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cDNA cloning and structural analysis of the human limbic-system-associated membrane protein (LAMP)
Journal article   Peer reviewed

cDNA cloning and structural analysis of the human limbic-system-associated membrane protein (LAMP)

Aurea F. Pimenta, Itzhak Fischer and Pat Levitt
Gene, v 170(2), pp 189-195
1996
DOI: https://doi.org/10.1016/0378-1119(96)84698-1
PMID: 8666243
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Cell adhesion molecules central nervous system glycoproteins glycosyl-phosphatidylinositol anchor immunoglobulin superfamily
The limbic-system-associated membrane protein (LAMP) is a 64–68-kDa neuronal surface glycoprotein distributed in cortical and subcortical regions of the limbic system. The human LAMP gene was cloned by RT-PCR using human cerebral cortex mRNA and oligodeoxyribonucleotide (oligo) primers derived from the rat lamp cDNA sequence. The human and rat LAMP cDNAs showed 94% identity at the nucleotide (nt) level, and the encoded 338-amino-acid (aa) polypeptides shared 99% sequence identity. All the important features of LAMP were conserved: (i) the deduced aa sequence reflecting a glycosyl-phosphatidylinositol (GPI)-anchor, ( ii) eight putative N-linked glycosylation sites, and ( iii) conserved pairs of Cys forming three internal repeats characteristic of the immunoglobulin superfamily (IgSF). Northern blot analysis indicated the presence of two mRNA transcripts in the human brain of a size identical to those identified in adult rat brain. These data indicate that LAMP is a highly conserved new member of the IgSF which, together with the opioid-binding cell adhesion molecule (OBCAM) and neurotrimin, comprises a new subfamily that has been designated as IgLONs. With a unique distribution in limbic structures, LAMP may play an important role in limbic system development and function, as suggested by previous in vitro and in vivo functional studies.

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Domestic collaboration
Web of Science research areas
Genetics & Heredity
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