Abstract

We report the detection of insulin-like antigens in a large range of species utilizing a modified ELISA plate assay and Western blotting. We tested the leaves or aerial parts of species of Rhodophyta (red alga), Bryophyta (mosses), Psilophyta (whisk ferns), Lycopodophyta (club mosses), Sphenopsida (horsetails), gymnosperms, and angiosperms, including monocots and dicots. We also studied species of fungi and a cyanobacterium, Spirulina maxima. The wide distribution of insulin-like antigens, which in some cases present the same electrophoretic mobility as bovine insulin, together with results recently published by us on the amino acid sequence of an insulin isolated from the seed coat of jack bean (Canavalia ensiformis) and from the developing fruits of cowpea (Vigna unguiculata), suggests that pathways depending on this hormone have been conserved through evolution.

Highlights

  • The peptide hormone insulin was discovered in 1921 by Banting and Best [1]

  • The results suggest that insulin-like antigens were present in most of the leaves examined

  • We showed that the alga Gracilariopsis sp, a common red alga from estuarine habitats, the cyanobacterium Spirulina maxima, and fungi like Shiitake (Lentinus edodes) and the yeast Saccharomyces cerevisiae all contain insulin-like antigens (Table 1)

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Summary

Introduction

The peptide hormone insulin was discovered in 1921 by Banting and Best [1]. Immediately after its discovery and isolation from dogs, two reports on the positive results obtained with similar purified preparations from several plants on the lowering of glucose levels in diabetic animals were published by Collip [2] and Best [3], investigators involved in the original discovery. Khanna et al [5,6,7] reported on the isolation of a protein from the fruits of the bitter gourd (Momordica charantia) that exerted positive effects on diabetic patients and showed properties similar to insulin. Following these reports, Collier et al [8] reported on the isolation from spinach, rye and Lemna gibba of proteins with molecular weights, chromatographic properties, immunological characteristics and biological activities identical to those of vertebrate insulins. No further structural information was given for these molecules at the time

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