Human Neuronal Pentraxin II (NPTX2): Conservation, Genomic Structure, and Chromosomal Localization

We have previously identified a novel rat neuronal member of the pentraxin family (neuronal pentraxin) that may mediate the uptake of synaptic material and the presynaptic snake venom toxin, taipoxin. Here we report human cDNA and genomic sequences of a second neuronal pentraxin. This pentraxin, whi...

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Bibliographic Details
Published in:Genomics (San Diego, Calif.) Calif.), 1995-07, Vol.28 (2), p.220-227
Main Authors: Hsu, Yung-Chin, Perin, Mark S.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Biological and medical sciences
Brain Chemistry
C-Reactive Protein - genetics
Chromosomes, Human, Pair 7
Cloning, Molecular
DNA, Complementary - genetics
Fundamental and applied biological sciences. Psychology
Genes. Genome
Glycosylation
Guinea Pigs
Humans
Leucine Zippers - genetics
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Nerve Tissue Proteins - genetics
Proteins - genetics
Rats
RNA, Messenger - analysis
Sequence Alignment
Sequence Homology, Amino Acid
Species Specificity
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Summary:We have previously identified a novel rat neuronal member of the pentraxin family (neuronal pentraxin) that may mediate the uptake of synaptic material and the presynaptic snake venom toxin, taipoxin. Here we report human cDNA and genomic sequences of a second neuronal pentraxin. This pentraxin, which we propose to name neuronal pentraxin II (NPII; gene symbol NPTX2), shows 54% amino acid identity to rat neuronal pentraxin (NPI) with 69% identity over the carboxyl-terminal half of NPI and is 88% identical to a newly identified sperm acrosomal pentraxin p50/apexin. Northern blot analysis reveals that NPII message is present in brain, testis, pancreas, liver, heart, and skeletal muscle, so, unlike NPI, NPII is not exclusively localized to neurons. Like NPI, NPII has potential N-linked glycosylation sites. The human NPII gene is 11 kb in length, contains four introns, and is localized to chromosome 7q21.3-q22.1. These data demonstrate the existence of a family of pentraxin proteins that are expressed in the brain and other tissues and that may play important roles in the uptake of extracellular material.
ISSN:0888-7543
1089-8646
DOI:10.1006/geno.1995.1134