ABSTRACT
Recently identified chondroitin sulphate proteoglycans in perineuronal nets include neurocan and phosphacan. However, the function and assembly of these components has yet to be resolved. In this study we show morphological alteration in Wisteria floribunda labelled nets around cortical interneurones both in tenascin-R knockout and tenascin-R/parvalbumin double knockout mice. This alteration reflects the loss of phosphacan and neurocan from cortical nets in mice deficient in tenascin-R. No effect on the membrane related cytoskeleton, as revealed by ankyrin(R), was observed in any of the mice. These results on mice lacking tenascin-R substantiate previously reported in vitro interactions between tenascin-R and phosphacan and neurocan.
Subject(s)
Cerebral Cortex/metabolism , Extracellular Matrix/metabolism , Neurons/metabolism , Parvalbumins/genetics , Parvalbumins/metabolism , Tenascin/genetics , Tenascin/metabolism , Animals , Cell Size/physiology , Cerebral Cortex/cytology , Chondroitin Sulfate Proteoglycans/metabolism , Extracellular Matrix/ultrastructure , Fluorescent Antibody Technique , Lectins, C-Type , Mice , Mice, Knockout , Nerve Tissue Proteins/metabolism , Neurocan , Neurons/cytology , Receptor-Like Protein Tyrosine Phosphatases, Class 5ABSTRACT
A special feature of the extracellular matrix in adult brains of various species is the concentration of certain components around different sub-populations of neurones, giving rise to net-like structures termed perineuronal nets. Recently, some of these components have been identified but the function of these nets has yet to be resolved. Using immunofluorescence microscopy, we report here that phosphacan, a chondroitin sulphate proteoglycan, is an additional component of Wisteria floribunda labelled perineuronal nets surrounding parvalbumin-expressing neurones in rat cerebral cortex. Glycoproteins such as tenascin-C and -R have been identified in perineuronal nets and the present detection of phosphacan immunoreactivity in the same entity is of potential physiological importance because of their previously described interactions.
Subject(s)
Cerebral Cortex/metabolism , Chondroitin Sulfate Proteoglycans/metabolism , Nerve Net/metabolism , Neurons/metabolism , Parvalbumins/metabolism , Plant Lectins , Animals , Cerebral Cortex/cytology , Female , Fluorescent Antibody Technique , Lectins , Male , Rats , Rats, Wistar , Receptor-Like Protein Tyrosine Phosphatases, Class 5 , Receptors, N-AcetylglucosamineABSTRACT
Human 2-D PAGE Databases established at the Danish Centre for Human Genome Research are now available on the World Wide Web (http://biobase.dk/cgi-bin/celis). The databanks, which offer a comprehensive approach to the analysis of the human proteome both in health and disease, contain data on known and unknown proteins recorded in various IEF and NEPHGE 2-D PAGE reference maps (non-cultured keratinocytes, non-cultured transitional cell carcinomas, MRC-5 fibroblasts and urine). One can display names and information on specific protein spots by clicking on the image of the gel representing the 2-D gel map in which one is interested. In addition, the database can be searched by protein name, keywords or organelle or cellular component. The entry files contain links to other databases such as Medline, Swiss-Prot, PIR, PDB, CySPID, OMIM, Methabolic pathways, etc. The on-line information is updated regularly.
