Nucleotide sequence and the encoded amino acids of human serum albumin mRNA.

Dugaiczyk, Achilles; Law, Simon W.; Dennison, Olivia

doi:10.1073/pnas.79.1.71

Cited by 293 publications

(119 citation statements)

References 17 publications

Supporting

Mentioning

114

Contrasting

Unclassified

Order By: Relevance

“…MDA levels were also elevated in β-TM patients (median [IQR], 30 nmol/ ml) with a range of 10-112 nmol/ml compared with the control group (median [IQR], 10 [7][8][9][10][11][12][13][14][15] nmol/ml; range 5-18 nmol/ml); p < 0.001 (Table 1 and Figure 1).…”

Section: Levels Of Ima and Mda In Patients With β-Tm And Healthy Contmentioning

confidence: 93%

“…Human serum albumin (HSA) is composed of 585 amino acids (66,438 Da), containing 17 pairs of intra-molecular disulfide bridges and one free cysteine (Cys34) [9]. HSA has the unique capability of binding reversibly or covalently to a wide diversity of ligands including water, cations (such as Ca 2+ , Na + and K + ), fatty acids, hormones, bilirubin and drugs [10].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Ischemia-modified albumin as a marker of vascular dysfunction and subclinical atherosclerosis in β-thalassemia major

et al. 2017

View full text Add to dashboard Cite

Background: Ischemia-modified albumin (IMA) is an altered type of serum albumin that forms under conditions of oxidative stress and an independent predictor of major adverse cardiovascular events. Objectives: To measure the levels of IMA in 45 children and adolescents with β-thalassemia major (β-TM) compared with 30 healthy controls and assess its relation to lipid peroxidation, vascular complications and subclinical atherosclerosis. Methods: β-TM patients without symptoms of heart disease were studied focusing on transfusion history, chelation therapy, serum ferritin, malondialdehyde (MDA) and IMA levels. Echocardiography was performed and carotid intima media thickness (CIMT) was assessed. Results: IMA and MDA levels were significantly higher in β-TM patients compared with controls (p < 0.001). IMA was higher among patients with heart disease, pulmonary hypertension risk and serum ferritin ≥2500 µg/l than those without. TM patients compliant to chelation had significantly lower IMA levels. IMA levels were positively correlated to MDA and CIMT while negatively correlated to ejection fraction and fractional shortening. Conclusion: Our results highlight the role of oxidative stress in the pathophysiology of vascular complications in thalassemia. IMA could be useful for screening of β-TM patients at risk of cardiopulmonary complications and atherosclerosis because its alteration occurs in early subclinical disease.

show abstract

Section: Levels Of Ima and Mda In Patients With β-Tm And Healthy Contmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Ischemia-modified albumin as a marker of vascular dysfunction and subclinical atherosclerosis in β-thalassemia major

et al. 2017

View full text Add to dashboard Cite

show abstract

“…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%

Characterization, primary structure, and evolution of lamprey plasma albumin

Gray

Doolittle

1992

Protein Science

View full text Add to dashboard Cite

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

show abstract

“…First, a large number of proteins are known to be proteolyzed within the endomembrane system, at sites separate from signal peptidase cleavage. These include the endoproteolytic processing of, for example, proalbumin (Dugaiczyk et al, 1982), proinsulin (Nolan et al, 1971), interleukin 3 (Fung et al, 1984;Yokota et al, 1984), prosomatostatin (Benoit et al, 1988;Lepage-Lezin et al, 1991 ;Goodman et al, 1983), prodynorphin (Devi et al, 1989;Civelli et al, 1985), and the procorticotropidendorphin precursor (Schnabel et al, 1989). These cleavages occur on either side of dibasic pairs of amino acids, such as Arg-Arg or Lys-Arg, or on the COOH- (Benoit et al, 1988;Fung et al, 1984) or NH,-terminal side (Devi et al, 1989;Civelli et al, 1985) of monobasic residues, usually Arg, in a number of processed proteins.…”

mentioning

confidence: 99%

Proteins of the Golgi apparatus

Bendiak

Ward

Simpson

1993

European Journal of Biochemistry

View full text Add to dashboard Cite

The Golgi marker enzyme, UDP‐galactose: N‐acetylglucosamine β1‐4galactosyltransferase (β1‐4GalT) was purified 44300‐fold in its intact, membrane‐bound form from rat liver membranes. The protein was isolated from detergent extracts as a high‐Mr form, having a Stokes radius approximating a globular protein of Mr 440000. It is comprised of a single protein component as observed on SDS/polyacrylamide gels, having an Mr near 51000, and does not have intermolecular disulfide crosslinks. N‐terminal sequencing of the enzyme demonstrated that it contains an N‐terminal hydrophobic stretch deduced previously from cDNA encoding for the enzyme. Previous studies have indicated that the protein may be translated at either of two AUG sites near the 5′ end of the mRNA [Russo, R. N, Shaper, N. L. & Shaper, J. H. (1990) J. Biol. Chem. 265, 3324–3331], giving rise to two polypeptides, one appended with 13 amino acids. In the work described here, evidence was only found for the sequence of the short form, missing a single methionine at the N‐terminus. Mild proteolytic treatment cleaved the enzyme, giving rise to low‐Mr forms which were fully catalytically active and which, upon sequencing, were missing a 66‐amino‐acid stretch from the N‐terminus (as compared to the mouse cDNA). Proteolytic treatment was accompanied by conversion of the form having a large Stokes radius to one approximating a globular protein with Mr near 50000. The N‐terminal stretch appears to contribute to maintenance of the form having a large Stokes radius. This may be the result of interaction with a detergent micelle, dimerization or oligomerization, or interaction with some other large, non‐protein molecule, although a detergent exchange still resulted in a form having a large Stokes radius.

show abstract

Nucleotide sequence and the encoded amino acids of human serum albumin mRNA.

Cited by 293 publications

References 17 publications

Ischemia-modified albumin as a marker of vascular dysfunction and subclinical atherosclerosis in β-thalassemia major

Ischemia-modified albumin as a marker of vascular dysfunction and subclinical atherosclerosis in β-thalassemia major

Characterization, primary structure, and evolution of lamprey plasma albumin

Proteins of the Golgi apparatus

Contact Info

Product

Resources

About