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Tissue protein chemistry of UV-absorbing compounds

W.M. BANDARANAYAKE, B.E. CHALKER AND W.C. DUNLAP


Symbiotic unicellular algae (zooxanthellae) in reef-building corals provide food and cause coral to deposit its calcium carbonate skeleton by photosynthesis. Further, the (UV) ultraviolet-absorbing agents called the mycosporins1, produced by the symbionts, protect shallow-water corals from the damaging effects of UV radiation.



Mycosporin-like amino acids (MAAs)(1-5), which absorb UV light strongly at (lmax 310-360) (e 35,000-40,000) nm, can be considered to be formed by the reaction of 4-dehydroxy gadusol (8) with amino acids and amino alcohols. The efficacy of these natural UV-absorbing substances could be used for the benefit of human skin protection and other commercial applications. Analogues of mycosporins can be synthesised, by reacting 1,3 diketones with primary and secondary amines, amino acids and amino alcohols.

MAAs, when present in marine invertebrates having symbiotic algae (e.g. Pacific staghorn coral Acropora formosa) are freely diffusable (i.e. soluble but not associated with any protein species) whereas, in invertebrates without symbiotic algae where MAAs are obtained mainly through diet, (e.g. crown-of-thorns starfish - Acanthaster planci) the MAAs are protein 'associated'. In these invertebrates protein-associated MAA's are distributed in most tissues but are concentrated on the outer epidermal tissues, and in the case of telostean fish, in their eye lenses as well.

Mesopelagic fish have been shown to possess a variety of largely unidentified short wave absorbing pigments within their lenses. Among the identified pigments are carotenoids, kyourenine (6) and 3-hydroxy kynurenine(7). The tryptophan derived pigments (6), (7), also found in terrestrial vertebrates, have been isolated from a deep sea species and several closely related tropical fresh water species, respectively2.



The lenses of many shallow water fish also absorb short wave radiation and the pigments in these lenses have been identified as MAAs3. These pigments appear more widespread and have been isolated from lenses of fish from a variety of habitats3. Pigments extracted from 52 species have been identified as palythine(2) asterina-330(3) palythinol(4) and palythene(5). In the majority of species asterina-330 was the most abundant pigment.

Gadusol(9), which is structurally related to the MAAs, is present in the fish ovaries that contain ripe eggs just before spawning, and is a rninor component in the fish lenses.

Asterina-330 and gadusol exist in association with soluble proteins in fish lenses. The highly unstable major complex with absorption lmax 330 nm when dissociated yielded asterina-330 (lmax330 nm) and a protein of MW 80-100 kDa (lmax280 nm). The second, relatively 'stable' minor complex of lmax323 nm, under similar conditions, yielded gadusol (lmax269) and a protein of MW 20-30 kDa (lmax280).

The molecular weights of the two proteins are characteristic of b and g crystallins, respectively, which are two of the three major soluble crystallin protein present in fish lenses.

Thus, it appears that while the highly unstable complex is an association of asterina-330 and b crystallin, the second complex probably is a Schiff's base formed by the 'reaction' of gadusol and g crystallin. It is interesting to note that this latter 'association' is similar in nature to the visual pigment Rhodopsin, (lmax498 nm) a Schiff's base which contains 11-cis retinal (lmax382 nm) as a prosthetic group and a lipoprotein, opsin (lmax280 nm). It is noteworthy that while gadusol was present in the ripe fish eggs, asterina-330 was absent. Asterina-330 may be assimilated through diet and/or may have been synthesised by the animal from the mycospoorins present in the diet.

It is suggested that the short-wave absorbing pigments in shallow water fish protect the retina from harmful UV light or they enhance visual acuity by excluding the shorter wavelengths responsible for chromatic aberration and scatter. However, the functional significance of these pigments and complexes remains unclear.

REFERENCES
1 Takano, S., et al., (1979) Chemistry Letters, 419.
2 Truscott, R.J.W., et al., (1992) Experimental Eye Research, 1015.
3 Dunlap,W.C. et al., (1989) Comparative Biochemistry and Physiology, 3(93B), 601.


For more information contact
Dr. W. Bandaranayake
Australian Institute of Marine Science
PMB 3, Townsville MC
Queensland 4810, Australia.

Fax: +61 7 47725852
e-mail:
banda@aims.gov.au

 

 

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