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Gene Review

Serpinb2  -  serine (or cysteine) peptidase inhibitor,...

Mus musculus

Synonyms: PAI-2, Pai2, Planh2, Plasminogen activator inhibitor 2, macrophage, Serpin B2, ...
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Disease relevance of Serpinb2


Psychiatry related information on Serpinb2


High impact information on Serpinb2

  • Using cells that exhibit a temperature-sensitive defect in ubiquitin conjugation, we report here that non-permissive temperature inhibited class I-restricted presentation of ovalbumin introduced into the cytosol, but did not affect presentation of an ovalbumin peptide synthesized from a minigene [7].
  • We have now analysed the ability of variant H-2Kb molecules to positively select T-cells that respond to H-2Kb with ovalbumin [8].
  • Furthermore, the ability of four different H-2Kb variants to select this response in the thymus correlates with their ability to present the ovalbumin peptide, indicating that a self-peptide mimic of the foreign peptide could be involved in positive selection [8].
  • We show that progesterone-mediated induction of transcription in untransformed oviduct cells depends on an ovalbumin gene flanking sequence between positions -95 and -222 [9].
  • A 5'-flanking sequence essential for progesterone regulation of an ovalbumin fusion gene [9].

Chemical compound and disease context of Serpinb2


Biological context of Serpinb2

  • We conclude that overexpression of PAI-2 promotes the development and progression of epidermal papillomas in a manner that does not involve inhibition of its extracellular target protease, uPA, but appears to be related to an inhibition of apoptosis [1].
  • Two mouse lines were established, one of which strongly expressed the transgene and produced elevated levels of PAI-2 in the epidermis [1].
  • In addition, a major up-regulation in PAI-1 mRNA levels was observed throughout the kidney, while PAI-2 mRNA was not detectable in the kidneys of control or LPS-injected animals [14].
  • Moreover, 20 days postcessation of the 5-day 25 ppm NO2 inhalation regimen, eosinophilic and neutrophilic inflammation, pulmonary lesions, and AHR were still present in mice immunized and challenged with OVA [15].
  • Secondly, transfection of a PAI-2 cDNA led to the synthesis of both forms of PAI-2 [16].

Anatomical context of Serpinb2

  • A mouse PAI-2-encoding transgene was targeted to basal epidermis and hair follicles under the control of the bovine keratin type 5 gene promoter [1].
  • The present study was designed to determine if TMA elicited eosinophil infiltration into lungs of sensitized mice similar to previous studies with the protein allergen ovalbumin (OA) [3].
  • Two forms of plasminogen activators inhibitor 2 (PAI-2) are synthesized by human and murine monocytes/macrophages: one accumulates in the cytosol, while the other is translocated into the endoplasmic reticulum, glycosylated and secreted [16].
  • Finally, in vitro translation of an mRNA transcript of the PAI-2 cDNA in the presence of microsomal membranes generated two topologically distinct forms of PAI-2 [16].
  • Transfected clones expressed PAI-2 at levels two to nine times higher than both the parental cell line and mock transfectants, as detected by ELISA of cell lysates and conditioned medium [4].

Associations of Serpinb2 with chemical compounds

  • In contrast, in mice immunized and challenged with OVA, inhalation of 25 ppm NO2 caused a marked augmentation of eosinophilic inflammation and terminal bronchiolar lesions, which extended significantly into the alveoli [15].
  • Adjuvant effects of protopanaxadiol and protopanaxatriol saponins from ginseng roots on the immune responses to ovalbumin in mice [17].
  • Plasminogen mRNA induction in the mouse brain after kainate excitation: codistribution with plasminogen activator inhibitor-2 (PAI-2) mRNA [18].
  • The insulin-mediated induction (3- to 4-fold) of PAI-1 and PAI-2 message was suppressed on exposure to PIs, which was reversed by troglitazone treatment [19].
  • Interestingly, this distribution pattern coincided with what we have recently described for the plasminogen activator inhibitor-2 (PAI-2) mRNA, however differing from that of the plasminogen activator inhibitor-1 (PAI-1) mRNA, as also shown here [18].

Physical interactions of Serpinb2

  • The clone with the highest PAI-2 expression exhibited complete inhibition of soluble and cell-surface-bound plasminogen activator activity [4].

Regulatory relationships of Serpinb2

  • In contrast, both OA-induced infiltration of eosinophils and increase of eotaxin content were abrogated in BALF from PAR2(-/-) mice [20].
  • Our results indicate that during differentiation of epidermal keratinocyte, PAI-2 expresses mainly in the more differentiated keratinocytes and may protect the terminal differentiated keratinocytes from prematuration through inhibiting involucrin expression in cornified envelope [21].

Other interactions of Serpinb2

  • PAI-2 but not PAI-1 mRNA was detected in fetal and neonatal epidermis, localized in the spinous layers [22].
  • After 48 h, both uPAR and PAI-2 mRNAs were expressed in the epidermal layers from the suprabasal keratinocytes up to the differentiating cells beneath the cornified layer and in hair follicle keratinocytes [23].
  • Neutrophils were markedly increased in the bronchoalveolar lavage fluid of CCSP(-/-) Ova mice, coinciding with increased myeloperoxidase activity and macrophage inflammatory protein-2 levels [24].
  • PAI-1 production, deposition of collagen and fibrin, and MMP-9 activity in the lung tissue or airways were greater after OVA challenge compared with saline challenge [25].
  • Twenty parts per million of NO(2) induced a significant increase of bronchopulmonary hyperreactivity in OVA-challenged mice and of permeability according to the fibronectin content of the bronchoalveolar lavage fluid (BALF) 24 h after exposure, as compared with air or 5 ppm NO(2) [26].

Analytical, diagnostic and therapeutic context of Serpinb2


  1. Overexpression of plasminogen activator inhibitor type 2 in basal keratinocytes enhances papilloma formation in transgenic mice. Zhou, H.M., Bolon, I., Nichols, A., Wohlwend, A., Vassalli, J.D. Cancer Res. (2001) [Pubmed]
  2. Fibronectin-binding protein I of Streptococcus pyogenes is a promising adjuvant for antigens delivered by mucosal route. Medina, E., Talay, S.R., Chhatwal, G.S., Guzmán, C.A. Eur. J. Immunol. (1998) [Pubmed]
  3. Trimellitic anhydride-induced eosinophilia in a mouse model of occupational asthma. Regal, J.F., Mohrman, M.E., Sailstad, D.M. Toxicol. Appl. Pharmacol. (2001) [Pubmed]
  4. Overexpression of plasminogen activator inhibitor 2 in human melanoma cells inhibits spontaneous metastasis in scid/scid mice. Mueller, B.M., Yu, Y.B., Laug, W.E. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  5. Sequential development of airway hyperresponsiveness and acute airway obstruction in a mouse model of allergic inflammation. Neuhaus-Steinmetz, U., Glaab, T., Daser, A., Braun, A., Lommatzsch, M., Herz, U., Kips, J., Alarie, Y., Renz, H. Int. Arch. Allergy Immunol. (2000) [Pubmed]
  6. Assessment of allergenic activity of a heat-coagulated ovalbumin after in vivo digestion. Joo, K., Kato, Y. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
  7. A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation. Michalek, M.T., Grant, E.P., Gramm, C., Goldberg, A.L., Rock, K.L. Nature (1993) [Pubmed]
  8. Role of self-peptides in positively selecting the T-cell repertoire. Nikolić-Zugić, J., Bevan, M.J. Nature (1990) [Pubmed]
  9. A 5'-flanking sequence essential for progesterone regulation of an ovalbumin fusion gene. Dean, D.C., Knoll, B.J., Riser, M.E., O'Malley, B.W. Nature (1983) [Pubmed]
  10. Infection of mice with Mycobacterium bovis-Bacillus Calmette-Guérin (BCG) suppresses allergen-induced airway eosinophilia. Erb, K.J., Holloway, J.W., Sobeck, A., Moll, H., Le Gros, G. J. Exp. Med. (1998) [Pubmed]
  11. Treatment of allergic airway inflammation and hyperresponsiveness by antisense-induced local blockade of GATA-3 expression. Finotto, S., De Sanctis, G.T., Lehr, H.A., Herz, U., Buerke, M., Schipp, M., Bartsch, B., Atreya, R., Schmitt, E., Galle, P.R., Renz, H., Neurath, M.F. J. Exp. Med. (2001) [Pubmed]
  12. TRACP Influences Th1 pathways by affecting dendritic cell function. Esfandiari, E., Bailey, M., Stokes, C.R., Cox, T.M., Evans, M.J., Hayman, A.R. J. Bone Miner. Res. (2006) [Pubmed]
  13. Reversal of Allergen-induced Airway Remodeling by CysLT1 Receptor Blockade. Henderson, W.R., Chiang, G.K., Tien, Y.T., Chi, E.Y. Am. J. Respir. Crit. Care Med. (2006) [Pubmed]
  14. LPS induces major changes in the extracellular proteolytic balance in the murine kidney. Moll, S., Schifferli, J.A., Huarte, J., Lemoine, R., Vassalli, J.D., Sappino, A.P. Kidney Int. (1994) [Pubmed]
  15. Nitrogen dioxide enhances allergic airway inflammation and hyperresponsiveness in the mouse. Poynter, M.E., Persinger, R.L., Irvin, C.G., Butnor, K.J., van Hirtum, H., Blay, W., Heintz, N.H., Robbins, J., Hemenway, D., Taatjes, D.J., Janssen-Heininger, Y. Am. J. Physiol. Lung Cell Mol. Physiol. (2006) [Pubmed]
  16. Facultative polypeptide translocation allows a single mRNA to encode the secreted and cytosolic forms of plasminogen activators inhibitor 2. Belin, D., Wohlwend, A., Schleuning, W.D., Kruithof, E.K., Vassalli, J.D. EMBO J. (1989) [Pubmed]
  17. Adjuvant effects of protopanaxadiol and protopanaxatriol saponins from ginseng roots on the immune responses to ovalbumin in mice. Sun, J., Hu, S., Song, X. Vaccine (2007) [Pubmed]
  18. Plasminogen mRNA induction in the mouse brain after kainate excitation: codistribution with plasminogen activator inhibitor-2 (PAI-2) mRNA. Sharon, R., Abramovitz, R., Miskin, R. Brain Res. Mol. Brain Res. (2002) [Pubmed]
  19. Synergistic antiadipogenic effects of HIV type 1 protease inhibitors with tumor necrosis factor alpha: suppression of extracellular insulin action mediated by extracellular matrix-degrading proteases. Mondal, D., Larussa, V.F., Agrawal, K.C. AIDS Res. Hum. Retroviruses (2001) [Pubmed]
  20. Abrogation of bronchial eosinophilic inflammation and attenuated eotaxin content in protease-activated receptor 2-deficient mice. Takizawa, T., Tamiya, M., Hara, T., Matsumoto, J., Saito, N., Kanke, T., Kawagoe, J., Hattori, Y. J. Pharmacol. Sci. (2005) [Pubmed]
  21. Plasminogen activator inhibitor 2: expression and role in differentiation of epidermal keratinocyte. Lian, X., Yang, T. Biol. Cell (2004) [Pubmed]
  22. Modulation of the plasminogen activator cascade during enhanced epidermal proliferation in vivo. Jensen, P.J., Lavker, R.M. Cell Growth Differ. (1996) [Pubmed]
  23. Differential expression of urokinase-type plasminogen activator, its receptor, and inhibitors in mouse skin after exposure to a tumor-promoting phorbol ester. Lund, L.R., Eriksen, J., Ralfkiaer, E., Rømer, J. J. Invest. Dermatol. (1996) [Pubmed]
  24. CCSP modulates airway dysfunction and host responses in an Ova-challenged mouse model. Wang, S.Z., Rosenberger, C.L., Espindola, T.M., Barrett, E.G., Tesfaigzi, Y., Bice, D.E., Harrod, K.S. Am. J. Physiol. Lung Cell Mol. Physiol. (2001) [Pubmed]
  25. PAI-1 promotes extracellular matrix deposition in the airways of a murine asthma model. Oh, C.K., Ariue, B., Alban, R.F., Shaw, B., Cho, S.H. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  26. Interference of a short-term exposure to nitrogen dioxide with allergic airways responses to allergenic challenges in BALB/c mice. Proust, B., Lacroix, G., Robidel, F., Marliere, M., Lecomte, A., Vargaftig, B.B. Mediators of inflammation. (2002) [Pubmed]
  27. Expression of plasminogen activator inhibitor 2 in the adult and embryonic mouse tissues. Kawata, Y., Mimuro, J., Kaneko, M., Shimada, K., Sakata, Y. Thromb. Haemost. (1996) [Pubmed]
  28. Regulation of IgE responses to inhaled antigen in mice by antigen-specific gamma delta T cells. McMenamin, C., Pimm, C., McKersey, M., Holt, P.G. Science (1994) [Pubmed]
  29. Antigen presentation in extracellular matrix: interactions of T cells with dendritic cells are dynamic, short lived, and sequential. Gunzer, M., Schäfer, A., Borgmann, S., Grabbe, S., Zänker, K.S., Bröcker, E.B., Kämpgen, E., Friedl, P. Immunity (2000) [Pubmed]
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