Cloning of cDNA encoding a newly recognized apolipoprotein-like protein and its expression in the northern sea urchin Mesocentrotus nudus

• Published in: Fisheries science Vol. 88; no. 2; pp. 259 - 273
• Main Authors: Yuhi, Tomoharu, Nishimiya, Osamu, Ohno, Kaoru, Takita, Asami, Inoguchi, Takako, Ura, Kazuhiro, Takagi, Yasuaki
• Format: Journal Article
• Language: English
• Published: Tokyo Springer Japan 01.03.2022; Springer Nature B.V
• Subjects: Animal embryos; Apolipoprotein B; Apolipoproteins; Biomedical and Life Sciences; Carotenoids; Cloning; Coelomic fluids; Complementary DNA; Digestive system; Digestive tract; DNA; Echinoidea; Egg yolk; Eggs; Fish & Wildlife Biology & Management; Food Science; Freshwater & Marine Ecology; Gametogenesis; Growth; Invertebrates; Life Sciences; Lipids; Manganese; Marine invertebrates; Mesocentrotus nudus; Molecular structure; Nutrients; Oogenesis; Original Article; Oviparity; Physiological functions; Precursors; Proteins; Saccharides; Sea urchins; Stomach; Structural analysis; Transcription; Transferrin; Transferrin-like protein; Transferrins; Vitellogenesis; Yolk; Yolk protein; Large lipid transfer protein superfamily; Major yolk protein; Apolipoprotein; Sea urchin
• ISSN: 0919-9268; 1444-2906
• DOI: 10.1007/s12562-022-01584-3

Accumulation of yolk precursor protein in the oviparous egg is essential for embryo growth. Transferrin-like protein, also known as major yolk protein, is a major precursor protein in sea urchins and sea cucumbers. In sea urchins, a new yolk protein was recently detected in Strongylocentrotus intermedius and Mesocentrotus nudus eggs. This protein, tentatively named yolk-related protein (YRP), was thought to have important physiological functions for sea urchin gonadal growth and gametogenesis. To understand the relationship between YRP and vitellogenesis, we investigated the molecular structure of sea urchin YRP, quantified the transcript levels during oogenesis, and identified the presence of YRP in coelomic fluid. Using molecular cloning, we characterized one cDNA that encoded YRP (mn- yrp ). Structural analysis revealed that mn-YRP is an apolipoprotein B (ApoB)-like protein that belongs to the large lipid transfer protein superfamily. Quantification of mn- yrp (mn- apob ) transcripts showed that mn- apob is mainly expressed in the stomach during gonadal growth. Immunobiochemical methods using antiserum revealed that mn-ApoB was present in the coelomic fluid. These results indicate that ApoB has a role in the transport of nutrients, such as sugar, lipids, and carotenoids, from the digestive tract to eggs via coelomic fluid in sea urchin.