Cloning and sequencing of cDNAs encoding plasma alpha-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of alpha-macroglobulin family.

Cloning and sequencing of cDNAs encoding plasma alpha-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of alpha-macroglobulin family. Research Abstract Details 

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Cloning and sequencing of cDNAs encoding plasma alpha-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of alpha-macroglobulin family. Abstract Text:

H Iwasaki,Y Suzuki,H Sinohara,

Several clones encoding plasma alpha-macroglobulin and murinoglobulin were isolated from guinea pig liver cDNA library and sequenced. The clones for alpha-macroglobulin contained overlapping sequences which together spanned a stretch of 4,546 nucleotides with one open reading frame coding for 1,476 amino acid residues. The clones for murinoglobulin contained overlapping sequences which together spanned a stretch of 4,578 nucleotides with one open reading frame coding for 1,464 amino acid residues. The phylogenetic analyses of 11 proteins of the alpha-macroglobulin family revealed that the mammalian tetrameric alpha-macroglobulins consist of two main branches: alpha M-1 subfamily (rat alpha 1- and mouse alpha-macroglobulins) and alpha M-2 subfamily (human alpha 2-, rat alpha 2-, and guinea pig alpha-macroglobulins). This dichotomy is in good accordance with their immunological, chemical, and physicochemical properties, and indicates that guinea pig alpha-macroglobulin is orthologous to human and rat alpha 2-macroglobulins but paralogous to rat alpha 1- and mouse alpha-macroglobulins. The divergence of the two subfamilies was a phylogenetically ancient event which occurred around the separation of metatherians and eutherians. The genes of the two subfamilies have been maintained in the rat, but either one became extinct in the mouse, guinea pig, or human. The tree also shows that guinea pig murinoglobulin forms one clade with mouse and rat murinoglobulins (alpha 1-inhibitor 3) prior to joining the alpha M-2 lineage, and suggests that murinoglobulin is not a primitive form of tetrameric alpha-macroglobulin, but rather has evolved under selective pressure which is different from that of the tetrameric paralogues.

Cloning and sequencing of cDNAs encoding plasma alpha-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of alpha-macroglobulin family. Publishing Authors By Initials

H Iwasaki,Y Suzuki,H Sinohara,

For similar proteins: blood proteins: acute-phase proteins: alpha-macroglobulins research abstracts see: proteins: blood proteins: acute-phase proteins: alpha-macroglobulins research

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Cloning and sequencing of cDNAs encoding plasma alpha-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of alpha-macroglobulin family. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 120

Page Numbers: 1167-75

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1996

Cloning and sequencing of cDNAs encoding plasma alpha-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of alpha-macroglobulin family. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Cloning and sequencing of cDNAs encoding plasma alpha-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of alpha-macroglobulin family. Keywords Mesh Terms:

KEYWORDS: alpha-Macroglobulins

MESH TERMS: genetics

Chemical & Substance for Abstract: Cloning and sequencing of cDNAs encoding plasma alpha-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of alpha-macroglobulin family. Information

Substance Name: murinoglobulin

Registry Number: 0

Grant and Affiliation Information for Cloning and sequencing of cDNAs encoding plasma alpha-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of alpha-macroglobulin family.

AFFILIATION: Department of Biochemistry, Kinki University School of Medicine, Osaka.

Country: JAPAN

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MEDLINETA: J Biochem

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ACCESSION NUMBER: D84339

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