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    SRPX2 sushi repeat containing protein X-linked 2 [ Homo sapiens (human) ]

    Gene ID: 27286, updated on 5-Mar-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    SRPX2 promotes cancer cell proliferation and migration of papillary thyroid cancer.

    SRPX2 promotes cancer cell proliferation and migration of papillary thyroid cancer.
    Guo H, Liu R, Wu J, Li S, Yao W, Xu J, Zheng C, Lu Y, Zhang H., Free PMC Article

    12/22/2023
    Local administration of liposomal-based Srpx2 gene therapy reverses pulmonary fibrosis by blockading fibroblast-to-myofibroblast transition.

    Local administration of liposomal-based Srpx2 gene therapy reverses pulmonary fibrosis by blockading fibroblast-to-myofibroblast transition.
    Wang Q, Liu J, Hu Y, Pan T, Xu Y, Yu J, Xiong W, Zhou Q, Wang Y., Free PMC Article

    08/7/2021
    SRPX2 promotes cell proliferation and invasion via activating FAK/SRC/ERK pathway in non-small cell lung cancer.

    SRPX2 promotes cell proliferation and invasion via activating FAK/SRC/ERK pathway in non-small cell lung cancer.
    Li X, Liu J, Sun H, Zou Y, Chen J, Chen Y, Chen C, Wu X.

    02/20/2021
    Sushi Repeat Containing Protein X-linked 2 Is a Downstream Signal of LEM Domain Containing 1 and Acts as a Tumor-Promoting Factor in Oral Squamous Cell Carcinoma.

    Sushi Repeat Containing Protein X-linked 2 Is a Downstream Signal of LEM Domain Containing 1 and Acts as a Tumor-Promoting Factor in Oral Squamous Cell Carcinoma.
    Sasahira T, Kurihara-Shimomura M, Nishiguchi Y, Shimomura H, Kirita T., Free PMC Article

    02/13/2021
    This study suggests that SRPX2 promotes angiogenesis of HUVECs through the cooperation of the uPAR and integrin/FAK pathway.

    Sushi repeat-containing protein X-linked 2 promotes angiogenesis through the urokinase-type plasminogen activator receptor dependent integrin αvβ3/focal adhesion kinase pathways.
    Liu K, Fan J, Wu J.

    07/20/2019
    Knockdown of SRPX2 inhibits cell proliferation and metastasis, and promotes chemosensitivity in esophageal squamous cell carcinoma cells.

    SRPX2 knockdown inhibits cell proliferation and metastasis and promotes chemosensitivity in esophageal squamous cell carcinoma.
    He F, Wang H, Li Y, Liu W, Gao X, Chen D, Wang Q, Shi G.

    04/6/2019
    We explore the contribution of SRPX2 variants to clinical phenotype in our patients and conclude that these variants at least partially explain the phenotype. Further studies are necessary to establish and confirm the association between SRPX2 and neurodevelopment particularly speech and language development.

    Exploring the association between SRPX2 variants and neurodevelopment: How causal is it?
    Schirwani S, McConnell V, Willoughby J, DDD Study, Balasubramanian M.

    01/5/2019
    SRPX2 potentially acts as an independent prognostic predictor and a drug-target for hepatocellular carcinoma patients.

    SRPX2, an independent prognostic marker, promotes cell migration and invasion in hepatocellular carcinoma.
    Lin X, Chang W, Wang Y, Tian M, Yu Z.

    05/5/2018
    Increased Sushi repeat-containing protein X-linked 2 is associated with progression of colorectal cancer.

    Increased Sushi repeat-containing protein X-linked 2 is associated with progression of colorectal cancer.
    Liu KL, Wu J, Zhou Y, Fan JH.

    03/19/2016
    In rolandic epilepsy patients no major role was found for an association with SRPX2 or ELP4 genes.

    Analysis of ELP4, SRPX2, and interacting genes in typical and atypical rolandic epilepsy.
    Reinthaler EM, Lal D, Jurkowski W, Feucht M, Steinböck H, Gruber-Sedlmayr U, Ronen GM, Geldner J, Haberlandt E, Neophytou B, Hahn A, Altmüller J, Thiele H, Toliat MR, EuroEPINOMICS Consortium, Lerche H, Nürnberg P, Sander T, Neubauer BA, Zimprich F.

    10/4/2014
    High SRPX2 expression is associated with gastric cancer.

    Impact of overexpression of Sushi repeat-containing protein X-linked 2 gene on outcomes of gastric cancer.
    Yamada T, Oshima T, Yoshihara K, Sato T, Nozaki A, Shiozawa M, Ota M, Yoshikawa T, Akaike M, Numata K, Rino Y, Kunisaki C, Tanaka K, Imada T, Masuda M.

    06/28/2014
    SRPX2 is an epilepsy- and language-associated gene that is a target of the foxhead box protein P2 (FoxP2) transcription factor.

    The human language-associated gene SRPX2 regulates synapse formation and vocalization in mice.
    Sia GM, Clem RL, Huganir RL., Free PMC Article

    12/21/2013
    The SRPX2 protein contains the P-DUDES structural domain in its C-terminal region. This domain has significant albeit remote sequence similarity to thioredoxin-like domains, and is predicted to possess an oxidoreductase function.

    [A case of mixed tumor of the palate].
    Arlotta P, Santori L, de Vecchi A.

    05/28/2013
    Hypomethylation of SRPX2 appeared at the transition from adenoma to carcinoma, and was correlated with adenocarcinoma histology, microsatellite stability, and poor differentiation.

    Non-CpG island promoter hypomethylation and miR-149 regulate the expression of SRPX2 in colorectal cancer.
    Øster B, Linnet L, Christensen LL, Thorsen K, Ongen H, Dermitzakis ET, Sandoval J, Moran S, Esteller M, Hansen TF, Lamy P, COLOFOL steering group, Laurberg S, Ørntoft TF, Andersen CL.

    04/27/2013
    SRPX2 is a novel chondroitin sulfate proteoglycan that is overexpressed in gastrointestinal cancer cells.

    SRPX2 is a novel chondroitin sulfate proteoglycan that is overexpressed in gastrointestinal cancer.
    Tanaka K, Arao T, Tamura D, Aomatsu K, Furuta K, Matsumoto K, Kaneda H, Kudo K, Fujita Y, Kimura H, Yanagihara K, Yamada Y, Okamoto I, Nakagawa K, Nishio K., Free PMC Article

    05/12/2012
    The FOXP2-SRPX2/uPAR network provides exciting insights into molecular pathways underlying speech-related disorders.

    Molecular networks implicated in speech-related disorders: FOXP2 regulates the SRPX2/uPAR complex.
    Roll P, Vernes SC, Bruneau N, Cillario J, Ponsole-Lenfant M, Massacrier A, Rudolf G, Khalife M, Hirsch E, Fisher SE, Szepetowski P., Free PMC Article

    03/12/2011
    acts as regulator of ICAM1 and E-selectin during endotoxemia

    Characterization of SVEP1, KIAA, and SRPX2 in an in vitro cell culture model of endotoxemia.
    Schwanzer-Pfeiffer D, Rossmanith E, Schildberger A, Falkenhagen D.

    08/30/2010
    These findings suggest that Srpx2 regulates endothelial cell migration and tube formation and provides a new target for modulating angiogenesis.

    Sushi repeat protein X-linked 2, a novel mediator of angiogenesis.
    Miljkovic-Licina M, Hammel P, Garrido-Urbani S, Bradfield PF, Szepetowski P, Imhof BA.

    01/25/2010
    the biological functions of SRPX2 include cellular migration and adhesion to cancer cells.

    SRPX2 is overexpressed in gastric cancer and promotes cellular migration and adhesion.
    Tanaka K, Arao T, Maegawa M, Matsumoto K, Kaneda H, Kudo K, Fujita Y, Yokote H, Yanagihara K, Yamada Y, Okamoto I, Nakagawa K, Nishio K.

    01/21/2010
    Interaction of SRPX2 with uPAR involved in the functioning, the development and disorders of the speech cortex.

    Epileptic and developmental disorders of the speech cortex: ligand/receptor interaction of wild-type and mutant SRPX2 with the plasminogen activator receptor uPAR.
    Royer-Zemmour B, Ponsole-Lenfant M, Gara H, Roll P, Lévêque C, Massacrier A, Ferracci G, Cillario J, Robaglia-Schlupp A, Vincentelli R, Cau P, Szepetowski P.

    01/21/2010
    The R75K human-specific variation occurred in an important functional loop of the first sushi domain of SRPX2, indicating that this evolutionary mutation may have functional importance

    Molecular evolution of the human SRPX2 gene that causes brain disorders of the Rolandic and Sylvian speech areas.
    Royer B, Soares DC, Barlow PN, Bontrop RE, Roll P, Robaglia-Schlupp A, Blancher A, Levasseur A, Cau P, Pontarotti P, Szepetowski P., Free PMC Article

    01/21/2010
    The involvement of SRPX2 in these disorders suggests an important role for SRPX2 in the perisylvian region critical for language and cognitive development.

    SRPX2 mutations in disorders of language cortex and cognition.
    Roll P, Rudolf G, Pereira S, Royer B, Scheffer IE, Massacrier A, Valenti MP, Roeckel-Trevisiol N, Jamali S, Beclin C, Seegmuller C, Metz-Lutz MN, Lemainque A, Delepine M, Caloustian C, de Saint Martin A, Bruneau N, Depétris D, Mattéi MG, Flori E, Robaglia-Schlupp A, Lévy N, Neubauer BA, Ravid R, Marescaux C, Berkovic SF, Hirsch E, Lathrop M, Cau P, Szepetowski P.

    01/21/2010
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