Linked Life Data

2505443

Source:http://linkedlifedata.com/resource/pubmed/id/2505443

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1989-10-6
pubmed:abstractText
Parathyroid hormone (PTH) and chromogranin A/secretory protein-I (SP-I) have been localized on immunoelectron microscopy in double-fixed tissues from adenomatous and secondary hyperplastic parathyroid glands. Storage organelles, identified on the basis of their consistent labelling, included tow morphologically distinct varieties of granules/vesicles; the mature granules and the progranules. The former consisted of dense, mostly rounded, medium to large-sized bodies which were strongly labelled and predominant in the proximity of the cell membrane. The other variety of body included a spectrum of small pale vesicles/granules which were mainly located in the Golgi area. Because their morphology and their labelling pattern varied other bodies were assumed to be engaged in degradation or cleavage of the secretory proteins. These bodies comprised crinophagic structures, that is to say multivesicular bodies and large Golgi-related vesicles, as well as a number of atypical solid bodies. Whereas most of the granulated cells stored a mature or a maturing population of vesicles/granules, the process of maturation appeared to be either absent or incomplete in a number of cells from some glands. The major defects were frequently associated with an unusual labelling pattern of the Golgi area and selectively affected groups of cells from all the transitional oxyphil cell adenomas. The minor defects concerned individual cells of different types present in both categories of glands. The present data suggest that in hyperfunctioning glands, the type of hormone processing depends on the capacity of each cell in progranule maturation and that the maturation capacity may decrease dramatically in adenomatous or chronically hyperstimulated cells of the transitional oxyphil type.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0174-7398
pubmed:author
pubmed:issnType
Print
pubmed:volume
415
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
305-16
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Storage and degradation of secretory proteins in adenomatous and secondary hyperplastic parathyroid cells. An immunoelectron microscope study.
pubmed:affiliation
Laboratoire d'Anatomie Pathologique, Hôpital Edouard Herriot, Lyon, France.
pubmed:publicationType
Journal Article