PRSS8 (protease, serine, 8)

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Delineation of proteolytic and non-proteolytic functions of membrane-anchored serine protease Prss8/prostasin

The membrane-anchored serine proteases prostasin and matriptase initiate a cell surface proteolytic pathway essential for epithelial function. Mice expressing only catalytically-inactive prostasin, unlike prostasin null mice, are viable, indicating that at least some of prostasin’s functions are non-proteolytic. Here we used knockin mice expressing catalytically-inactive prostasin (Prss8) to sh...

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The serine protease prostasin (PRSS8) is a potential biomarker for early detection of ovarian cancer

BACKGROUND Ovarian cancer (OVC) is the deadliest of all gynecologic cancers, primarily as a consequence of asymptomatic progression. The complex nature of OVC creates challenges for early detection, and there is a lack of specific and sensitive biomarkers suitable for screening and detecting early stage OVC. METHODS Potential OVC biomarkers were identified by bioinformatic analysis. Candidate...

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The epidermal barrier function is dependent on the serine protease CAP1/Prss8

Serine proteases are proteolytic enzymes that are involved in the regulation of various physiological processes. We generated mice lacking the membrane-anchored channel-activating serine protease (CAP) 1 (also termed protease serine S1 family member 8 [Prss8] and prostasin) in skin, and these mice died within 60 h after birth. They presented a lower body weight and exhibited severe malformation...

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PAR2 absence completely rescues inflammation and ichthyosis caused by altered CAP1/Prss8 expression in mouse skin

Altered serine protease activity is associated with skin disorders in humans and in mice. The serine protease channel-activating protease-1 (CAP1; also termed protease serine S1 family member 8 (Prss8)) is important for epidermal homeostasis and is thus indispensable for postnatal survival in mice, but its roles and effectors in skin pathology are poorly defined. In this paper, we report that t...

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Serine protease mechanism and specificity.

Almost one-third of all proteases can be classified as serine proteases, named for the nucleophilic Ser residue at the active site. This mechanistic class was originally distinguished by the presence of the AspHis-Ser “charge relay” system or “catalytic triad”.1 The Asp-His-Ser triad can be found in at least four different structural contexts, indicating that this catalytic machinery has evolve...

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ژورنال

عنوان ژورنال: Atlas of Genetics and Cytogenetics in Oncology and Haematology

سال: 2012

ISSN: 1768-3262

DOI: 10.4267/2042/47537