2014 journal article
Lrp13 is a novel vertebrate lipoprotein receptor that binds vitellogenins in teleost fishes
JOURNAL OF LIPID RESEARCH, 55(11), 2287–2295.
author keywords: affinity purification; egg; endocytosis; oocyte; oogenesis; ovary; vitellogenesis; very low density lipoprotein receptor; yolk; low density lipoprotein receptor-related protein 13
MeSH headings : Animals; Bass; Cloning, Molecular; Fish Proteins / chemistry; Fish Proteins / genetics; Fish Proteins / metabolism; Gene Expression Regulation; Humans; Intracellular Space / metabolism; Protein Binding; Protein Transport; Receptors, Lipoprotein / chemistry; Receptors, Lipoprotein / genetics; Receptors, Lipoprotein / metabolism; Vitellogenins / metabolism
TL;DR:
The Lrp13 appears to function as a vitellogenin receptor and may be an important mediator of yolk formation in fishes and other oviparous vertebrates and the presence of lp13 orthologs in mammals suggests that this lipoprotein receptor is widely distributed among vertebrates, where it may generally play a role in lipop protein metabolism.
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open access via www.jlr.org (publisher PDF)
UN Sustainable Development Goal Categories
14. Life Below Water
(Web of Science; OpenAlex)
Source: Web Of Science
Added: August 6, 2018
Transcripts encoding a novel member of the lipoprotein receptor superfamily, termed LDL receptor-related protein (Lrp)13, were sequenced from striped bass (Morone saxatilis) and white perch (Morone americana) ovaries. Receptor proteins were purified from perch ovary membranes by protein-affinity chromatography employing an immobilized mixture of vitellogenins Aa and Ab. RT-PCR revealed lrp13 to be predominantly expressed in striped bass ovary, and in situ hybridization detected lrp13 transcripts in the ooplasm of early secondary growth oocytes. Quantitative RT-PCR confirmed peak lrp13 expression in the ovary during early secondary growth. Quantitative mass spectrometry revealed peak Lrp13 protein levels in striped bass ovary during late-vitellogenesis, and immunohistochemistry localized Lrp13 to the oolemma and zona radiata of vitellogenic oocytes. Previously unreported orthologs of lrp13 were identified in genome sequences of fishes, chicken (Gallus gallus), mouse (Mus musculus), and dog (Canis lupus familiaris). Zebrafish (Danio rerio) and Nile tilapia (Oreochromis niloticus) lrp13 loci are discrete and share genomic synteny. The Lrp13 appears to function as a vitellogenin receptor and may be an important mediator of yolk formation in fishes and other oviparous vertebrates. The presence of lrp13 orthologs in mammals suggests that this lipoprotein receptor is widely distributed among vertebrates, where it may generally play a role in lipoprotein metabolism.