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ADAM10 is expressed in human podocytes and found in urinary vesicles of patients with glomerular kidney diseases.

Gutwein P, Schramme A, Abdel-Bakky MS, Doberstein K, Hauser IA, Ludwig A, Altevogt P, Gauer S, Hillmann A, Weide T, Jespersen C, Eberhardt W, Pfeilschifter J.

J Biomed Sci. 2010 Jan 13;17:3. doi: 10.1186/1423-0127-17-3.


CXCL16 is expressed in podocytes and acts as a scavenger receptor for oxidized low-density lipoprotein.

Gutwein P, Abdel-Bakky MS, Schramme A, Doberstein K, Kämpfer-Kolb N, Amann K, Hauser IA, Obermüller N, Bartel C, Abdel-Aziz AA, El Sayed el SM, Pfeilschifter J.

Am J Pathol. 2009 Jun;174(6):2061-72. doi: 10.2353/ajpath.2009.080960. Epub 2009 May 12.


The transcription factor PAX2 regulates ADAM10 expression in renal cell carcinoma.

Doberstein K, Pfeilschifter J, Gutwein P.

Carcinogenesis. 2011 Nov;32(11):1713-23. doi: 10.1093/carcin/bgr195. Epub 2011 Aug 30.


Anticancer chemotherapy inhibits MHC class I-related chain a ectodomain shedding by downregulating ADAM10 expression in hepatocellular carcinoma.

Kohga K, Takehara T, Tatsumi T, Miyagi T, Ishida H, Ohkawa K, Kanto T, Hiramatsu N, Hayashi N.

Cancer Res. 2009 Oct 15;69(20):8050-7. doi: 10.1158/0008-5472.CAN-09-0789. Epub 2009 Oct 13.


Increase of disintergin metalloprotease 10 (ADAM10) expression in oral squamous cell carcinoma.

Ko SY, Lin SC, Wong YK, Liu CJ, Chang KW, Liu TY.

Cancer Lett. 2007 Jan 8;245(1-2):33-43. Epub 2005 Nov 23.


Expression of A disintegrin and metalloprotease 10 in pancreatic carcinoma.

Gaida MM, Haag N, Günther F, Tschaharganeh DF, Schirmacher P, Friess H, Giese NA, Schmidt J, Wente MN.

Int J Mol Med. 2010 Aug;26(2):281-8.


A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10.

Parkin E, Harris B.

J Neurochem. 2009 Mar;108(6):1464-79. doi: 10.1111/j.1471-4159.2009.05907.x. Epub 2009 Jan 22.


Adam10 is essential for early embryonic cardiovascular development.

Zhang C, Tian L, Chi C, Wu X, Yang X, Han M, Xu T, Zhuang Y, Deng K.

Dev Dyn. 2010 Oct;239(10):2594-602. doi: 10.1002/dvdy.22391.


ADAM10 promotes pituitary adenoma cell migration by regulating cleavage of CD44 and L1.

Pan Y, Han C, Wang C, Hu G, Luo C, Gan X, Zhang F, Lu Y, Ding X.

J Mol Endocrinol. 2012 Jun 26;49(1):21-33. doi: 10.1530/JME-11-0174. Print 2012 Aug.


L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth.

Maretzky T, Schulte M, Ludwig A, Rose-John S, Blobel C, Hartmann D, Altevogt P, Saftig P, Reiss K.

Mol Cell Biol. 2005 Oct;25(20):9040-53.


Constitutive activation of metalloproteinase ADAM10 in mantle cell lymphoma promotes cell growth and activates the TNFα/NFκB pathway.

Armanious H, Gelebart P, Anand M, Belch A, Lai R.

Blood. 2011 Jun 9;117(23):6237-46. doi: 10.1182/blood-2010-10-313940. Epub 2011 Mar 25.


ADAM17 upregulation in human renal disease: a role in modulating TGF-alpha availability?

Melenhorst WB, Visser L, Timmer A, van den Heuvel MC, Stegeman CA, van Goor H.

Am J Physiol Renal Physiol. 2009 Sep;297(3):F781-90. doi: 10.1152/ajprenal.90610.2008. Epub 2009 Jun 17.


Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.

Escrevente C, Morais VA, Keller S, Soares CM, Altevogt P, Costa J.

Biochim Biophys Acta. 2008 Jun;1780(6):905-13. doi: 10.1016/j.bbagen.2008.03.004. Epub 2008 Mar 13.


Tumoural CXCL16 expression is a novel prognostic marker of longer survival times in renal cell cancer patients.

Gutwein P, Schramme A, Sinke N, Abdel-Bakky MS, Voss B, Obermüller N, Doberstein K, Koziolek M, Fritzsche F, Johannsen M, Jung K, Schaider H, Altevogt P, Ludwig A, Pfeilschifter J, Kristiansen G.

Eur J Cancer. 2009 Feb;45(3):478-89. doi: 10.1016/j.ejca.2008.10.023. Epub 2008 Dec 11.


Altered expression of ADAMs (A Disintegrin And Metalloproteinase) in fibrillating human atria.

Arndt M, Lendeckel U, Röcken C, Nepple K, Wolke C, Spiess A, Huth C, Ansorge S, Klein HU, Goette A.

Circulation. 2002 Feb 12;105(6):720-5.


Tetraspanin15 regulates cellular trafficking and activity of the ectodomain sheddase ADAM10.

Prox J, Willenbrock M, Weber S, Lehmann T, Schmidt-Arras D, Schwanbeck R, Saftig P, Schwake M.

Cell Mol Life Sci. 2012 Sep;69(17):2919-32. doi: 10.1007/s00018-012-0960-2. Epub 2012 Mar 25.


Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans.

Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E, Blobel CP, Himanen JP, Lackmann M, Nikolov DB.

Cell. 2005 Oct 21;123(2):291-304.


Effects of neuron-specific ADAM10 modulation in an in vivo model of acute excitotoxic stress.

Clement AB, Hanstein R, Schröder A, Nagel H, Endres K, Fahrenholz F, Behl C.

Neuroscience. 2008 Mar 18;152(2):459-68. doi: 10.1016/j.neuroscience.2007.10.060. Epub 2008 Jan 12.


The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition.

Rapti M, Atkinson SJ, Lee MH, Trim A, Moss M, Murphy G.

Biochem J. 2008 Apr 15;411(2):433-9. doi: 10.1042/BJ20071430.


Differential gene expression in ADAM10 and mutant ADAM10 transgenic mice.

Prinzen C, Trümbach D, Wurst W, Endres K, Postina R, Fahrenholz F.

BMC Genomics. 2009 Feb 5;10:66. doi: 10.1186/1471-2164-10-66.

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