Linked Life Data

6549320

Source:http://linkedlifedata.com/resource/pubmed/id/6549320

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1985-4-9
pubmed:abstractText
The major glycoproteins synthesized by human breast epithelial cells have been characterized [6,8]. The most consistently observed and prominent component in supernatants of organ cultures of breast surgical specimens and of MCF-7 cells was gp 68 which has been immunologically identified as alpha-1-antichymotrypsin (Achy). In the present study we demonstrate that this glycoprotein can form an irreversible complex with chymotrypsin, which indicates that it is a functional inhibitor. The 14C-glucosamine-labeled gp 68 forms a stable, 88,000-dalton, enzyme-inhibitor complex with chymotrypsin. The molecule is secreted continuously for 9 days into a chemically defined, serum-free medium. In addition to the de novo synthesized inhibitor, another component is absorbed from fetal bovine serum and subsequently released into serum-free medium. This component also forms an irreversible, 88,000-dalton complex with enzyme. The observations establish that two types of inhibitors are associated with human breast epithelial cells, one actively synthesized and the other derived from serum. Both of these molecules may have significant roles in stabilizing cell surface components and in protecting extracellular matrices from untimely degradation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0730-2312
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-67
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Active proteinase inhibitors associated with human breast epithelial cells.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't