Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2024 Feb 26:11:1334931.
doi: 10.3389/fmolb.2024.1334931. eCollection 2024.

Serpin peptidase inhibitor, clade E, member 2 in physiology and pathology: recent advancements

Shutong Wu #  1   2 , Yuchao Yang #  1   3 , Meiling Zhang  4 , Asmat Ullah Khan  1 , Jingxing Dai  1 , Jun Ouyang  1
Affiliations
Review

Serpin peptidase inhibitor, clade E, member 2 in physiology and pathology: recent advancements

Shutong Wu et al. Front Mol Biosci. .

Abstract

Serine protease inhibitors (serpins) are the most numerous and widespread multifunctional protease inhibitor superfamily and are expressed by all eukaryotes. Serpin E2 (serpin peptidase inhibitor, clade E, member 2), a member of the serine protease inhibitor superfamily is a potent endogenous thrombin inhibitor, mainly found in the extracellular matrix and platelets, and expressed in numerous organs and secreted by many cell types. The multiple functions of serpin E2 are mainly mediated through regulating urokinase-type plasminogen activator (uPA, also known as PLAU), tissue-type plasminogen activator (tPA, also known as PLAT), and matrix metalloproteinase activity, and include hemostasis, cell adhesion, and promotion of tumor metastasis. The importance serpin E2 is clear from its involvement in numerous physiological and pathological processes. In this review, we summarize the structural characteristics of the Serpin E2 gene and protein, as well as its roles physiology and disease.

Keywords: conformational diseases; hemostasis; osteoarthritis; pathology; physiological processes; reproductive; serpin E2; tumor metastasis.

PubMed Disclaimer

Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

FIGURE 1
FIGURE 1
Effects of Serpin E2 on murine sperm capacitation.
FIGURE 2
FIGURE 2
Serpin E2 improves OA by inhibiting MMP13 activity.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

References

    1. AbdelHafez F. F., Klausen C., Zhu H., Yi Y., Leung P. C. K. (2023). Growth differentiation factor myostatin regulates epithelial-mesenchymal transition genes and enhances invasion by increasing serine protease inhibitors E1 and E2 in human trophoblast cells. FASEB J. 37, e23204. 10.1096/fj.202300740R - DOI - PubMed
    1. Aguzzi A. (2006). Prion diseases of humans and farm animals: epidemiology, genetics, and pathogenesis. J. Neurochem. 97, 1726–1739. 10.1111/j.1471-4159.2006.03909.x - DOI - PubMed
    1. Apte R. S., Chen D. S., Ferrara N. (2019). VEGF in signaling and disease: beyond discovery and development. Cell 176, 1248–1264. 10.1016/j.cell.2019.01.021 - DOI - PMC - PubMed
    1. Aymonnier K., Kawecki C., Arocas V., Boulaftali Y., Bouton M. C. (2021). Serpins, new therapeutic targets for hemophilia. Thromb. Haemost. 121, 261–269. 10.1055/s-0040-1716751 - DOI - PubMed
    1. Aymonnier K., Kawecki C., Venisse L., Boulaftali Y., Christophe O. D., Lenting P. J., et al. (2019). Targeting protease nexin-1, a natural anticoagulant serpin, to control bleeding and improve hemostasis in hemophilia. Blood 134, 1632–1644. 10.1182/blood.2019000281 - DOI - PMC - PubMed