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Updated: Jul 18, 2026

Functional Cloning Using a Xenopus Oocyte Expression System
Published on: January 30, 2016
Cloning and expression analysis of goldfish (Carassius auratus L.) prominin
John G Walsh1, Daniel R Barreda, Miodrag Belosevic
1Department of Biological Sciences, CW-405 Biological Sciences Centre, University of Alberta, Edmonton, Alta T6G 2E9, Canada.
Abstract:
The integral membrane protein known as prominin was first identified on the apical surface of mouse neural epithelial cells as well as on the surface of human haematopoietic progenitor cells. This report describes a prominin-like sequence and expression analysis of the prominin in the goldfish. The predicted amino acid sequence for goldfish prominin shares all of the hallmark structural characteristics of the prominin family, however the relatedness assessed using the percent amino acid identity indicated that goldfish prominin cannot be placed into the current mammalian dichotomy of type 1 or 2. The real time PCR analyses indicated that prominin was broadly expressed in different tissues with particularly high levels observed in the kidney and gill of the goldfish. Goldfish prominin was also found to be differentially expressed in subpopulations of in vitro-derived goldfish macrophages, with the highest expression observed in progenitor cells.

