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Your search keyword '"NIH 3T3 Cells"' showing total 2 results
Start Over Descriptor "NIH 3T3 Cells" Language dutch; flemish
2 results on '"NIH 3T3 Cells"'

1. Current concepts in RET-related genetics, signaling and therapeutics

Author

Bart J. L. Eggen, Robert M.W. Hofstra, Grzegorz M. Burzynski, Ivan Plaza-Menacho, Jan Willem B. de Groot, Faculty of Science and Engineering, Faculteit Medische Wetenschappen/UMCG, Groningen Biomolecular Sciences and Biotechnology, Celbiochemie, Molecular Neuroscience and Ageing Research, and Restoring organ function by means of regenerative medicine

Subjects
endocrine system, congenital, hereditary, and neonatal diseases and abnormalities, endocrine system diseases, MEDULLARY-THYROID CARCINOMA, Multiple endocrine neoplasia type 2, Multiple Endocrine Neoplasia Type 2a, RECEPTOR TYROSINE KINASE, Biology, medicine.disease_cause, Germline, Receptor tyrosine kinase, CELL-PROLIFERATION, Cancer syndrome, Mice, ENTERIC NERVOUS-SYSTEM, AUTOPHOSPHORYLATION SITES, Genetics, medicine, Animals, Humans, Hirschsprung Disease, Multiple endocrine neoplasia, neoplasms, GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries), TRANSGENIC MICE, Mutation, Polymorphism, Genetic, Proto-Oncogene Proteins c-ret, medicine.disease, SPORADIC HIRSCHSPRUNG-DISEASE, Enzyme Activation, Haplotypes, SEQUENCE VARIANT, MULTIPLE ENDOCRINE NEOPLASIA, biology.protein, ComputingMethodologies_DOCUMENTANDTEXTPROCESSING, NIH 3T3 Cells, Signal transduction, Signal Transduction, NEUROTROPHIC FACTOR
Abstract

The receptor tyrosine kinase RET is expressed in cell lineages derived from the neural crest and has a key role in regulating cell proliferation, migration, differentiation and survival during embryogenesis. Germline and somatic mutations in RET that produce constitutively activated receptors cause the cancer syndrome multiple endocrine neoplasia type 2 and several endocrine and neural-crest-derived tumors, whereas mutations resulting in nonfunctional RET or lower expression of RET are found in individuals affected with Hirschsprung disease. This review focuses on the genetics and molecular mechanisms underlying the different inherited human neural-crest-related disorders in which RET dysfunction has a crucial role and discusses RET as a potential therapeutic target.

Published
2006

2. Alternative splicing of the actin binding domain of human cortactin affects cell migration

Author

Ying-xin Fan, Wouter H. Moolenaar, Ellen Schuuring-Scholtes, Jos H. de Graaf, Agnes G S H van Rossum, Ed Schuuring, Philip M. Kluin, Xi Zhan, and Rijksuniversiteit Groningen

Subjects
Arp2/3 complex, Biochemistry, ARP2/3 COMPLEX, chemistry.chemical_compound, Mice, Cell Movement, Protein Isoforms, Phosphorylation, Cytoskeleton, Glutathione Transferase, CYCLIN D1, TYROSINE PHOSPHORYLATION, biology, Reverse Transcriptase Polymerase Chain Reaction, HUMAN CARCINOMAS, Microfilament Proteins, Cell migration, Exons, Cell biology, COS Cells, Cortactin, PROTEIN CORTACTIN, Binding domain, Protein Binding, Genetic Vectors, Immunoblotting, macromolecular substances, Transfection, FILAMENT NETWORK FORMATION, Filamentous actin, Animals, Humans, BREAST-CANCER, Molecular Biology, EMS1 GENE, Dose-Response Relationship, Drug, Alternative splicing, Tyrosine phosphorylation, CHROMOSOME 11Q13 REGION, Cell Biology, Molecular biology, Actins, Protein Structure, Tertiary, CONTACT SITES, Alternative Splicing, chemistry, Microscopy, Fluorescence, biology.protein, NIH 3T3 Cells, Tyrosine
Abstract

Cortactin is a filamentous actin (F-actin)-binding protein that regulates cytoskeletal dynamics by activating the Arp2/3 complex; it binds to F-actin by means of six N-terminal "cortactin repeats". Gene amplification of 11q13 and consequent overexpression of cortactin in several human cancers is associated with lymph node metastasis. Overexpression as well as tyrosine phosphorylation of cortactin has been reported to enhance cell migration, invasion, and metastasis. Here we report the identification of two alternative splice variants (SV1 and SV2) that affect the cortactin repeats: SV1-cortactin lacks the 6th repeat (exon 11), whereas SV2-cortactin lacks the 5th and 6th repeats (exons 10 and 11). SV-1 cortactin is found co-expressed with wild type (wt)-cortactin in all tissues and cell lines examined, whereas the SV2 isoform is much less abundant. SV1-cortactin binds F-actin and promotes Arp2/3-mediated actin polymerization equally well as wt-cortactin, whereas SV2-cortactin shows reduced F-actin binding and polymerization. Alternative splicing of cortactin does not affect its subcellular localization or growth factor-induced tyrosine phosphorylation. However, cells that overexpress SV1- or SV2-cortactin show significantly reduced cell migration when compared with wt-cortactin-overexpressing cells. Thus, in addition to overexpression and tyrosine phosphorylation, alternative splicing of the F-actin binding domain of cortactin is a new mechanism by which cortactin influences cell migration.

Published
2003

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