14): 2130–7. doi:10.1161/CIRCULATIONAHA.105.552547. PMID 16186419.
  27. ^ Hanigan MH, Gallagher BC, Townsend DM, Gabarra V (April 1999). "Gamma-glutamyl transpeptidase accelerates tumor growth and increases the resistance of tumors to cisplatin in vivo". Carcinogenesis. 20 (4): 553–559. doi:10.1093/carcin/20.4.553. ISSN 0143-3334. PMC 6522259. PMID 10223181.

External links edit

January 01, 1970
gamma, glutamyltransferase, also, glutamyltransferase, gamma, gamma, glutamyl, transpeptidase, transferase, type, enzyme, that, catalyzes, transfer, gamma, glutamyl, functional, groups, from, molecules, such, glutathione, acceptor, that, amino, acid, peptide, . Gamma glutamyltransferase also g glutamyltransferase GGT gamma GT gamma glutamyl transpeptidase 1 EC 2 3 2 2 is a transferase a type of enzyme that catalyzes the transfer of gamma glutamyl functional groups from molecules such as glutathione to an acceptor that may be an amino acid a peptide or water forming glutamate 1 2 268 GGT plays a key role in the gamma glutamyl cycle a pathway for the synthesis and degradation of glutathione as well as drug and xenobiotic detoxification 3 Other lines of evidence indicate that GGT can also exert a pro oxidant role with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology 4 This transferase is found in many tissues the most notable one being the liver and has significance in medicine as a diagnostic marker Gamma glutamyl transpeptidaseIdentifiersSymbolG glu transpeptPfamPF01019InterProIPR000101PROSITEPDOC00404Membranome274Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary Gamma glutamyltransferaseIdentifiersEC no 2 3 2 2CAS no 9046 27 9DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins gamma glutamyltransferase 1IdentifiersSymbolGGT1Alt symbolsGGTNCBI gene2678HGNC4250OMIM231950RefSeqNM 001032364UniProtP19440Other dataEC number2 3 2 2LocusChr 22 q11 1 11 2Search forStructuresSwiss modelDomainsInterPro gamma glutamyltransferase 2IdentifiersSymbolGGT2Alt symbolsGGTNCBI gene2679HGNC4251OMIM137181RefSeqNM 002058UniProtP36268Other dataEC number2 3 2 2LocusChr 22 q11 1 11 2Search forStructuresSwiss modelDomainsInterPro Contents 1 Nomenclature 2 Function 3 Biochemistry 4 Clinical significance 4 1 Alcohol use 4 2 Xenobiotics 4 3 Cardiovascular disease 4 4 Neoplasms 5 Examples 6 References 7 External linksNomenclature editThe name g glutamyltransferase is preferred by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology 5 2 The Expert Panel on Enzymes of the International Federation of Clinical Chemistry also used this name 6 2 The older name is gamma glutamyl transpeptidase GGTP 2 Function editGGT is present in the cell membranes of many tissues including the kidneys bile duct pancreas gallbladder spleen heart brain and seminal vesicles 7 It is involved in the transfer of amino acids across the cellular membrane 8 and leukotriene metabolism 9 It is also involved in glutathione metabolism by transferring the glutamyl moiety to a variety of acceptor molecules including water certain L amino acids and peptides leaving the cysteine product to preserve intracellular homeostasis of oxidative stress 10 11 This general reaction is 5 L glutamyl peptide an amino acid peptide 5 L glutamyl amino acidBiochemistry editIn prokaryotes and eukaryotes GGT consists of two polypeptide chains a heavy and a light subunit processed from a single chain precursor by an autocatalytic cleavage 12 The active site of GGT is known to be located in the light subunit citation needed Co translational N glycosylation serves a significant role in the proper autocatalytic cleavage and proper folding of GGT Single site mutations at asparagine residues were shown to result in a functionally active yet slightly less thermally stable version of the enzyme in vitro while knockout of all asparagine residues resulted in an accumulation of the uncleaved propeptide form of the enzyme 12 Clinical significance edit GGT test redirects here For the test known as GTT see Glucose tolerance test GGT is predominantly used as a diagnostic marker for liver disease citation needed Elevated serum GGT activity can be found in diseases of the liver biliary system pancreas and kidneys 13 14 Latent elevations in GGT are typically seen in patients with chronic viral hepatitis infections often taking 12 months or more to present citation needed Individual test results should always be interpreted using the reference range from the laboratory that performed the test though example reference ranges are 15 85 IU L for men and 5 55 IU L for women 15 GGT is similar to alkaline phosphatase ALP in detecting disease of the biliary tract Indeed the two markers correlate well though there are conflicting data about whether GGT has better sensitivity 16 17 In general ALP is still the first test for biliary disease The main value of GGT is in verifying that ALP elevations are in fact due to biliary disease ALP can also be increased in certain bone diseases but GGT is not 17 Alcohol use edit GGT is elevated by ingestion of large quantities of alcohol needs reference However determination of high levels of total serum GGT activity is not specific to alcohol intoxication 18 and the measurement of selected serum forms of the enzyme offer more specific information 19 Isolated elevation or disproportionate elevation compared to other liver enzymes such as ALT or alanine transaminase can indicate harmful alcohol use or alcoholic liver disease 20 and can indicate excess alcohol consumption up to 3 or 4 weeks prior to the test citation needed The mechanism for this elevation is unclear Alcohol might increase GGT production by inducing hepatic microsomal production or it might cause the leakage of GGT from hepatocytes 21 Xenobiotics edit Numerous drugs can raise GGT levels including barbiturates and phenytoin 22 GGT elevation has also been occasionally reported following nonsteroidal anti inflammatory drugs including aspirin St John s wort and kava 23 Cardiovascular disease edit More recently slightly elevated serum GGT has also been found to correlate with cardiovascular diseases and is under active investigation as a cardiovascular risk marker GGT in fact accumulates in atherosclerotic plaques 24 suggesting a potential role in pathogenesis of cardiovascular diseases 25 and circulates in blood in the form of distinct protein aggregates 19 some of which appear to be related to specific pathologies such as metabolic syndrome alcohol addiction and chronic liver disease Elevated levels of GGT can also be due to congestive heart failure 26 Neoplasms edit GGT is expressed in high levels in many different tumors It is known to accelerate tumor growth and to increase resistance to cisplatin in tumors 27 Examples editHuman proteins that belong to this family include GGT1 GGT2 GGT6 GGTL3 GGTL4 GGTLA1 and GGTLA4 References edit a b Tate SS Meister A 1985 50 g Glutamyl transpeptidase from kidney gamma Glutamyl transpeptidase from kidney Methods in Enzymology Vol 113 pp 400 19 doi 10 1016 S0076 6879 85 13053 3 ISBN 978 0 12 182013 8 PMID 2868390 a b c d Whitfield JB August 2001 Gamma glutamyl transferase Critical Reviews in Clinical Laboratory Sciences 38 4 263 355 doi 10 1080 20014091084227 PMID 11563810 S2CID 1070555 Courtay C Oster T Michelet F Visvikis A Diederich M Wellman M Siest G June 1992 Gamma glutamyltransferase nucleotide sequence of the human pancreatic cDNA Evidence for a ubiquitous gamma glutamyltransferase polypeptide in human tissues Biochemical Pharmacology 43 12 2527 33 doi 10 1016 0006 2952 92 90140 E PMID 1378736 Dominici S Paolicchi A Corti A Maellaro E Pompella A 2005 Prooxidant Reactions Promoted by Soluble and Cell Bound g Glutamyltransferase Activity Prooxidant reactions promoted by soluble and cell bound gamma glutamyltransferase activity Methods in Enzymology Vol 401 pp 484 501 doi 10 1016 S0076 6879 05 01029 3 ISBN 978 0 12 182806 6 PMID 16399404 EC 2 3 2 2 International Union of Biochemistry and Molecular Biology 2011 Retrieved 9 October 2016 Shaw LM Stromme JH London JL Theodorsen L December 1983 International Federation of Clinical Chemistry Scientific Committee Analytical Section Expert Panel on Enzymes IFCC methods for measurement of enzymes Part 4 IFCC methods for gamma glutamyltransferase gamma glutamyl peptide amino acid gamma glutamyltransferase EC 2 3 2 2 IFCC Document Stage 2 Draft 2 1983 01 with a view to an IFCC Recommendation Clinica Chimica Acta International Journal of Clinical Chemistry 135 3 315F 338F doi 10 1016 0009 8981 83 90291 7 PMID 6141014 Goldberg DM 1980 Structural functional and clinical aspects of gamma glutamyltransferase CRC Critical Reviews in Clinical Laboratory Sciences 12 1 1 58 doi 10 3109 10408368009108725 PMID 6104563 Meister A August 1974 The gamma glutamyl cycle Diseases associated with specific enzyme deficiencies Annals of Internal Medicine 81 2 247 53 doi 10 7326 0003 4819 81 2 247 PMID 4152527 Raulf M Stuning M Konig W May 1985 Metabolism of leukotrienes by L gamma glutamyl transpeptidase and dipeptidase from human polymorphonuclear granulocytes Immunology 55 1 135 47 PMC 1453575 PMID 2860060 Schulman JD Goodman SI Mace JW Patrick AD Tietze F Butler EJ July 1975 Glutathionuria inborn error of metabolism due to tissue deficiency of gamma glutamyl transpeptidase Biochemical and Biophysical Research Communications 65 1 68 74 doi 10 1016 S0006 291X 75 80062 3 PMID 238530 Yokoyama H June 2007 Gamma glutamyl transpeptidase gammaGTP in the era of metabolic syndrome Nihon Arukōru Yakubutsu Igakkai Zasshi Japanese Journal of Alcohol Studies amp Drug Dependence in Japanese 42 3 110 24 PMID 17665541 a b West MB Wickham S Quinalty LM Pavlovicz RE Li C Hanigan MH 19 August 2011 Autocatalytic cleavage of human gamma glutamyl transpeptidase is highly dependent on N glycosylation at asparagine 95 The Journal of Biological Chemistry 286 33 28876 28888 doi 10 1074 jbc M111 248823 ISSN 1083 351X PMC 3190695 PMID 21712391 Fine A McIntosh WB May 1975 Elevation of Serum Gamma Glutamyl Transpeptidase in End Stage Chronic Renal Failure Scottish Medical Journal 20 3 113 115 doi 10 1177 003693307502000309 ISSN 0036 9330 PMID 242073 S2CID 23177210 Endre ZH Pickering JW Walker RJ Devarajan P Edelstein CL Bonventre JV Frampton CM Bennett MR Ma Q Sabbisetti VS Vaidya VS Walcher AM Shaw GM Henderson SJ Nejat M Schollum JB George PM 2 May 2011 Improved performance of urinary biomarkers of acute kidney injury in the critically ill by stratification for injury duration and baseline renal function Kidney International 79 10 1119 1130 doi 10 1038 ki 2010 555 ISSN 0085 2538 PMC 3884688 PMID 21307838 Mannion CM 2012 General Laboratory Manual PDF Department of Pathology Hackensack University Medical Centre p 129 Retrieved 20 February 2014 Betro MG Oon RC Edwards JB November 1973 Gamma glutamyl transpeptidase in diseases of the liver and bone American Journal of Clinical Pathology 60 5 672 8 doi 10 1093 ajcp 60 5 672 PMID 4148049 a b Lum G Gambino SR April 1972 Serum gamma glutamyl transpeptidase activity as an indicator of disease of liver pancreas or bone Clinical Chemistry 18 4 358 62 doi 10 1093 clinchem 18 4 358 PMID 5012259 Lamy J Baglin MC Ferrant JP Weill J 1974 Determination de la gamma glutamyl transpeptidase senque des ethyliques a la suite du sevrage Clin Chim Acta 56 2 169 73 doi 10 1016 0009 8981 74 90225 3 PMID 4154814 a b Franzini M Bramanti E Ottaviano V Ghiri E Scatena F Barsacchi R Pompella A Donato L Emdin M Paolicchi A March 2008 A high performance gel filtration chromatography method for gamma glutamyltransferase fraction analysis Analytical Biochemistry 374 1 1 6 doi 10 1016 j ab 2007 10 025 hdl 11382 3163 PMID 18023410 Kaplan MM Matloff DS Selinger MJ Quaroni EG 1985 Biochemical basis for serum enzyme abnormalities in alcoholic liver disease In Chang NC Chao HM eds Early identification of alcohol abuse Proceedings of a workshop October 31 November 1 1983 Rockville Maryland National Institute on Alcohol Abuse and Alcoholism pp 186 198 LCCN 84601128 Research Monograph No 17 Barouki R Chobert MN Finidori J Aggerbeck M Nalpas B Hanoune J 1983 Ethanol effects in a rat hepatoma cell line induction of gamma glutamyltransferase Hepatology 3 3 323 9 doi 10 1002 hep 1840030308 PMID 6132864 S2CID 84080031 Rosalki SB Tarlow D Rau D August 1971 Plasma gamma glutamyl transpeptidase elevation in patients receiving enzyme inducing drugs Lancet 2 7720 376 7 doi 10 1016 S0140 6736 71 90093 6 PMID 4105075 Kava Uses Benefits amp Dosage Herbal Database Drugs com Emdin M Pompella A Paolicchi A October 2005 Gamma glutamyltransferase atherosclerosis and cardiovascular disease triggering oxidative stress within the plaque Circulation 112 14 2078 80 doi 10 1161 CIRCULATIONAHA 105 571919 PMID 16203922 Pompella A Emdin M Passino C Paolicchi A 2004 The significance of serum gamma glutamyltransferase in cardiovascular diseases Clinical Chemistry and Laboratory Medicine 42 10 1085 91 doi 10 1515 CCLM 2004 224 PMID 15552264 S2CID 4248204 Ruttmann E Brant LJ Concin H Diem G Rapp K Ulmer H October 2005 Gamma glutamyltransferase as a risk factor for cardiovascular disease mortality an epidemiological investigation in a cohort of 163 944 Austrian adults Circulation 112 14 2130 7 doi 10 1161 CIRCULATIONAHA 105 552547 PMID 16186419 Hanigan MH Gallagher BC Townsend DM Gabarra V April 1999 Gamma glutamyl transpeptidase accelerates tumor growth and increases the resistance of tumors to cisplatin in vivo Carcinogenesis 20 4 553 559 doi 10 1093 carcin 20 4 553 ISSN 0143 3334 PMC 6522259 PMID 10223181 External links editMedlinePlus Encyclopedia Gamma glutamyl transpeptidase GGT blood test gamma Glutamyltransferase at the U S National Library of Medicine Medical Subject Headings MeSH GGT Lab Tests Online Overview of all the structural information available in the PDB for UniProt P19440 Gamma glutamyltransferase 1 at the PDBe KB Portal nbsp Biology Retrieved from https en wikipedia org w index php title Gamma glutamyltransferase amp oldid 1216939358, wikipedia, wiki, book, books, library,

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