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Expression and characterization of C...

Haque, Aftabul.

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Expression and characterization of C-terminal domains of human complement protein factor H.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Expression and characterization of C-terminal domains of human complement protein factor H./
Author:	Haque, Aftabul.
Description:	103 p.
Notes:	Source: Masters Abstracts International, Volume: 42-01, page: 0236.
Contained By:	Masters Abstracts International42-01.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1415261

Expression and characterization of C-terminal domains of human complement protein factor H.
Haque, Aftabul.

Expression and characterization of C-terminal domains of human complement protein factor H. - 103 p.

Source: Masters Abstracts International, Volume: 42-01, page: 0236.

Thesis (M.S.)--Stephen F. Austin State University, 2003.

Factor H is a plasma protein that selectively regulates complement activation on host cells. Human factor H has 20 domains, among which the C-terminal domains are thought to play important roles in distinguishing between the self and non-self cells by binding with C3b and cell-surface polyanions. The C-terminal domains of human factor H were cloned and expressed in a eukaryotic expression system and their affinity for human C3 and its degradation products (C3b, iC3b, C3c and C3d) was determined. Four recombinant proteins, rH19-20, rH18-20, rH17-20 and rH16-20, bound C3b (<italic>K</italic>d's = 1.7 to 2.4 μM). Among the other C3 fragments, only iC3b and C3d showed binding to rH19-20 (<italic>K</italic>d's = 2.8 and 1.9 μM, respectively), whereas C3 and C3c showed no binding. The last C-terminal domain alone (rH20) showed no binding to any of the C3 fragments, but rH19 could not be expressed. Arginine at position 1215 of factor H was found recently to be a critical residue mutated in patients with inherited atypical hemolytic uremic syndrome (aHUS). A construct of rH19-20, where arginine 1215 in domain 20 was replaced with alanine (rH19-20R1215A) did not show any significant change in binding with C3b or C3d (<italic>K</italic>d's = 0.8 and 0.9 μM, respectively). This study demonstrates that the C-terminal C3b binding site on factor H is localized on domains 19–20 or on domain 19. This study also suggests that the pathogenesis of hemolytic uremic syndrome is not due to an altered binding interaction between the mutated C-terminal of factor H (rH19-20R1215A) and C3b, rather it may be due to an altered interaction with the host cell-surface polyanions.Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Expression and characterization of C-terminal domains of human complement protein factor H.
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100 1 $a Haque, Aftabul. $3 1945932
245 1 0 $a Expression and characterization of C-terminal domains of human complement protein factor H.
300 $a 103 p.
500 $a Source: Masters Abstracts International, Volume: 42-01, page: 0236.
500 $a Adviser: Michael K. Pangburn.
502 $a Thesis (M.S.)--Stephen F. Austin State University, 2003.
520 $a Factor H is a plasma protein that selectively regulates complement activation on host cells. Human factor H has 20 domains, among which the C-terminal domains are thought to play important roles in distinguishing between the self and non-self cells by binding with C3b and cell-surface polyanions. The C-terminal domains of human factor H were cloned and expressed in a eukaryotic expression system and their affinity for human C3 and its degradation products (C3b, iC3b, C3c and C3d) was determined. Four recombinant proteins, rH19-20, rH18-20, rH17-20 and rH16-20, bound C3b (<italic>K</italic>d's = 1.7 to 2.4 μM). Among the other C3 fragments, only iC3b and C3d showed binding to rH19-20 (<italic>K</italic>d's = 2.8 and 1.9 μM, respectively), whereas C3 and C3c showed no binding. The last C-terminal domain alone (rH20) showed no binding to any of the C3 fragments, but rH19 could not be expressed. Arginine at position 1215 of factor H was found recently to be a critical residue mutated in patients with inherited atypical hemolytic uremic syndrome (aHUS). A construct of rH19-20, where arginine 1215 in domain 20 was replaced with alanine (rH19-20R1215A) did not show any significant change in binding with C3b or C3d (<italic>K</italic>d's = 0.8 and 0.9 μM, respectively). This study demonstrates that the C-terminal C3b binding site on factor H is localized on domains 19–20 or on domain 19. This study also suggests that the pathogenesis of hemolytic uremic syndrome is not due to an altered binding interaction between the mutated C-terminal of factor H (rH19-20R1215A) and C3b, rather it may be due to an altered interaction with the host cell-surface polyanions.
590 $a School code: 6340.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Engineering, Biomedical. $3 1017684
650 4 $a Health Sciences, Immunology. $3 1017716
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791 $a M.S.
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856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1415261