The cell line data base and the new catalogue: Detailed information on 2650 human and animal cell lines

Manniello, A.; Aresu, Ottavia; Parodi, Brunella; Romano, Paolo; Iannotta, B.; Rondanina, Gabriella; Viegi, L.; Ruzzon, Tiziana

doi:10.1007/bf00746077

Cited by 4 publications

(1 citation statement)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To investigate the role of adherens junctions in the localization of NPRAP-ABP complexes, we used MDCK cells, which express high levels of E-cadherin, and which at confluence form a uniform monolayer with prominent adherens junctions (Manniello et al, 1993;Lu et al, 1999). We asked whether the E-cadherin-NPRAP complex can form at these junctions and if so, whether it can associate with ABP.…”

Section: Nprap Draws Abp and Glur2 To Adherens Junctionsmentioning

confidence: 99%

Synaptic Anchorage of AMPA Receptors by Cadherins through Neural Plakophilin-Related Arm Protein–AMPA Receptor-Binding Protein Complexes

Silverman¹,

Restituito²,

Lü³

et al. 2007

J. Neurosci.

113

View full text Add to dashboard Cite

Cadherins function in the adhesion of presynaptic and postsynaptic membranes at excitatory synapses. Here we show that the cadherinassociated protein neural plakophilin-related arm protein (NPRAP; also called ␦-catenin) binds via a postsynaptic density-95 (PSD-95)/ discs large/zona occludens-1 (PDZ) interaction to AMPA receptor (AMPAR)-binding protein (ABP) and the related glutamate receptor (GluR)-interacting protein (GRIP), two multi-PDZ proteins that bind the GluR2 and GluR3 AMPAR subunits. The resulting cadherin-NPRAP-ABP/GRIP complexes serve as anchorages for AMPARs. Exogenous NPRAP that was bound to cadherins at adherens junctions of Madin-Darby canine kidney cells recruited ABP from the cytosol to form cadherin-NPRAP-ABP complexes, dependent on NPRAP interaction with the ABP PDZ domain 2. The cadherin-NPRAP-ABP complexes also bound GluR2. In cultured hippocampal neurons, dominant-negative mutants of NPRAP designed to disrupt tethering of ABP to NPRAP-cadherin complexes reduced surface levels of endogenous GluR2, indicating that interaction with cadherin-NPRAP-ABP complexes stabilized GluR2 at the neuronal plasma membrane. Cadherins, NPRAP, GRIP, and GluR2 copurified in the fractionation of synaptosomes and the postsynaptic density, two fractions enriched in synaptic proteins. Furthermore, synaptosomes contain NPRAP-GRIP complexes, and NPRAP localizes with the postsynaptic marker PSD-95 and with AMPARs and GRIP at spines of hippocampal neurons. Thus, tethering is likely to take place at synaptic or perisynaptic sites. NPRAP also binds PSD-95, which is a scaffold for NMDA receptors, for AMPARs in complexes with auxiliary subunits, the TARPs (transmembrane AMPA receptor regulator proteins), and for adhesion molecules. Thus, the interaction of scaffolding proteins with cadherin-NPRAP complexes may anchor diverse signaling and adhesion molecules at cadherins.

show abstract

Section: Nprap Draws Abp and Glur2 To Adherens Junctionsmentioning

confidence: 99%

Synaptic Anchorage of AMPA Receptors by Cadherins through Neural Plakophilin-Related Arm Protein–AMPA Receptor-Binding Protein Complexes

Silverman¹,

Restituito²,

Lü³

et al. 2007

J. Neurosci.

113

View full text Add to dashboard Cite

show abstract

The New Catalogue of the Cell Line Data Base

Manniello¹,

Romano²,

Parodi³

et al. 1995

Animal Cell Technology: Developments Towards the 21st Century

View full text Add to dashboard Cite

Antibody variable-region sequencing as a method for hybridoma cell-line authentication

Koren

Kosmač

Venturini

et al. 2008

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Cross-contamination and misidentification of various cell lines is a widespread problem that can lead to spurious scientific conclusions. DNA fingerprinting is a powerful identification technique, which can be effectively used for the authentication of human cell lines. In contrast to human cancer cell lines, little attention has so far been given to establishing authentication practices for hybridoma cell lines. Since the majority of hybridomas stem from inbred animals, they have high genetic uniformity, which reduces the applicability of DNA fingerprinting. In the present study, we propose antibody variable-region sequencing as a method of choice for hybridoma cell-line authentication. This method focuses on the most diverse characteristic of hybridoma cell lines and thereby achieves a very high discriminatory power. The sequencing of light-chain variable regions has proven to be especially suitable for routine use because of its high success rate. Two other possible authentication methods, random amplified polymorphic DNA analysis and two-dimensional gel electrophoresis, were also examined. Compared to these and other methods that can be used for discrimination between hybridoma cell lines, variable-region sequencing has many advantages, most notably those of a very high discriminatory power, insensitivity to changes in experimental conditions, simple data analysis, and accessibility to most laboratories.

show abstract

The cell line data base and the new catalogue: Detailed information on 2650 human and animal cell lines

Cited by 4 publications

References 1 publication

Synaptic Anchorage of AMPA Receptors by Cadherins through Neural Plakophilin-Related Arm Protein–AMPA Receptor-Binding Protein Complexes

Synaptic Anchorage of AMPA Receptors by Cadherins through Neural Plakophilin-Related Arm Protein–AMPA Receptor-Binding Protein Complexes

The New Catalogue of the Cell Line Data Base

Antibody variable-region sequencing as a method for hybridoma cell-line authentication

Contact Info

Product

Resources

About