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Tissue
protein chemistry of UV-absorbing compounds
W.M. BANDARANAYAKE, B.E. CHALKER AND W.C. DUNLAP
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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.
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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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