Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family

Nardelli-Haefliger, Denise; Moskaitis, John E.; Schoenberg, Daniel R.; Wahli, Walter

doi:10.1007/bf02103621

Cited by 52 publications

(31 citation statements)

References 47 publications

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“…Through quantitative amino acid sequence comparisons, it is apparent that albumins and alpha-fetoproteins are more similar to each other than either is to the vitamin D-binding proteins. Specifically, the albumin/alpha-fetoprotein divergence has been estimated to have occurred between 300 and 500 million years (Myr) ago , with another estimate putting the separation somewhat later at 220-340 Myr ago (Haefliger et al, 1989). The gene duplication events involving the vitamin D-binding protein are generally agreed to predate the albumin/ alpha-fetoprotein divergence, with the only published estimate placing the separation between 560 and 600 Myr ago (Haefliger et al, 1989).…”

mentioning

confidence: 98%

“…This is not altogether unexpected, as the lamprey, which does not have a calcified skeleton, has no requirement for efficient regulation of calcium metabolism. This puts the occurrence of the vitamin D-binding proteinlalbumin gene duplication events at no greater than 450 Myr ago, in contrast to the 560-600 Myr ago predicted by Haefliger et al (1989). The sequence alignments (Fig.…”

Section: Chronology Of a Familymentioning

confidence: 99%

“…In 1975 the amino acid sequences of bovine (Brown, 1975) and human (Behrens et al, 1975;Meloun et al, 1975) albumins were reported. Since that time, the cDNA sequence, and thus the inferred amino acid sequence, has been determined for the following vertebrate albumins: human (Lawn et al, 1981;Dugaiczyk et al, 1982), rat (Sargent et al, 1981b), mouse (Minghetti et al, 1985), pig (Weinstock & Baldwin, 1988), sheep (Brown et al, 1989), frog (Haefliger et al, 1989), and salmon (Byrnes & Gannon, 1990). The most characteristic feature of the albumin sequence is the repetitious pattern of 17 disulfide bridges that organizes the molecule into three homologous, yet distinct, domains.…”

mentioning

confidence: 99%

“…Specifically, the albumin/alpha-fetoprotein divergence has been estimated to have occurred between 300 and 500 million years (Myr) ago , with another estimate putting the separation somewhat later at 220-340 Myr ago (Haefliger et al, 1989). The gene duplication events involving the vitamin D-binding protein are generally agreed to predate the albumin/ alpha-fetoprotein divergence, with the only published estimate placing the separation between 560 and 600 Myr ago (Haefliger et al, 1989). Given that the cyclostomes (lampreys and hagfish) and mammals last shared a common ancestor about 450 Myr ago, and that the major duplication events leading to modern, three-domain albumins are thought to have occurred some 400-600 Myr ago (Doolittle, 1984), there was Kuyas et al, 1983.…”

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confidence: 99%

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Characterization, primary structure, and evolution of lamprey plasma albumin

Gray

Doolittle

1992

Protein Science

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The most abundant protein found in blood plasma from the sea lamprey (Petromyzon marinus) has the hallmarks of a plasma albumin: namely, high abundance, solubility in distilled water, a small number of tryptophans, and a high content of cysteines and charged residues. As in other vertebrate albumins, not all the cysteines are disulfide bonded. An unusual feature of this protein is its molecular weight of 175,000, roughly 2.5 times the size of other vertebrate albumins. Its amino acid sequence, deduced from a series of overlapping cDNA clones, can be aligned with other members of the gene family including plasma albumin, alpha-fetoprotein, and vitamin-D binding protein, confirming that it is indeed an oversized albumin. An unusual feature of the sequence is a 28-amino acid stretch consisting of a serine-threonine repeat with the general motif (STTT). Lamprey albumin contains a 23-amino acid putative signal peptide and a 6-residue putative propeptide, which, when cleaved, yield a mature protein of 1,394 amino acids with a calculated molecular weight of 157,000. The sequence also includes nine potential N-linked glycosylation sites (Asn-X-Ser/Thr), consistent with observation that lamprey albumin is a glycoprotein. If all the potential glycosylation sites were occupied by clusters of 2,000 molecular weight each, the total molecular weight would be 175,000. Like other members of the gene family, lamprey albumin is composed of a series of 190-amino acid repeats, there being seven such domains all together. Quantitative amino acid sequence comparisons of lamprey albumin with the other members of the gene family indicate that it diverged from an ancestral albumin prior to the gene duplications leading to this diverse group. This notion is confirmed by the pattern of amino acid insertions and deletions observed in a consideration of all domains that compose this family. Furthermore, it suggests that the invention of albumin antedates the vertebrate radiation.Keywords: plasma albumin; protein evolution; sea lamprey Plasma albumin is the most abundant protein in vertebrate blood plasma and also among the most readily purified. The ability to secure relatively pure albumin in large quantities has led to it becoming one of the most familiar and extensively studied of all proteins. Its principal role is thought to be that of a transport protein, reversibly binding fatty acids, bilirubin, and a myriad of other molecules, as well as its being a major contributor to the effective osmotic pressure of the plasma. As a result of its ligand-binding properties and high concentration, albumin provides a stabilizing effect on plasma solute levels, buffering the concentration of metabolites. Paradoxically, humans and some other animals appear to be quite capable of surviving with levels of albumin in

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confidence: 98%

Section: Chronology Of a Familymentioning

confidence: 99%

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confidence: 99%

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Characterization, primary structure, and evolution of lamprey plasma albumin

Gray

Doolittle

1992

Protein Science

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“…The sequences of a number of albumins have been determined including those of human serum albumin (HSA) [4-71, bovine serum albumin (BSA) [8] (Holowachuk E. W., unpublished results), ovine serum albumin (OSA) [9], porcine serum albumin (PSA) [lo], rat serum albumin (RSA) [ll], mouse serum albumin (MSA) [12], frog serum albumin [13], salmon serum albumin [14] and lamprey serum albumin [15]. In all of these albumins the characteristic repeating series of disulphides is strictly conserved leading to further expectation of a common topology.…”

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X‐ray and primary structure of horse serum albumin (Equus caballus) at 0.27‐nm resolution

Holowachuk

Norton

et al. 1993

European Journal of Biochemistry

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The amino-acid sequence and three-dimensional structure of equine serum albumin have been determined. The amino-acid sequence was deduced from cDNA isolated from equine liver. Comparisons of the primary structure of equine serum albumin with human serum albumin and bovine serum albumin reveal 76.1 % and 73.9% sequence identity, respectively. The three-dimensional structure was determined crystallographically by the molecular-replacement method using molecular coordinates from the previously determined structure of human serum albumin, to a resolution of 0.27 nm. In accordance with the primary structure, the three-dimensional structures are highly conserved. There is a root-mean-square difference between a-carbons of the two structures of 0.201 nm. The association constants (Ka) for the binding of 2,3,5-triiodobenzoic acid were determined by ultrafiltration methods for equine and human serum albumins to be approximately 1WM-l and 105M-', respectively. Crystallographic studies of equine serum albumin reveal two binding sites for 2,3,5-triiodobenzoic acid identical with those previously reported for human serum albumin which are located within subdomains IIA and IIIA. Details and comparisons of the binding chemistry are discussed.As the most abundant protein of the circulatory system albumin functions as a multipurpose transport molecule and is a principal contributor to colloid osmotic blood pressure.

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Partial clone of the gene for AS protein of the lampreyPetromyzon marinus, a member of the albumin supergene family whose expression is restricted to the larval and metamorphic phases of the life cycle

et al. 1998

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AS was previously found to be a liver‐synthesized serum protein that is found in the larval (ammocoete), metamorphosing, and juvenile individuals during the life cycle of Petromyzon marinus but not in the sexually mature upstream‐migrant individuals (Filosa et al. [1982] Comp. Biochem. Physiol., 72B:521–530; [1986] Comp. Biochem. Physiol., 83B:143–149; Ito et al. [1988] J. Exp. Zool., 245:256–263). In the present work, a partial clone for the gene for the AS protein was isolated from a cDNA expression library made from ammocoete liver. Northern blots using this clone showed hybridization with mRNA from the intervals of the life cycle prior to the upstream‐migration period but not from the upstream‐migration period itself. The cloned DNA was sequenced and the deduced amino acid sequence was found to have 40% identity with an albumin (our SDS‐1 protein) from the upstream migrants of P. Marinus (Gray and Doolittle, [1992] Protein Sci., 1:289–302), which is homologous to mammalian serum albumin. Thus the lamprey has two genes, AS and SDS‐1, that code for different but similar albumin‐like proteins, which predominate at different phases in its life cycle. It is suggested that AS protein, because it is present only at the earlier phases of the life cycle and because its gene is transcribed only during this same period, may be an early version of the α‐fetoprotein (AFP) of mammals that is found only in the embryonic, fetal, and neonatal phase of their life cycle. J. Exp. Zool. 282:301–309, 1998. © 1998 Wiley‐Liss, Inc.

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Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family

Cited by 52 publications

References 47 publications

Characterization, primary structure, and evolution of lamprey plasma albumin

Characterization, primary structure, and evolution of lamprey plasma albumin

X‐ray and primary structure of horse serum albumin (Equus caballus) at 0.27‐nm resolution

Partial clone of the gene for AS protein of the lampreyPetromyzon marinus, a member of the albumin supergene family whose expression is restricted to the larval and metamorphic phases of the life cycle

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