Linked Life Data

8228989

Source:http://linkedlifedata.com/resource/pubmed/id/8228989

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1993-11-29
pubmed:abstractText
Certain halogenated hydrocarbons, e.g., dichloroacetylene, are nephrotoxic to experimental animals and neurotoxic to humans; cysteine-S-conjugate beta-lyases may play a role in the nephrotoxicity. We now show that with dichlorovinylcysteine as substrate the only detectable cysteine-S-conjugate beta-lyase in rat brain homogenates is identical to glutamine transaminase K. The predominant (mitochondrial) form of glutamine transaminase K in rat brain was shown to be immunologically distinct from the predominant (cytosolic) form of the enzyme in rat kidney. Glutamine transaminase K and omega-amidase (constituents of the glutaminase II pathway) activities were shown to be widespread throughout the rat brain. However, the highest specific activities of these enzymes were found in the choroid plexus. The high activity of glutamine transaminase K in choroid plexus was also demonstrated by means of an immunohistochemical staining procedure. Glutamine transaminase K has a broad specificity toward amino acid and alpha-keto acid substrates. The omega-amidase also has a broad specificity; presumably, however, the natural substrates are alpha-ketoglutaramate and alpha-ketosuccinamate, the alpha-keto acid analogues of glutamine and asparagine, respectively. The high activities of both glutamine transaminase K and omega-amidase in the choroid plexus suggest that the two enzymes are linked metabolically and perhaps are coordinately expressed in that organ. The data suggest that the natural substrate of glutamine transaminase K in rat brain is indeed glutamine and that the metabolism of glutamine through the glutaminase II pathway (i.e., L-glutamine and alpha-keto acid-->alpha-ketoglutarate and L-amino acid + ammonia) is an important function of the choroid plexus. Moreover, the present findings also suggest that any explanation of the neurotoxicity of halogenated xenobiotics must take into account the role of glutamine transminase K and its presence in the choroid plexus.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1731-41
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
High activities of glutamine transaminase K (dichlorovinylcysteine beta-lyase) and omega-amidase in the choroid plexus of rat brain.
pubmed:affiliation
Department of Biochemistry, Cornell University Medical College, New York, NY 10021.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.