Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1987-11-25
pubmed:abstractText
The distribution of transglutaminases, the Ca2+-dependent protein cross-linking enzymes, in the human pituitary gland was investigated by immunohistological methods using specific antibodies. Tissue-type transglutaminase was specifically localized in ACTH-producing cells, and the cells producing GH, PRL, TSH, FSH, and LH contained no appreciable amount of the enzyme. No detectable plasma-type transglutaminase (coagulation factor XIII) was found in pituitary tissue. In a previous study we demonstrated that ACTH-producing cells contain very little Ca2+-dependent proteinases (calpain), but a remarkable amount of their inhibitor, calpastatin. Pituitary gland cells producing hormones other than ACTH contained calpains, but no detectable calpastatin. These results collectively suggest that intracellular substrate proteins in ACTH-producing cells are protected from Ca2+-dependent degradation and are substrates for Ca2+-dependent cross-linking catalyzed by the tissue-type transglutaminase. In other pituitary gland cells, conversely, the intracellular substrate proteins are more likely to undergo Ca2+-dependent degradation than cross-linking.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-972X
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
885-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Specific localization of tissue-type transglutaminase in adrenocorticotropin-producing cells of the human pituitary gland as demonstrated by immunohistochemistry.
pubmed:affiliation
Department of Clinical Science, Kyoto University Faculty of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't