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    HTRA4 HtrA serine peptidase 4 [ Homo sapiens (human) ]

    Gene ID: 203100, updated on 4-Jan-2025

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Identification of HTRA4 as a Transcriptional Target of p63 in Trophoblast.

    Identification of HTRA4 as a Transcriptional Target of p63 in Trophoblast.
    Donohoe ME, Morey R, Li Y, Pizzo D, Kallol S, Cho HY, Soncin F, Parast MM.,

    07/1/2024
    HtrA4 is required for human trophoblast stem cell differentiation into syncytiotrophoblast.

    HtrA4 is required for human trophoblast stem cell differentiation into syncytiotrophoblast.
    Thach B, Wang Y, Heng S, Nie G.

    02/28/2024
    Deficiency of HtrA4 in BeWo cells downregulates angiogenesis through IL-6/JAK/STAT3 signaling.

    Deficiency of HtrA4 in BeWo cells downregulates angiogenesis through IL-6/JAK/STAT3 signaling.
    Pei CZ, Seok J, Kim GJ, Choi BC, Baek KH.

    10/4/2023
    Cellular Functions of High-Temperature Requirement Factor A4 in Placenta.

    Cellular Functions of High-Temperature Requirement Factor A4 in Placenta.
    Pei CZ, Choi BC, Park JH, Park HY, Paek J, Lee KJ, Yun BS, Kim YJ, Baek KH., Free PMC Article

    06/14/2023
    HtrA4 is up-regulated during trophoblast syncytialization and BeWo cells fail to syncytialize without HtrA4.

    HtrA4 is up-regulated during trophoblast syncytialization and BeWo cells fail to syncytialize without HtrA4.
    Mansilla M, Wang Y, Lim R, Palmer K, Nie G., Free PMC Article

    12/11/2021
    Elevated circulating HtrA4 in preeclampsia may alter endothelial expression of senescence genes.

    Elevated circulating HtrA4 in preeclampsia may alter endothelial expression of senescence genes.
    Wang Y, Lim R, Nie G.

    02/6/2021
    HtrA4 may play a major role in inhibiting endothelial repair in pregnancy complication preeclampsia.

    HtrA4 may play a major role in inhibiting endothelial repair in pregnancy complication preeclampsia.
    Wang Y, Lim R, Nie G., Free PMC Article

    09/19/2020
    New insight into the mechanism of the HtrA4 protease function in cell death and oncogenesis; they may help to develop new anti-cancer therapeutic strategies.

    HtrA4 Protease Promotes Chemotherapeutic-Dependent Cancer Cell Death.
    Wenta T, Rychlowski M, Jarzab M, Lipinska B., Free PMC Article

    06/20/2020
    concentrations found in preeclampsia cleaved VE-cadherin in HUVECs as an endothelial model, disrupted cell-cell connections and induced intercellular gaps

    Elevated protease HtrA4 in the maternal circulation of preeclampsia may contribute to endothelial barrier disruption by cleaving key junctional protein VE-cadherin.
    Tseng E, Yee Teoh SS, Wang Y, Nie G.

    03/14/2020
    Discerning the mechanism of action of HtrA4: a serine protease implicated in the cell death pathway.

    Discerning the mechanism of action of HtrA4: a serine protease implicated in the cell death pathway.
    Kummari R, Dutta S, Chaganti LK, Bose K.

    02/15/2020
    The HtrA1-PDZ and HtrA4-PDZ as well as HtrA2-PDZ and HtrA3-PDZ respond similarly to different halogen substitutions of peptide; -Br substitution at R2-position and -I substitution at R4-position are most effective in improving peptide selectivity for HtrA1-PDZ/HtrA4-PDZ and HtrA2-PDZ/HtrA3-PDZ, respectively; -F substitution would not address substantial effect on peptide selectivity for all the 4 domains

    Peptide selectivity between the PDZ domains of human pregnancy-related serine proteases (HtrA1, HtrA2, HtrA3, and HtrA4) can be reshaped by different halogen probes.
    Sun ML, Sun LM, Wang YQ.

    10/5/2019
    the aberrant expression of HTRA1 or HTRA4 may be involved in the onset of preeclampsia, and increased HTRA1 or HTRA4 expression may affect trophoblast functions.

    Elevated HTRA1 and HTRA4 in severe preeclampsia and their roles in trophoblast functions.
    Liu C, Xing F, He Y, Zong S, Luo C, Li C, Duan T, Wang K, Zhou Q.

    11/10/2018
    GATA3 knockdown elevated HtrA4 expression in BeWo and JEG-3 trophoblast cell lines and enhanced the invasion activities of both lines. This study uncovered a new GATA3 function in placenta as a negative regulator of GCM1 activity and trophoblastic invasion.

    GATA3 inhibits GCM1 activity and trophoblast cell invasion.
    Chiu YH, Chen H., Free PMC Article

    12/31/2016
    HtrA4 represents a novel placenta-specific serine protease that is altered specifically in early-onset preeclampsia with potential causal roles in endothelial dysfunction and disease development.

    Human HtrA4 Expression Is Restricted to the Placenta, Is Significantly Up-Regulated in Early-Onset Preeclampsia, and High Levels of HtrA4 Cause Endothelial Dysfunction.
    Singh H, Zhao M, Chen Q, Wang Y, Li Y, Kaitu'u-Lino TJ, Tong S, Nie G.

    10/17/2015
    Conditioned media from these two cell lines after decidualization treatment suppress HtrA4-expressing JAR cell invasion in an HtrA1- or HtrA3-dependent manner.

    Functional antagonism between high temperature requirement protein A (HtrA) family members regulates trophoblast invasion.
    Chen YY, Chuang PY, Chen CP, Chiu YH, Lo HF, Cheong ML, Huang JY, Kuo PL, Chen H., Free PMC Article

    12/20/2014
    Data suggest that increased HtrA4 (and HtrA1) in placenta tissues may be involved in onset of pre-eclampsia; elevated level of HtrA4 (but not HtrA1) in sera has potential as biomarker for pre-eclampsia.

    Upregulation of HtrA4 in the placentas of patients with severe pre-eclampsia.
    Inagaki A, Nishizawa H, Ota S, Suzuki M, Inuzuka H, Miyamura H, Sekiya T, Kurahashi H, Udagawa Y.

    03/23/2013
    study reveals a novel function of GCM1 and HtrA4 in regulation of trophoblast invasion and that abnormal HrtA4 expression may contribute to shallow trophoblast invasion in preeclampsia

    High-temperature requirement protein A4 (HtrA4) suppresses the fusogenic activity of syncytin-1 and promotes trophoblast invasion.
    Wang LJ, Cheong ML, Lee YS, Lee MT, Chen H., Free PMC Article

    11/24/2012
    FLJ90724 or HTRA4 is a member of the HtrA family of proteases

    The HtrA family of proteases: implications for protein composition and cell fate.
    Clausen T, Southan C, Ehrmann M.

    12/28/2004
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