Linked Life Data

2414959

Source:http://linkedlifedata.com/resource/pubmed/id/2414959

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1985-12-18
pubmed:abstractText
ALP and gamma-GT are 2 brush border enzymes that can be individually demonstrated on adjacent sections by the histochemical methods of Mayahara (ALP) and Rutenberg (gamma-GT). On the basis of each enzyme activity, it was possible to recognize different categories of tubules in the mouse nephron. In fact, both enzymes were heterogeneously distributed along the proximal tubule, but in opposite gradients. The various staining intensities probably corresponded to proximal segmentation, but were sometimes difficult to evaluate. A technique was perfected to localize both enzymes in the same tissue section. Since each enzyme produced a distinct type of colored precipitates (ALP: black, gamma-GT: red), 4 categories of tubules could be identified, according to staining characteristics: 1. black tubules where ALP activity was predominant, corresponded to S1 segments, 2. black and red tubules where the 2 activities were about equivalent, were considered as parts of S2, 3. red ones where gamma-GT activity was high, were identified as portions of S3, 4. negative tubules where no activity was apparent, represented distal and straight collecting tubules. In addition to economize time and tissue, this simple technique permits to easily estimate variations in enzyme activities that probably correspond to structural and functional differences in the segments of the proximal tubule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-1281
pubmed:author
pubmed:issnType
Print
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Identification of proximal tubule segments in the mouse nephron by simultaneous visualization of alkaline phosphatase and gamma-glutamyl transpeptidase.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't