Biochemistry of the erythrocyte Rh polypeptides: A review

Peter C Agre, B. L. Smith, S. Hartel-Schenk

Research output: Contribution to journalArticle

Abstract

The clinically important Rh blood group system is complex, consisting of multiple distinct antigens. Despite clinical recognition for over 50 years, the Rh blood group antigens have remained poorly understood on a molecular level until the recent identification and characterization of the ''Rh polypeptides,'' the core structural proteins of the Rh antigens. This group of erythrocyte membrane proteins of molecular weight 30,000-35,000 daltons was first recognized by employing Rh-specific antibodies to immunoprecipitate radiolabeled components of erythrocyte membranes. By using antibodies specific for the Rh D, c, and E antigens, a series of highly related non-identical proteins were immunoprecipitated, indicating that the Rh antigens are composed of multiple related proteins. The Rh polypeptides have been purified and characterized, and they were found to have several unusual biochemical characteristics. The Rh polypeptides penetrate the membrane bilayer; they are linked to the underlying membrane skeleton; they are covalently fatty acid acylated with palmitate. While the Rh antigenic reactivity is unique to human erythrocytes, the Rh polypeptides have been isolated from erythrocytes of diverse species and are thought to be fundamental components of all mammalian erythrocyte membranes. The functional role of the Rh polypeptides remains undefined, but a role in the organization of membrane phospholipid is suspected.

Original languageEnglish (US)
Pages (from-to)461-467
Number of pages7
JournalYale Journal of Biology and Medicine
Volume63
Issue number5
StatePublished - 1990

Fingerprint

Biochemistry
Erythrocytes
Membranes
Erythrocyte Membrane
Peptides
Antigens
Blood Group Antigens
Dilatation and Curettage
Proteins
Antibodies
Palmitates
Skeleton
Phospholipids
Membrane Proteins
Fatty Acids
Molecular Weight
Molecular weight

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Biochemistry of the erythrocyte Rh polypeptides : A review. / Agre, Peter C; Smith, B. L.; Hartel-Schenk, S.

In: Yale Journal of Biology and Medicine, Vol. 63, No. 5, 1990, p. 461-467.

Research output: Contribution to journalArticle

Agre, PC, Smith, BL & Hartel-Schenk, S 1990, 'Biochemistry of the erythrocyte Rh polypeptides: A review', Yale Journal of Biology and Medicine, vol. 63, no. 5, pp. 461-467.
Agre, Peter C ; Smith, B. L. ; Hartel-Schenk, S. / Biochemistry of the erythrocyte Rh polypeptides : A review. In: Yale Journal of Biology and Medicine. 1990 ; Vol. 63, No. 5. pp. 461-467.
@article{73a1618b4da54908bbfaa3603302cc8b,
title = "Biochemistry of the erythrocyte Rh polypeptides: A review",
abstract = "The clinically important Rh blood group system is complex, consisting of multiple distinct antigens. Despite clinical recognition for over 50 years, the Rh blood group antigens have remained poorly understood on a molecular level until the recent identification and characterization of the ''Rh polypeptides,'' the core structural proteins of the Rh antigens. This group of erythrocyte membrane proteins of molecular weight 30,000-35,000 daltons was first recognized by employing Rh-specific antibodies to immunoprecipitate radiolabeled components of erythrocyte membranes. By using antibodies specific for the Rh D, c, and E antigens, a series of highly related non-identical proteins were immunoprecipitated, indicating that the Rh antigens are composed of multiple related proteins. The Rh polypeptides have been purified and characterized, and they were found to have several unusual biochemical characteristics. The Rh polypeptides penetrate the membrane bilayer; they are linked to the underlying membrane skeleton; they are covalently fatty acid acylated with palmitate. While the Rh antigenic reactivity is unique to human erythrocytes, the Rh polypeptides have been isolated from erythrocytes of diverse species and are thought to be fundamental components of all mammalian erythrocyte membranes. The functional role of the Rh polypeptides remains undefined, but a role in the organization of membrane phospholipid is suspected.",
author = "Agre, {Peter C} and Smith, {B. L.} and S. Hartel-Schenk",
year = "1990",
language = "English (US)",
volume = "63",
pages = "461--467",
journal = "Yale Journal of Biology and Medicine",
issn = "0044-0086",
publisher = "Yale Journal of Biology and Medicine Inc.",
number = "5",

}

TY - JOUR

T1 - Biochemistry of the erythrocyte Rh polypeptides

T2 - A review

AU - Agre, Peter C

AU - Smith, B. L.

AU - Hartel-Schenk, S.

PY - 1990

Y1 - 1990

N2 - The clinically important Rh blood group system is complex, consisting of multiple distinct antigens. Despite clinical recognition for over 50 years, the Rh blood group antigens have remained poorly understood on a molecular level until the recent identification and characterization of the ''Rh polypeptides,'' the core structural proteins of the Rh antigens. This group of erythrocyte membrane proteins of molecular weight 30,000-35,000 daltons was first recognized by employing Rh-specific antibodies to immunoprecipitate radiolabeled components of erythrocyte membranes. By using antibodies specific for the Rh D, c, and E antigens, a series of highly related non-identical proteins were immunoprecipitated, indicating that the Rh antigens are composed of multiple related proteins. The Rh polypeptides have been purified and characterized, and they were found to have several unusual biochemical characteristics. The Rh polypeptides penetrate the membrane bilayer; they are linked to the underlying membrane skeleton; they are covalently fatty acid acylated with palmitate. While the Rh antigenic reactivity is unique to human erythrocytes, the Rh polypeptides have been isolated from erythrocytes of diverse species and are thought to be fundamental components of all mammalian erythrocyte membranes. The functional role of the Rh polypeptides remains undefined, but a role in the organization of membrane phospholipid is suspected.

AB - The clinically important Rh blood group system is complex, consisting of multiple distinct antigens. Despite clinical recognition for over 50 years, the Rh blood group antigens have remained poorly understood on a molecular level until the recent identification and characterization of the ''Rh polypeptides,'' the core structural proteins of the Rh antigens. This group of erythrocyte membrane proteins of molecular weight 30,000-35,000 daltons was first recognized by employing Rh-specific antibodies to immunoprecipitate radiolabeled components of erythrocyte membranes. By using antibodies specific for the Rh D, c, and E antigens, a series of highly related non-identical proteins were immunoprecipitated, indicating that the Rh antigens are composed of multiple related proteins. The Rh polypeptides have been purified and characterized, and they were found to have several unusual biochemical characteristics. The Rh polypeptides penetrate the membrane bilayer; they are linked to the underlying membrane skeleton; they are covalently fatty acid acylated with palmitate. While the Rh antigenic reactivity is unique to human erythrocytes, the Rh polypeptides have been isolated from erythrocytes of diverse species and are thought to be fundamental components of all mammalian erythrocyte membranes. The functional role of the Rh polypeptides remains undefined, but a role in the organization of membrane phospholipid is suspected.

UR - http://www.scopus.com/inward/record.url?scp=0025648334&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025648334&partnerID=8YFLogxK

M3 - Article

C2 - 2127333

AN - SCOPUS:0025648334

VL - 63

SP - 461

EP - 467

JO - Yale Journal of Biology and Medicine

JF - Yale Journal of Biology and Medicine

SN - 0044-0086

IS - 5

ER -