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The Inab phenotype: characterization of the membrane protein and complement regulatory defect.

Publication ,  Journal Article
Telen, MJ; Green, AM
Published in: Blood
July 1989

Recent demonstration that Cromer-related human blood group antigens reside on decay-accelerating factor (DAF) has led to identification of an apparent null phenotype (Inab) for erythrocyte DAF. This study examined expression of other phosphatidylinositol (PI)-anchored proteins by Inab erythrocytes and showed that the PI-linked membrane proteins acetylcholinesterase (AchE) and lymphocyte function-associated antigen-3 (LFA-3) are normally expressed by these cells. Furthermore, studies of the complement sensitivity of Inab RBCs demonstrated them to be abnormally complement sensitive, with an apparent defect in downregulation of C3 convertase activity. Thus, the Inab phenotype appears to represent an instance of hereditary erythrocyte DAF deficiency whose mechanism differs from that of paroxysmal nocturnal hemoglobinuria (PNH) and which is unassociated with clinically evident hemolytic disease.

Duke Scholars

Published In

Blood

ISSN

0006-4971

Publication Date

July 1989

Volume

74

Issue

1

Start / End Page

437 / 441

Location

United States

Related Subject Headings

  • Phosphatidylinositols
  • Membrane Proteins
  • Membrane Glycoproteins
  • Immunology
  • Humans
  • Erythrocyte Membrane
  • Erythrocyte Aging
  • Complement System Proteins
  • CD58 Antigens
  • CD55 Antigens
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Telen, M. J., and A. M. Green. “The Inab phenotype: characterization of the membrane protein and complement regulatory defect.Blood 74, no. 1 (July 1989): 437–41.
Telen, M. J., and A. M. Green. “The Inab phenotype: characterization of the membrane protein and complement regulatory defect.Blood, vol. 74, no. 1, July 1989, pp. 437–41.

Published In

Blood

ISSN

0006-4971

Publication Date

July 1989

Volume

74

Issue

1

Start / End Page

437 / 441

Location

United States

Related Subject Headings

  • Phosphatidylinositols
  • Membrane Proteins
  • Membrane Glycoproteins
  • Immunology
  • Humans
  • Erythrocyte Membrane
  • Erythrocyte Aging
  • Complement System Proteins
  • CD58 Antigens
  • CD55 Antigens