J Exp Zool 2000 Dec 15;2884:335-44. doi: 10.1002/1097-010X(20001215)288:4<335::AID-JEZ6>3.0.CO;2-1.

Serum amyloid A protein in an echinoderm: its primary structure and expression during intestinal regeneration in the sea cucumber Holothuria glaberrima.

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Serum amyloid A (SAA) proteins comprise a family of highly conserved apolipoproteins found in all mammals thus far investigated, and also in ducks and salmonid fishes. However, no invertebrate SAA homologues have been detected to date. Here we report the characterization of the first SAA homologue in a nonvertebrate deuterostome, the echinoderm Holothuria glaberrima. A 971-base-pair cDNA was obtained from a regenerating intestine cDNA library. The clone contains a 369-nucleotide open reading frame corresponding to a 122-amino-acid protein exhibiting a high degree of homology to members of the SAA superfamily. Sequence alignments of the holothuroid and vertebrate SAA proteins make evident a remarkable degree of conservation, even between phylogenetically disparate groups. Northern blots and immunohistochemistry show that SAA expression increases during regeneration of the holothuroid digestive tract as compared with normal nonregenerating tissue, and that the SAA protein is expressed by cells of the coelomic epithelium of the regenerating intestine. While SAA expression during the initial wound healing stage of regeneration is minimal, it increases during subsequent stages, peaking at day 15 of regeneration, concomitantly with lumen formation and the organization of the muscular layers of the regenerating digestive tract. Although in vertebrates SAA proteins may be part of a well-conserved anti-inflammatory mechanism, their exact biological function remains obscure. Our results suggest the possibility that SAA proteins, although structurally conserved, may possess enough functional diversity to participate in processes other than anti-inflammatory responses.

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Genes referenced: LOC100887844