Plasminogen activator inhibitor 2 (PAI-2) is not inactivated by exposure to oxidants which can be released from activated neutrophils

Baker, Mark S.; Green, Simon P.; Goss, Neil H.; Katrantzis, Michael; Doe, William F.

doi:10.1016/0006-291x(90)90909-7

Cited by 18 publications

(10 citation statements)

References 25 publications

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“…The mass of the peptide which was identified as P3 by N-terminal sequencing was between 15 and 16 mass units greater than the predicted mass. One possible explanation for this observation is the previously documented (28,29) oxidation of methionine by chloramine-T. The EMS and N-terminal sequencing results are summarized in Table Ia. The loss of tyrosine fluorescence due to iodination can clearly be seen when the tryptic map of non-iodinated bIGFBP-2 ( Fig.…”

Section: Resultsmentioning

confidence: 75%

The Insulin-like Growth Factor (IGF) Binding Site of Bovine Insulin-like Growth Factor Binding Protein-2 (bIGFBP-2) Probed by Iodination

Hobba

Forbes

Parkinson

et al. 1996

Journal of Biological Chemistry

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Section: Resultsmentioning

confidence: 75%

The Insulin-like Growth Factor (IGF) Binding Site of Bovine Insulin-like Growth Factor Binding Protein-2 (bIGFBP-2) Probed by Iodination

Hobba

Forbes

Parkinson

et al. 1996

Journal of Biological Chemistry

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“…62 Thus by analogy to normal intrauterine placental growth, the role of PAI-2 in gingiva is thought to be to protection from excessive proteolysis and tissue destruction. 44 Given that PAI-2 expression is highly upregulated by proinflammatory mediators (Table 2) and is resistant to oxidation due to the absence of a reactive site methionine (as found in PAI-1), 63 it would seem reasonable to suggest that PAI-2 may be the primary PA inhibitor at sites of inflammation.…”

Section: Extracellular Roles Of Plasminogen Activator Inhibitor 2: Inmentioning

confidence: 99%

Forty Years Later and the Role of Plasminogen Activator Inhibitor Type 2/SERPINB2 Is Still an Enigma

Lee

Cochran

Lobov

et al. 2011

Semin Thromb Hemost

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Plasminogen activator inhibitor (PAI)-2 expression is acutely upregulated in pregnancy, inflammation, infection, and other pathophysiological conditions. Circumstances that prevent PAI-2 upregulation are associated with chronic pathology. Altogether this strongly suggests that PAI-2 is one of the many proteins that maintain homeostasis during damage or stress. However, several functions ranging from a classical serpin to various intracellular roles have been ascribed to PAI-2 and, because none of these have been definitively proven in vivo, to this day its precise role or roles remains an enigma. This review readdresses the evidence supporting a role for PAI-2 in fibrinolysis and proteolysis within extracellular environments and includes a review of the many potential intracellular functions attributed to PAI-2.

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“…An increased PAI-1/PAI-2 ratio and placental oxidative stress have been reported as good predictors of preeclampsia (Wikstrom et al, 2009). Given the known susceptibility of protease inhibitors including PAI-1 (Baker et al, 1990) and α 2 M (Deby- Dupont et al, 1994) to inactivation by reactive oxygen species, it is plausible that PAI-2, which is resistant to inactivation by oxidants (Baker et al, 1990), is an important regulator of fibrinolytic activity under these conditions (Fig. 2).…”

Section: Disease Implicationsmentioning

confidence: 99%

PZP and PAI-2: Structurally-diverse, functionally similar pregnancy proteins?

Wyatt

Cater

Ranson

2016

The International Journal of Biochemistry & Cell Biology

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Pregnancy zone protein (PZP) and plasminogen activator inhibitor type 2 (PAI-2) are two multifunctional proteins that are elevated in normal pregnancy and numerous other inflammatory states. Both proteins were originally identified as protease inhibitors, but current evidence supports the notion that they may also function as modulators of T-helper cells and/or extracellular chaperones. Exacerbated inflammation, fibrinolytic disturbances and misfolded proteins are all implicated in the pathology of preeclampsia, a leading cause of maternal and foetal mortality and morbidity. Notably, reduced levels of PZP or PAI-2 are associated with preeclampsia and clarification of their diverse functions in normal pregnancy could provide much needed insight regarding the pathogenesis of this disorder. Given that inflammation and protein misfolding underlie the pathology of a very large number of disorders, the contributions of PZP and PAI-2 to extracellular proteostasis and immunoregulation could be broad-reaching. Given that inflammation and protein misfolding underlie the pathology of a very large number of disorders, the contributions of PZP and PAI-2 to extracellular proteostasis and immunoregulation could be broad-reaching.

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Plasminogen activator inhibitor 2 (PAI-2) is not inactivated by exposure to oxidants which can be released from activated neutrophils

Cited by 18 publications

References 25 publications

The Insulin-like Growth Factor (IGF) Binding Site of Bovine Insulin-like Growth Factor Binding Protein-2 (bIGFBP-2) Probed by Iodination

The Insulin-like Growth Factor (IGF) Binding Site of Bovine Insulin-like Growth Factor Binding Protein-2 (bIGFBP-2) Probed by Iodination

Forty Years Later and the Role of Plasminogen Activator Inhibitor Type 2/SERPINB2 Is Still an Enigma

PZP and PAI-2: Structurally-diverse, functionally similar pregnancy proteins?

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