Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1998-2-17
pubmed:abstractText
Polysialyltransferase (PST) is an enzyme that catalyzes the addition of polysialic acid (PSA), a homopolymer of alpha-2,8-linked sialic acid residues, onto neural cell adhesion molecule (NCAM). The expression of PSA-NCAM in the brain is developmentally regulated and is of critical importance; however, the temporal and spatial developmental expression of brain PST, a potential key player in the control of PSA-NCAM levels, remains unclear. In the present study, we have cloned the coding region of rat PST cDNA by reverse transcription-polymerase chain reaction, using primers based on the hamster PST-1 cDNA sequence. A 39-mer oligonucleotide complementary to rat PST cDNA was synthesized to investigate the distribution of its mRNA in the developing and adult rat brain by Northern blot and in situ hybridization. In the embryonic rat brain, PST mRNA was detected abundantly throughout the neuroepithelia of most brain regions. At post-natal days 1 and 14, PST was detected throughout the neocortex, in the pyramidal cells (PC) of the hippocampus proper, the granule cell layer (GCL) of the dentate gyrus, the anterior ventral nucleus of the thalamus (AVNT) and the GCL and external germinal layer of the cerebellum. Finally, from PD21 until adulthood, expression of PST mRNA was restricted to the PC layer of the hippocampus proper, the GCL of the dentate gyrus, the AVNT, the GCL of the cerebellum and the dorsal and lateral nucleus of the anterior olfactory bulb. The developmental profile of PST mRNA is paralleled in some structures by that of the PSA-NCAM, there are, however, notable exceptions. Therefore, our results demonstrate that expression of rat PST mRNA is developmentally regulated, is present in the adult rat brain in restricted areas and may be involved in regulating temporal and spatial expression of PSA-NCAM.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0169-328X
pubmed:author
pubmed:issnType
Print
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-81
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9427508-Aging, pubmed-meshheading:9427508-Amino Acid Sequence, pubmed-meshheading:9427508-Animals, pubmed-meshheading:9427508-Brain, pubmed-meshheading:9427508-Cloning, Molecular, pubmed-meshheading:9427508-Cricetinae, pubmed-meshheading:9427508-Embryonic and Fetal Development, pubmed-meshheading:9427508-Female, pubmed-meshheading:9427508-Gene Expression Regulation, Developmental, pubmed-meshheading:9427508-Gene Expression Regulation, Enzymologic, pubmed-meshheading:9427508-Gestational Age, pubmed-meshheading:9427508-Humans, pubmed-meshheading:9427508-In Situ Hybridization, pubmed-meshheading:9427508-Male, pubmed-meshheading:9427508-Mice, pubmed-meshheading:9427508-Molecular Sequence Data, pubmed-meshheading:9427508-Pregnancy, pubmed-meshheading:9427508-RNA, Messenger, pubmed-meshheading:9427508-Rats, pubmed-meshheading:9427508-Rats, Sprague-Dawley, pubmed-meshheading:9427508-Recombinant Proteins, pubmed-meshheading:9427508-Sequence Alignment, pubmed-meshheading:9427508-Sequence Homology, Amino Acid, pubmed-meshheading:9427508-Sialyltransferases, pubmed-meshheading:9427508-Transcription, Genetic
pubmed:year
1997
pubmed:articleTitle
Cloning and in situ hybridization analysis of the expression of polysialyltransferase mRNA in the developing and adult rat brain.
pubmed:affiliation
Douglas Hospital Research Centre, Department of Psychiatry, McGill University, Montreal, Que., Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't