Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-3-24
pubmed:abstractText
Human epidermal keratinocytes synthesize a complex plasminogen activator proteolytic cascade, consisting of two plasminogen activating enzymes and two inhibitors, that is thought to play a role in epidermal migration and differentiation as well as in several cutaneous diseases. Quantification of the plasminogen activator cascade proteins in keratinocytes reveals that plasminogen activator inhibitor type 2 (PAI-2) is distinct from the other components (i.e., urokinase and tissue-type plasminogen activators and inhibitor type 1) in several respects: (i) PAI-2 remains mostly cell-associated, rather than secreted; (ii) The level of cell-associated PAI-2 is at least 50-fold greater than that of the other components; (iii) PAI-2 is the only component whose level is enhanced upon elevation of the Ca2+ concentration, which is well known to induce a more differentiated phenotype in keratinocyte culture. Immunocytochemical localization experiments reveal that most keratinocytes contain PAI-2, which in a subpopulation of more differentiated cells is resistant to detergent extraction. Additional immunocytochemical localization and immunoblot experiments demonstrate that some of the PAI-2 becomes incorporated into the cornified envelope during terminal differentiation of the keratinocyte. These studies raise the possibility that PAI-2 may have an intracellular role associated with the terminal stage of keratinocyte differentiation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:volume
217
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
65-71
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Plasminogen activator inhibitor type 2: an intracellular keratinocyte differentiation product that is incorporated into the cornified envelope.
pubmed:affiliation
Department of Dermatology, University of Pennsylvania, Philadelphia 19104-6142.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.