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Bovine C4b binding protein. Molecular cloning of the alpha- and beta-chains provides structural background for lack of complex formation with protein S

Hillarp, Andreas LU ; Thern, Anette LU and Dahlbäck, Björn LU (1994) In Journal of immunology 153(9). p.4190-4199
Abstract

C4b binding protein (C4BP) regulates the complement system. It also interacts with anticoagulant protein S and with serum amyloid P component. Human C4BP is composed of seven identical 70-kDa alpha-chains and one 45-kDa beta-chain. The binding site for C4b is located on the alpha-chain, whereas the beta-chain binds protein S. Nothing is known about the structure and function of bovine C4BP. No complexed form of protein S was detected by using a gel filtration chromatography system combined with Western blotting. Bovine cDNA clones encoding the C4BP alpha- and beta-chains were isolated from a bovine liver cDNA library. Three overlapping alpha-chain clones predicted a 562-amino acid residues-long mature polypeptide. The overall amino acid... (More)

C4b binding protein (C4BP) regulates the complement system. It also interacts with anticoagulant protein S and with serum amyloid P component. Human C4BP is composed of seven identical 70-kDa alpha-chains and one 45-kDa beta-chain. The binding site for C4b is located on the alpha-chain, whereas the beta-chain binds protein S. Nothing is known about the structure and function of bovine C4BP. No complexed form of protein S was detected by using a gel filtration chromatography system combined with Western blotting. Bovine cDNA clones encoding the C4BP alpha- and beta-chains were isolated from a bovine liver cDNA library. Three overlapping alpha-chain clones predicted a 562-amino acid residues-long mature polypeptide. The overall amino acid sequence similarity with the human alpha-chain was 61%. Like its human counterpart, the bovine alpha-chain is composed of eight contiguous short consensus repeat units, each of approximately 60 amino acid residues, and a carboxyl-terminal nonrepeat region. One bovine beta-chain clone was found and characterized. It predicted a mature bovine beta-chain of 181 amino acid residues. The identity with the human beta-chain was 65% at the amino acid level. A noteworthy difference between bovine and human beta-chains was that the bovine beta-chain only contained two short consensus repeats compared with three in human beta-chain. Sequence alignment indicates that the region corresponding to residues 1-60 (repeat 1) in the human beta-chain is absent in the homologous bovine polypeptide. Because the short consensus repeats of the human beta-chain contain the binding site for protein S, the lack of one repeat unit in the bovine beta-chain may provide a clue to the lack of complex formation between C4BP and protein S in bovine plasma.

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Contribution to journal
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published
subject
keywords
Amino Acid Sequence, Animals, Base Sequence, Blotting, Western, Carrier Proteins/chemistry, Cattle, Chromatography, Gel, Cloning, Molecular, Humans, Integrin alphaXbeta2, Molecular Sequence Data, Polymerase Chain Reaction, Protein Binding, Protein S/metabolism, Sequence Homology, Amino Acid
in
Journal of immunology
volume
153
issue
9
pages
4190 - 4199
publisher
American Association of Immunologists
external identifiers
  • scopus:0028097042
  • pmid:7930621
ISSN
0022-1767
language
English
LU publication?
yes
id
c6b80807-cf90-4724-8c95-7fe6b72bd18e
alternative location
https://www.jimmunol.org/content/153/9/4190.long
date added to LUP
2022-08-29 10:32:12
date last changed
2024-01-03 15:55:53
@article{c6b80807-cf90-4724-8c95-7fe6b72bd18e,
  abstract     = {{<p>C4b binding protein (C4BP) regulates the complement system. It also interacts with anticoagulant protein S and with serum amyloid P component. Human C4BP is composed of seven identical 70-kDa alpha-chains and one 45-kDa beta-chain. The binding site for C4b is located on the alpha-chain, whereas the beta-chain binds protein S. Nothing is known about the structure and function of bovine C4BP. No complexed form of protein S was detected by using a gel filtration chromatography system combined with Western blotting. Bovine cDNA clones encoding the C4BP alpha- and beta-chains were isolated from a bovine liver cDNA library. Three overlapping alpha-chain clones predicted a 562-amino acid residues-long mature polypeptide. The overall amino acid sequence similarity with the human alpha-chain was 61%. Like its human counterpart, the bovine alpha-chain is composed of eight contiguous short consensus repeat units, each of approximately 60 amino acid residues, and a carboxyl-terminal nonrepeat region. One bovine beta-chain clone was found and characterized. It predicted a mature bovine beta-chain of 181 amino acid residues. The identity with the human beta-chain was 65% at the amino acid level. A noteworthy difference between bovine and human beta-chains was that the bovine beta-chain only contained two short consensus repeats compared with three in human beta-chain. Sequence alignment indicates that the region corresponding to residues 1-60 (repeat 1) in the human beta-chain is absent in the homologous bovine polypeptide. Because the short consensus repeats of the human beta-chain contain the binding site for protein S, the lack of one repeat unit in the bovine beta-chain may provide a clue to the lack of complex formation between C4BP and protein S in bovine plasma.</p>}},
  author       = {{Hillarp, Andreas and Thern, Anette and Dahlbäck, Björn}},
  issn         = {{0022-1767}},
  keywords     = {{Amino Acid Sequence; Animals; Base Sequence; Blotting, Western; Carrier Proteins/chemistry; Cattle; Chromatography, Gel; Cloning, Molecular; Humans; Integrin alphaXbeta2; Molecular Sequence Data; Polymerase Chain Reaction; Protein Binding; Protein S/metabolism; Sequence Homology, Amino Acid}},
  language     = {{eng}},
  month        = {{11}},
  number       = {{9}},
  pages        = {{4190--4199}},
  publisher    = {{American Association of Immunologists}},
  series       = {{Journal of immunology}},
  title        = {{Bovine C4b binding protein. Molecular cloning of the alpha- and beta-chains provides structural background for lack of complex formation with protein S}},
  url          = {{https://www.jimmunol.org/content/153/9/4190.long}},
  volume       = {{153}},
  year         = {{1994}},
}