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PMID: 10852913 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis.

The Journal of biological chemistry ·Vol. 275 ·No. 33 ·2000-08-18 ·Pages 25641-51

Liu Z, Chen Y, Mo R, Hui C, Cheng JF, Mohandas N, Huang CH

Abstract

In mammals, the Rh family includes the variable Rh polypeptides and invariant RhAG glycoprotein. These polytopic proteins are confined to the erythroid lineage and are assembled into a multisubunit complex essential for Rh antigen expression and plasma membrane integrity. Here, we report the characterization of RhCG and Rhcg, a pair of novel Rh homologues present in human and mouse nonerythroid tissues. Despite sharing a notable similarity to the erythroid forms, including the 12-transmembrane topological fold, the RHCG/Rhcg pair is distinct in chromosome location, genomic organization, promoter structure, and tissue-specific expression. RHCG and Rhcg map at 15q25 of human chromosome 15 and the long arm of mouse chromosome 7, respectively, each having 11 exons and a CpG-rich promoter. Northern blots detected kidney and testis as the major organs of RHCG or Rhcg expression. In situ hybridization revealed strong expression of Rhcg in the kidney collecting tubules and testis seminiferous tubules. Confocal imaging of transiently expressed green fluorescence protein fusion proteins localized RhCG exclusively to the plasma membrane, a distribution confirmed by cellular fractionation and Western blot analysis. In vitro translation and ex vivo expression showed that RhCG carries a complex N-glycan, probably at the (48)NLS(50) sequon of exoloop 1. These results pinpoint RhCG and Rhcg as novel polytopic membrane glycoproteins that may function as epithelial transporters maintaining normal homeostatic conditions in kidney and testis.

MeSH Terms
Amidohydrolases/metabolism Amino Acid Sequence Animals Base Sequence Blood Proteins Cation Transport Proteins Cell Line Cell Membrane/metabolism Chromosome Mapping Chromosomes, Human, Pair 15 DNA, Complementary/metabolism Exons Genetic Linkage Glycosylation HeLa Cells Humans In Situ Hybridization, Fluorescence Introns Kidney/metabolism Male Membrane Glycoproteins/biosynthesis,chemistry,genetics Mice Molecular Sequence Data Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Phylogeny Protein Biosynthesis Protein Structure, Secondary Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid Testis/metabolism Tissue Distribution Transcription, Genetic
Chemicals
Blood Proteins Cation Transport Proteins DNA, Complementary Membrane Glycoproteins RHAG protein, human RHCG protein, human Rhag protein, mouse Rhcg protein, mouse Amidohydrolases Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Liu Z
Laboratory of Biochemistry and Molecular Genetics, Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021, USA.
Chen Y
Mo R
Hui C
Cheng J F
Mohandas N
Huang C H
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2000-08-18
Pages
25641-51
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NHLBI NIH HHS · HL54459 · United States
Databases
GENBANK
AF183390, AF183391, AF193807, AF193808, AF193809, AF193810, AF193811, AF193812, AF209468, AF219981, AF219986, AF238372, AF238377
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