The same substitution, glutamic acid----lysine at position 501, occurs in three alloalbumins of Asiatic origin: albumins Vancouver, Birmingham, and Adana.

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

doi:10.1073/pnas.85.18.6692

Cited by 18 publications

(28 citation statements)

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“…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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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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confidence: 99%

Point substitutions in Japanese alloalbumins.

Arai

Madison²,

Huss³

et al. 1989

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

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“…Alloalbuminemia is rare and has a cumulative frequency of only 1:3000 to 1:10,000 in most populations (18-25); thus, it is usually expressed in a heterozygous fashion. More than 100 alloalbumins that have been given geographical or tribal names have been identified by genetic screening (18)(19)(20), by blood donor surveys (21), or by clinical electrophoresis (22, 23), and at least 20 different sites of structural change have been determined (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17). Four types of alloalbumins have been identified: (i) a series of single-point mutants (1-7, 12-14, 16), (ii) several chain-termination mutants (10, 11), (iii) proalbumins (variants that retain a basic amino-terminal hexapeptide because of a mutation in the Arg-Arg propeptide sequence required for post-transcriptional processing) (8,15), and (iv) arginyl-albumin, a variant that begins with arginine followed by a polypeptide sequence of the usual length (585 amino acid residues) (ref.…”

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“…Because of the number and variety of the specimens reported here and the fact that most of the methods have been published in detail (1)(2)(3)(4)(5)(6)(7)(8)(9), only a summary of the methods is given for each individual albumin. The general procedure consists of seven steps and was modified as required in each case.…”

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“…The general procedure consists of seven steps and was modified as required in each case. The steps are as follows: (i) cellulose"acetate (Microzone) electrophoresis at pH 8.6 of the serum or the purified albumin; (ii) purification by HPLC of the total albumin (normal albumin A plus variant) by a method later referred to as the two-step procedure (4), reduction and carboxymethylation of the purified albumin and cleavage with CNBr (3, 4, 9); (iii) analytical isoelectric focusing of the CNBr digest to identify the CNBr fragment in which the substitution was localized (3)(4)(5)(6)(7)(8); (iv) HPLC peptide mapping on a preparative scale to purify the variant CNBr fragment (1-4); (v) HPLC peptide mapping of a tryptic or Staphylococcus aureus V8 protease digest of the purified CNBr fragment (1-5); (vi) amino acid analysis of the variant peptide(s) with the Beckman model 121M amino acid analyzer; and (vii) automated sequence determination with the Beckman model 890C sequencer (9) or with the Applied Biosystems model 477B sequencer. After K.A.…”

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“…The two-step procedure for purification of albumin consists of a combination of anion-exchange HPLC on a TSK-DEAE 5PW column (7.5 x 75 mm; Anspec, Ann Arbor, MI) and gel filtration with a TSK 4000SW column (7.5 X 600 mm; Anspec) under conditions described elsewhere (3,4 $To whom reprint requests should be addressed.…”

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Point substitutions in albumin genetic variants from Asia.

Arai

Madison²,

Shimizu³

et al. 1990

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

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Despite their rarity and physiologically neutral character, more inherited structural variants of serum albumin (alloalbumins) are known than for any other human protein except hemoglobin. Including three previously unreported examples described here, we have identified 13 different point substitutions in alloalbumins of Japanese origin. Of these only albumin B and two proalbumins have been reported in other ethnic groups, and these are the most common variants of European origin. Some alloalbumins of Asiatic origin, but not yet identified in Japanese, are present in diverse ethnic groups. An alloalbumin found in indigenes of New Guinea (lysine -* asparagine at position 313) is also present in Caucasians of various European descents. Albumin Lambadi, occurring in a tribal group in south India, has a mutation (glutamic acid -* lysine at position 501) also found as a rare variant in individuals of diverse ethnic origin resident on four continents. These results suggest that some alloalbumins with the same substitution may have originated by independent mutations in various populations. This, together with the apparent clustering of point substitutions in the protein structure, may reflect hypermutability of the albumin gene.Because of recent studies (1-17) more heritable structural variants of serum albumin (alloalbumins) are known than for any other human protein except hemoglobin. However, unlike the situation with hemoglobin variants, no adverse effect on molecular function has been attributed to alloalbumins. Alloalbuminemia is rare and has a cumulative frequency of only 1:3000 to 1:10,000 in most populations (18-25); thus, it is usually expressed in a heterozygous fashion. More than 100 alloalbumins that have been given geographical or tribal names have been identified by genetic screening (18)(19)(20), by blood donor surveys (21), or by clinical electrophoresis (22, 23), and at least 20 different sites of structural change have been determined (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17). Four types of alloalbumins have been identified: (i) a series of single-point mutants (1-7, 12-14, 16), (ii) several chain-termination mutants (10, 11), (iii) proalbumins (variants that retain a basic amino-terminal hexapeptide because of a mutation in the Arg-Arg propeptide sequence required for post-transcriptional processing) (8,15), and (iv) arginyl-albumin, a variant that begins with arginine followed by a polypeptide sequence of the usual length (585 amino acid residues) (ref. 17; C. B. Laurell and F.W.P., unpublished results).Recently we have undertaken a series of collaborative studies on alloalbumins from populations throughout the world (1-3, 5, 6). Our objectives have been to determine the structural changes and to correlate these with the molecular properties ofalbumin and with such genetic characteristics as the site and type of mutation, heritability, and frequency. In this paper we report structural studies on alloalbumins from eight unrelated Japanese residents of Japan or Hawaii and a...

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