Literature DB >> 17922076

Convergent evolution of human and bovine haptoglobin: partial duplication of the genes.

Krzysztof B Wicher1, Erik Fries.   

Abstract

Haptoglobin (Hp) is a hemoglobin-binding plasma protein consisting of two types of chains, called alpha and beta, which originate from a common polypeptide. In humans, but not in other mammals, Hp has been shown to occur in two allelic forms, Hp1 and Hp2, which differ in the length of the alpha-chain. The longer alpha-chain (in Hp2) seems to have arisen by an internal duplication of a gene segment coding for almost the entire alpha-chain of Hp1. In this article we show that Hp of cow (Bos taurus) contains an alpha-chain, the structure of which is similar to that of the human Hp2 alpha-chain. Furthermore, comparison of the structure of bovine Hp and human Hp2 suggests that the bovine gene arose by a duplication of the gene segment homologous to that duplicated in human Hp2. However, a phylogenetic analysis indicates that the two genes were formed independently. The evolutionary pressure that has led to the fixation of the Hps with a longer alpha-chain is not known.

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Year:  2007        PMID: 17922076     DOI: 10.1007/s00239-007-9002-3

Source DB:  PubMed          Journal:  J Mol Evol        ISSN: 0022-2844            Impact factor:   2.395


  34 in total

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Authors:  Sergei L Kosakovsky Pond; Simon D W Frost
Journal:  Bioinformatics       Date:  2005-02-15       Impact factor: 6.937

2.  Effect of haptoglobin phenotypes on growth of Streptococcus pyogenes.

Authors:  J Delanghe; M Langlois; J Ouyang; G Claeys; M De Buyzere; B Wuyts
Journal:  Clin Chem Lab Med       Date:  1998-09       Impact factor: 3.694

3.  Haptoglobin evolution: polymeric forms of Hp in the Bovidae and Cervidae families.

Authors:  J C Travis; B G Sanders
Journal:  J Exp Zool       Date:  1972-04

4.  Structure-function analysis of the antioxidant properties of haptoglobin.

Authors:  M Melamed-Frank; O Lache; B I Enav; T Szafranek; N S Levy; R M Ricklis; A P Levy
Journal:  Blood       Date:  2001-12-15       Impact factor: 22.113

5.  Increased susceptibility in Hp knockout mice during acute hemolysis.

Authors:  S K Lim; H Kim; S K Lim; A bin Ali; Y K Lim; Y Wang; S M Chong; F Costantini; H Baumman
Journal:  Blood       Date:  1998-09-15       Impact factor: 22.113

6.  Haptoglobin 1-1 is associated with susceptibility to severe Plasmodium falciparum malaria.

Authors:  I K Quaye; F A Ekuban; B Q Goka; V Adabayeri; J A Kurtzhals; B Gyan; N A Ankrah; L Hviid; B D Akanmori
Journal:  Trans R Soc Trop Med Hyg       Date:  2000 Mar-Apr       Impact factor: 2.184

7.  The haptoglobin 2-2 genotype is associated with a reduced incidence of Plasmodium falciparum malaria in children on the coast of Kenya.

Authors:  Sarah H Atkinson; Tabitha W Mwangi; Sophie M Uyoga; Edna Ogada; Alex W Macharia; Kevin Marsh; Andrew M Prentice; Thomas N Williams
Journal:  Clin Infect Dis       Date:  2007-02-07       Impact factor: 9.079

8.  Haptoglobin genotypes are not associated with resistance to severe malaria in The Gambia.

Authors:  Christophe Aucan; Andrew J Walley; Brian M Greenwood; Adrian V S Hill
Journal:  Trans R Soc Trop Med Hyg       Date:  2002 May-Jun       Impact factor: 2.184

9.  Evolution of haptoglobin: comparison of complementary DNA encoding Hp alpha 1S and Hp alpha 2FS.

Authors:  J L Brune; F Yang; D R Barnett; B H Bowman
Journal:  Nucleic Acids Res       Date:  1984-06-11       Impact factor: 16.971

10.  Covalent structure of human haptoglobin: a serine protease homolog.

Authors:  A Kurosky; D R Barnett; T H Lee; B Touchstone; R E Hay; M S Arnott; B H Bowman; W M Fitch
Journal:  Proc Natl Acad Sci U S A       Date:  1980-06       Impact factor: 11.205

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  1 in total

1.  Haptoglobin Is a Divergent MASP Family Member That Neofunctionalized To Recycle Hemoglobin via CD163 in Mammals.

Authors:  Anthony K Redmond; Yuko Ohta; Michael F Criscitiello; Daniel J Macqueen; Martin F Flajnik; Helen Dooley
Journal:  J Immunol       Date:  2018-09-07       Impact factor: 5.422

  1 in total

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