Literature DB >> 21533456

Transient transformation of mammalian cells by MN protein, a tumor-associated cell adhesion molecule with carbonic anhydrase activity.

J Zavada1, Z Zavadova, O Machon, L Kutinova, R Opavsky, J Pastorek.   

Abstract

The MN protein is associated with certain human carcinomas, but absent in most normal tissues. It is a transmembrane protein; its extracellular part contains a domain homologous with carbonic anhydrases (CAs) and a proteoglycan-like region. In the present study, we observed that cells (human CGL1 and mouse NIH3T3 cells) transfected with MN cDNA showed morphologic transformation, but reverted to normal phenotype after 4-5 weeks. This reversion was not due to the loss, silencing, or mutations of MN insert. We also found that MN protein exerted CA enzymatic activity, but this was not relevant for morphologic transformation of cells. MN is an adhesion protein, involved in cell-to-cell contacts, this probably could explain its role in tumorigenesis.

Entities:  

Year:  1997        PMID: 21533456     DOI: 10.3892/ijo.10.4.857

Source DB:  PubMed          Journal:  Int J Oncol        ISSN: 1019-6439            Impact factor:   5.650


  2 in total

1.  Carbonic anhydrase isozymes IX and XII in gastric tumors.

Authors:  Mari Leppilampi; Juha Saarnio; Tuomo J Karttunen; Jyrki Kivelä; Silvia Pastoreková; Jaromir Pastorek; Abdul Waheed; William S Sly; Seppo Parkkila
Journal:  World J Gastroenterol       Date:  2003-07       Impact factor: 5.742

2.  Feasibility and constraints of particle targeting using the antigen-antibody interaction.

Authors:  Viola Tokárová; Anna Pittermannová; Vlastimil Král; Pavlína Řezáčová; František Štěpánek
Journal:  Nanoscale       Date:  2013-10-29       Impact factor: 7.790

  2 in total

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