Literature DB >> 11854009

Cutting to the chase: calpain proteases in cell motility.

Angela Glading1, Douglas A Lauffenburger, Alan Wells.   

Abstract

Calpains are a large family of intracellular proteases whose precise and limited cleavage of specific proteins might be an integral regulatory aspect of signaling pathways. This intriguing mechanism for transducing biochemical and biophysical information from the external milieu seems to operate during cell motility. The two first described and ubiquitous isoforms, mu-calpain and M-calpain, have been implicated in enabling cell spreading by modifying adhesion sites and in promoting locomotion of adherent cells by facilitating rear-end detachment. Recent elucidation of the molecular structure of calpain opens the door for understanding how these pluripotential signal proteins are regulated to help govern migration. Armed with this knowledge, the precise roles of calpains in inflammation, wound repair and tumor progression can be ascertained and offer novel therapeutic targets.

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Year:  2002        PMID: 11854009     DOI: 10.1016/s0962-8924(01)02179-1

Source DB:  PubMed          Journal:  Trends Cell Biol        ISSN: 0962-8924            Impact factor:   20.808


  123 in total

Review 1.  Syntrophins entangled in cytoskeletal meshwork: Helping to hold it all together.

Authors:  Sahar S Bhat; Roshia Ali; Firdous A Khanday
Journal:  Cell Prolif       Date:  2018-12-04       Impact factor: 6.831

2.  Induction of protective immunity against Schistosoma mansoni via DNA priming and boosting with the large subunit of calpain (Sm-p80): adjuvant effects of granulocyte-macrophage colony-stimulating factor and interleukin-4.

Authors:  Afzal A Siddiqui; Troy Phillips; Hugues Charest; Ron B Podesta; Martha L Quinlin; Justin R Pinkston; Jenny D Lloyd; Michelle Paz; Rachael M Villalovos; Janet Pompa
Journal:  Infect Immun       Date:  2003-07       Impact factor: 3.441

3.  MEKK1 regulates calpain-dependent proteolysis of focal adhesion proteins for rear-end detachment of migrating fibroblasts.

Authors:  Bruce D Cuevas; Amy N Abell; James A Witowsky; Toshiaki Yujiri; Nancy Lassignal Johnson; Kamala Kesavan; Marti Ware; Peter L Jones; Scott A Weed; Roberta L DeBiasi; Yoshitomo Oka; Kenneth L Tyler; Gary L Johnson
Journal:  EMBO J       Date:  2003-07-01       Impact factor: 11.598

Review 4.  Guiding neuronal growth cones using Ca2+ signals.

Authors:  John Henley; Mu-ming Poo
Journal:  Trends Cell Biol       Date:  2004-06       Impact factor: 20.808

5.  EGF-like factors induce expansion of the cumulus cell-oocyte complexes by activating calpain-mediated cell movement.

Authors:  Ikko Kawashima; Zhilin Liu; Lisa K Mullany; Toshihiro Mihara; JoAnne S Richards; Masayuki Shimada
Journal:  Endocrinology       Date:  2012-06-06       Impact factor: 4.736

6.  ZF21 protein regulates cell adhesion and motility.

Authors:  Makoto Nagano; Daisuke Hoshino; Takeharu Sakamoto; Noritaka Kawasaki; Naohiko Koshikawa; Motoharu Seiki
Journal:  J Biol Chem       Date:  2010-05-03       Impact factor: 5.157

7.  m-Calpain activation is regulated by its membrane localization and by its binding to phosphatidylinositol 4,5-bisphosphate.

Authors:  Ludovic Leloup; Hanshuang Shao; Yong Ho Bae; Bridget Deasy; Donna Stolz; Partha Roy; Alan Wells
Journal:  J Biol Chem       Date:  2010-08-20       Impact factor: 5.157

8.  Increased calpain correlates with Th1 cytokine profile in PBMCs from MS patients.

Authors:  Sarah A Imam; Mary K Guyton; Azizul Haque; Arthur Vandenbark; William R Tyor; Swapan K Ray; Naren L Banik
Journal:  J Neuroimmunol       Date:  2007-09-04       Impact factor: 3.478

9.  Wnt5A activates the calpain-mediated cleavage of filamin A.

Authors:  Michael P O'Connell; Jennifer L Fiori; Katherine M Baugher; Fred E Indig; Amanda D French; Tura C Camilli; Brittany P Frank; Rachel Earley; Keith S Hoek; Joanne H Hasskamp; E George Elias; Dennis D Taub; Michel Bernier; Ashani T Weeraratna
Journal:  J Invest Dermatol       Date:  2009-01-29       Impact factor: 8.551

10.  Hematopoietic PBX-interacting protein (HPIP) is over expressed in breast infiltrative ductal carcinoma and regulates cell adhesion and migration through modulation of focal adhesion dynamics.

Authors:  S Bugide; D David; A Nair; N Kannan; V S K Samanthapudi; J Prabhakar; B Manavathi
Journal:  Oncogene       Date:  2014-12-08       Impact factor: 9.867

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