The disintegrin domain of ADAM9: a ligand for multiple beta1 renal integrins

The Biochemical Journal
Rajeev M MahimkarDavid H Lovett

Abstract

Renal tubular epithelial cells in all nephron segments express a distinct member of the metalloprotease-disintegrin family, ADAM9 (a disintegrin and metalloprotease 9), in a punctate basolateral distribution co-localized to the beta1 integrin chain [Mahimkar, Baricos, Visaya, Pollock and Lovett (2000) J. Am. Soc. Nephrol. 11, 595-603]. Discrete segments of the nephron express several defined beta1 integrins, suggesting that ADAM9 interacts with multiple renal integrins and thereby regulates epithelial cell-matrix interactions. Intact ADAM9 and a series of deletion constructs sequentially lacking the metalloprotease domain and the disintegrin domain were assembled as chimaeras with a C-terminal GFP (green fluorescent protein) tag. Stable expression of the ADAM9/GFP protein on the surface of HEK-293 cells (human embryonic kidney 293 cells) significantly decreased adhesion to types I and IV collagen, vitronectin and laminin, but had little effect on adhesion to fibronectin. Expression of the disintegrin/cysteine-rich/GFP construct yielded a similar, but more marked pattern of decreased adhesion. Expression of the cysteine-rich/GFP construct had no effect on adhesion, indicating that the disintegrin domain was responsible for the c...Continue Reading

References

Mar 1, 1992·Clinical & Experimental Metastasis·K R GehlsenP Sriramarao
Mar 1, 1996·The Journal of Biological Chemistry·J KrätzschmarC P Blobel
Jan 5, 1999·Science·H QiS Artavanis-Tsakonas
May 18, 1999·The American Journal of Pathology·K IbaU M Wewer
Feb 1, 2000·Trends in Genetics : TIG·P Primakoff, D G Myles
Apr 7, 2000·Journal of the American Society of Nephrology : JASN·Rajeev M MahimkarDavid H Lovett
Aug 5, 2000·American Journal of Physiology. Renal Physiology·J A Kreidberg, J M Symons
Feb 13, 2001·Biochemical and Biophysical Research Communications·M ZhouP I Croucher
Nov 29, 2001·The Journal of Biological Chemistry·Lance C BridgesRon D Bowditch
Dec 6, 2001·The International Journal of Biochemistry & Cell Biology·Roy A Black
Jan 10, 2002·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Farrah Kheradmand, Zena Werb
Feb 2, 2002·The Journal of Biological Chemistry·Susan Wohler SunnarborgDavid C Lee

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Citations

Jun 28, 2008·BMC Cancer·Florian R FritzscheGlen Kristiansen
Feb 10, 2012·Spermatogenesis·Ricardo D MorenoRaúl Lagos-Cabré
Jul 11, 2006·Progress in Neurobiology·Peng YangTheo Hagg
Mar 15, 2015·Journal of Leukocyte Biology·Rafael S AmendolaChristina Barja-Fidalgo
Sep 29, 2017·Cancers·Marion LavergnePierre H Mangin
Apr 20, 2006·Birth Defects Research. Part C, Embryo Today : Reviews·Thomas TousseynDieter Hartmann
Dec 7, 2014·American Journal of Physiology. Lung Cellular and Molecular Physiology·Daniela DreymuellerAndreas Ludwig
Jul 27, 2014·The Journal of Immunology : Official Journal of the American Association of Immunologists·Robin RoychaudhuriCaroline A Owen
Mar 15, 2014·Molecular Medicine Reports·Xiaohong LvDonghua Qian
Sep 3, 2020·Cell Adhesion & Migration·M A Haoyuan, L I Yanshu
Oct 25, 2020·International Journal of Molecular Sciences·Cheng-Wei ChouYuh-Pyng Sher
Apr 22, 2021·Nature Reviews. Nephrology·Justyna WozniakAndreas Ludwig
Apr 30, 2021·Proceedings of the National Academy of Sciences of the United States of America·Masataka UmedaGeorge C Tsokos

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