Identical structural changes in inherited albumin variants from different populations.

Arai, Kunio; Ishioka, Noriaki; Huss, Karen; Madison, Jeanne; Putnam, Frank W.

doi:10.1073/pnas.86.2.434

Cited by 23 publications

(35 citation statements)

References 21 publications

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“…In the present work the five variants were compared at pH 4.0 and 5.6 with reference alloalbumins for which the substitution was known. The reference variants with known substitutions are albumin Mexico (slow + 1, 550 Asp Gly) (10), albumin B Lubeck (slow +2, 570 Glu -* Lys) (15), and proalbumin Pollibauer (Lille type, slow +2, -2 Arg -+ His) (11). The five Japanese variants showed different combinations of mobilities in the two buffer systems; all were also different from albumin B and proallbumin Pollibauer.…”

Section: Resultsmentioning

confidence: 99%

“…However, we recently reported that the 570 Glu -* Lys exchange is present in an albumin variant occurring in two unrelated Japanese and one Cambodian (15). The two type B albumins from Japan were designated Tokyo-1 and Shinanomachi-1, and the one from Cambodia was designated Phnom Penh.…”

Section: Sugita Et Al (21) Had Reported That the Molecular Abnormalitymentioning

confidence: 99%

“…This, together with its susceptibility to limited digestion with trypsin (11), suggested that this variant was a proalbumin. Purification of the proalbumin component was accomplished by use of ion-exchange HPLC (15). The purified proalbumin was applied directly to the Beckman protein sequencer and analyzed for 10 cycles.…”

Section: Sugita Et Al (21) Had Reported That the Molecular Abnormalitymentioning

confidence: 99%

“…Structural study of albumin Saitama-1 was done essentially by the procedure described by Arai et al for B albumins (15) except that the sequence was determined with the Applied Biosystems sequencer. Isoelectric focusing of a CNBr digest of the purified carboxymethylated albumin indicated that the substitution was located in CNBr fragment CB7 (residues 549-585).…”

Section: Sugita Et Al (21) Had Reported That the Molecular Abnormalitymentioning

confidence: 99%

“…For want of structural information such variants generally have been assigned ethnic or geographical names. Recently we (4,(9)(10)(11)(12)(13)(14)(15) and others (16)(17)(18)(19)(20)(21) have determined the structural change in a number of variant albumins. We have now completed the structural study of the five rare types of inherited albumin variants discovered in the Biochemical Genetics Study of the Radiation Effects Research Foundation (RERF); this surveyed some 30 blood and plasma polypeptides in a cohort of 15,581 unrelated children in Nagasaki and Hiroshima (2).…”

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confidence: 99%

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Point substitutions in Japanese alloalbumins.

Arai

Madison²,

Huss³

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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We have completed the structural study of five rare types of inherited albumin variants (alloalbumins) discovered in the Biochemical Genetics Study of 15,581 unrelated children in Hiroshima and Nagasaki. We have also identified the structural chane inl five other alloalbumin specimens detected during clinical electrophoresis of sera from Japanese living near Tokyo. Each of the five albumin variants from Nagasaki and Hiroshima has a single amino acid substitution. AlU of these substitutions differ, and none has been reported in non-Japanese populations. No instances of proalbumin variants or of albumin B (the most frequent alloalbumins in Caucasians) were detected in the children in Hiroshima and Nagasaki. However, one instance of a variant proalbumin and two examples of albumin B occurred in Japanese from the vicinity of Tokyo. In addition a previously unreported point substitution was found in albumin Tochigi, which is present in two unrelated persons from Tochigi prefecture. Four of the point mutations in the Japanese alloalbumins are in close proximity in a short segment of the polypeptide chain (residues 354-382) in which three additional point substitutions have been reported in diverse populations. These results, combined with earlier data, suggest that point substitutions are grouped in certain segments of the albumin molecule.

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Section: Resultsmentioning

confidence: 99%

Section: Sugita Et Al (21) Had Reported That the Molecular Abnormalitymentioning

confidence: 99%

Section: Sugita Et Al (21) Had Reported That the Molecular Abnormalitymentioning

confidence: 99%

Section: Sugita Et Al (21) Had Reported That the Molecular Abnormalitymentioning

confidence: 99%

mentioning

confidence: 99%

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Point substitutions in Japanese alloalbumins.

Arai

Madison²,

Huss³

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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Mutations and polymorphisms of the gene of the major human blood protein, serum albumin

et al. 2008

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Communicated by Jürgen HorstWe have tabulated the 77 currently known mutations of the familiar human blood protein, serum albumin (ALB). A total of 65 mutations result in bisalbuminemia. Physiological and structural effects of these mutations are included where observed. Most of the changes are benign. The majority of them were detected upon clinical electrophoretic studies, as a result of a point mutation of a charged amino acid residue. Three were discovered by their strong binding of thyroxine or triiodothyronine. A total of 12 of the tabulated mutations result in analbuminemia, defined as a serum albumin concentration of o1 g/L. These were generally detected upon finding a low albumin concentration in patients with mild edema, and involve either splicing errors negating translation or premature stop codons producing truncated albumin molecules. A total of nine mutations, five of those with analbuminemia and four resulting in variants modified near the C-terminal end, cause frameshifts. Allotypes from three of the point mutations become N-glycosylated and one C-terminal frameshift mutation shows O-glycosylation. Hum Mutat 29(8), [1007][1008][1009][1010][1011][1012][1013][1014][1015][1016] 2008.

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Protein Binding of Anticancer Drugs

Sparreboom¹,

Loos²

2004

Handbook of Anticancer Pharmacokinetics and Pharmacodynamics

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Identical structural changes in inherited albumin variants from different populations.

Cited by 23 publications

References 21 publications

Point substitutions in Japanese alloalbumins.

Point substitutions in Japanese alloalbumins.

Mutations and polymorphisms of the gene of the major human blood protein, serum albumin

Protein Binding of Anticancer Drugs

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