Expression of Plasminogen Activator Inhibitor 2 in the Adult and Embryonic Mouse Tissues

Kawata, Yoichi; Mimuro, Jun; Kaneko, Munekiyo; Shimada, Kazuyuki; Sakata, Yoichi

doi:10.1055/s-0038-1650624

Cited by 11 publications

(9 citation statements)

References 33 publications

(42 reference statements)

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“…One such proteinase inhibitor, which we have previously suggested may be involved in the regulation of keratinocyte differentiation, is plasminogen activator inhibitor type 2 (PAI-2; Lyons-Giordano et al 1994;Jensen et al 1995;Wang and Jensen 1998). A recent survey of mouse organs revealed that the highest level of this inhibitor is in epidermal keratinocytes (Kawata et al 1996), consistent with the observations that PAI-2 mRNA, antigen, and activity are readily detectable in human epidermis in vivo (Hibino et al 1988;Lyons-Giordano et al 1994).…”

Section: Introductionsupporting

confidence: 62%

Differentiating cells of murine stratified squamous epithelia constitutively express plasminogen activator inhibitor type 2 (PAI-2)

Risse¹,

Brown²,

Lavker³

et al. 1998

Histochemistry and Cell Biology

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In stratified squamous epithelia a critical balance among cell proliferation, differentiation, and death must be maintained in order for these tissues to fulfill their barrier function. Previous studies have demonstrated that plasminogen activator inhibitor 2 (PAI-2) is a product of differentiating epidermal keratinocytes, suggesting a role for this inhibitor during squamous differentiation. Furthermore, in certain tumor cell lines, overexpression of PAI-2 confers resistance to the induction of programmed cell death, suggesting cytoprotective function(s). In the present study we demonstrate that PAI-2 mRNA and protein are constitutively and uniquely expressed in differentiating cells of murine stratified squamous epithelia, including epidermis, esophagus, vagina, oral mucosa, and tongue. PAI-2 immunohistochemical localization patterns suggest a predominantly cytosolic distribution, consistent with biochemical identification of the major PAI-2 species as a 43-kDa, presumably non-glycosylated protein. Functional analysis shows that the majority of epithelial PAI-2 is active. In contrast to the high levels of PAI-2 expression in stratified squamous epithelia, little or no PAI-2 is detectable in simple epithelia. These findings suggest that epithelial PAI-2 may mediate inhibition of intracellular proteinases associated with events during terminal differentiation and death that are unique to stratified squamous epithelia.

show abstract

Section: Introductionsupporting

confidence: 62%

Differentiating cells of murine stratified squamous epithelia constitutively express plasminogen activator inhibitor type 2 (PAI-2)

Risse¹,

Brown²,

Lavker³

et al. 1998

Histochemistry and Cell Biology

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“…However, we cannot exclude the possibility that PAI-2 plays an important role in human placental function. Though present in human trophoblasts, PAI-2 mRNA is not detected in the murine placenta at significant levels until very late in gestation (17-18 days postcoitum) (36).…”

Section: Discussionmentioning

confidence: 94%

The plasminogen activator inhibitor-2 gene is not required for normal murine development or survival

Dougherty

Pearson

Yang

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

111

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Plasminogen activator inhibitor-2 (PAI-2), a member of the serpin gene family, is thought to serve as a primary regulator of plasminogen activation in the extravascular compartment. High levels of PAI-2 are found in keratinocytes, monocytes, and the human trophoblast, the latter suggesting a role in placental maintenance or embryo development. The primarily intracellular distribution of PAI-2 also may indicate a unique regulatory role in a protease-dependent cellular process such as apoptosis. To examine the potential functions of PAI-2 in vivo, we generated PAI-2-deficient mice by gene targeting in embryonic stem cells. Homozygous PAI-2-deficient mice exhibited normal development, survival, and fertility and were also indistinguishable from normal controls in response to a bacterial infectious challenge or endotoxin infusion. No differences in monocyte recruitment into the peritoneum were observed after thioglycollate injection. Epidermal wound healing was equivalent among PAI-2 ؊͞؊ null and control mice. Finally, crossing PAI-2 ؊͞؊ with PAI-1 ؊͞؊ mice to generate animals deficient in both plasminogen activator inhibitors failed to uncover an overlap in function between these two related proteins.

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“…It is possible that CHD4 becomes less important for regulating plasmin activation on LECs after birth as the plasminogen activator inhibitor (PAI) proteins PAI-1 and PAI-2 become more widely expressed and functional. The insignificance of embryonic PAI activity is demonstrated by the lack of developmental defects in PAI-deficient embryos and by the limited expression of PAI-2 at E15.5 (33)(34)(35). Genetic studies will provide the best opportunity for deciphering the relative impact of CHD4 and the PAIs on LV thrombus protection after birth.…”

Section: Discussionmentioning

confidence: 99%

CHD4-regulated plasmin activation impacts lymphovenous hemostasis and hepatic vascular integrity

Crosswhite¹,

Podsiadlowska²,

Curtis³

et al. 2016

Journal of Clinical Investigation

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Expression of Plasminogen Activator Inhibitor 2 in the Adult and Embryonic Mouse Tissues

Cited by 11 publications

References 33 publications

Differentiating cells of murine stratified squamous epithelia constitutively express plasminogen activator inhibitor type 2 (PAI-2)

Differentiating cells of murine stratified squamous epithelia constitutively express plasminogen activator inhibitor type 2 (PAI-2)

The plasminogen activator inhibitor-2 gene is not required for normal murine development or survival

CHD4-regulated plasmin activation impacts lymphovenous hemostasis and hepatic vascular integrity

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