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LEPREL1, a novel ER and Golgi resident member of the Leprecan family.

Journal article
Authors Sofia Järnum
Christian Kjellman
Anna Darabi
Ingar Nilsson
Klaus Edvardsen
Pierre Åman
Published in Biochemical and biophysical research communications
Volume 317
Issue 2
Pages 342-51
ISSN 0006-291X
Publication year 2004
Published at Institute of Laboratory Medicine, Dept of Pathology
Pages 342-51
Language en
Links dx.doi.org/10.1016/j.bbrc.2004.03.0...
Keywords Amino Acid Sequence, Animals, Cell Line, Tumor, Endoplasmic Reticulum, metabolism, ultrastructure, Fibrosarcoma, genetics, metabolism, Golgi Apparatus, metabolism, ultrastructure, Humans, Membrane Glycoproteins, chemistry, genetics, metabolism, Mice, Molecular Sequence Data, Organ Specificity, Proteoglycans, chemistry, genetics, metabolism, Sequence Analysis, Protein, Sequence Homology, Amino Acid, Species Specificity, Tissue Distribution
Subject categories Medical and Health Sciences

Abstract

We have identified a novel protein, Leprecan-like 1 (LEPREL1), with profound similarity to the Leprecan family of proteoglycans. The genomic organization of the Leprecan gene family was found to be highly conserved. Expression analysis shows that LEPREL1 is expressed in most tissues as a 3.4 kb transcript encoding an 80 kDa protein. A LEPREL1 specific antibody stains many cell types including adipocytes and neuroendocrine cells of the gastrointestinal epithelium. Muscle tissue contains a specific 6.5 kb transcript and a 200 kDa protein. The 3.4 kb LEPREL1 transcript encodes a 708 amino acid protein containing a signal sequence, four tetratricopeptide repeats (TPRs), a leucine zipper, a P-loop, a prolyl 4-hydroxylase alpha domain (P4Halpha), and a C-terminal KDEL ER-retention motif. LEPREL1 is localized to the ER and Golgi network and over-expressing it affects normal protein disulfide isomerase staining patterns in the ER.

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