Molecular cloning of human protein 4. 2: A major component of the erythrocyte membrane

Protein 4.2 (P4.2) comprises {approx}5% of the protein mass of human erythrocyte (RBC) membranes. Anemia occurs in patients with RBCs deficient in P4.2, suggesting a role for this protein in maintaining RBC stability and integrity. The authors now report the molecular cloning and characterization of...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1990-02, Vol.87:3
Main Authors: Sung, L.A., Chien, Shu, Lambert, K., Chang, Longsheng, Bliss, S.A., Bouhassira, E.E., Nagel, R.L., Schwartz, R.S., Rybicki, A.C.
Format: Article
Language:English
Subjects:
AMINO ACID SEQUENCE
ANEMIAS
ANIMALS
BASIC BIOLOGICAL SCIENCES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BLOOD COAGULATION FACTORS
BODY FLUIDS
CELL CONSTITUENTS
CELL MEMBRANES
CLONING
COAGULANTS
DAYS LIVING RADIOISOTOPES
DISEASES
DNA
DNA HYBRIDIZATION
DNA SEQUENCING
DNA-CLONING
DRUGS
ERYTHROCYTES
GUINEA PIGS
HEMATOLOGIC AGENTS
HEMIC DISEASES
HYBRIDIZATION
ISOTOPES
LIGHT NUCLEI
MAMMALS
MATERIALS
MEMBRANES
MOLECULAR STRUCTURE
NUCLEI
NUCLEIC ACIDS
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PATIENTS
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PROTEINS
RADIOISOTOPES
RECOMBINANT DNA
RODENTS
STRUCTURAL CHEMICAL ANALYSIS
SYMPTOMS
VERTEBRATES 550201 > Biochemistry-- Tracer Techniques
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Description
Summary:Protein 4.2 (P4.2) comprises {approx}5% of the protein mass of human erythrocyte (RBC) membranes. Anemia occurs in patients with RBCs deficient in P4.2, suggesting a role for this protein in maintaining RBC stability and integrity. The authors now report the molecular cloning and characterization of human RBC P4.2 cDNAs. By immunoscreening a human reticulocyte cDNA library and by using the polymerase chain reaction, two cDNA sequences of 2.4 and 2.5 kilobases (kb) were obtained. These cDNAs differ only by a 90-base-air insert in the longer isoform located three codons downstream from the putative initiation site. The 2.4- and 2.5-kb cDNAs predict proteins of {approx}77 and {approx}80 kDa, respectively, and the authenticity was confirmed by sequence identity with 46 amino acids of three cyanogen bromide-cleaved peptides of P4.2. Northern blot analysis detected a major 2.4-kb RNA species in reticulocytes. Isolation of two P4.2 cDNAs implies existence of specific regulation of P4.2 expression in human RBCs. Human RBC P4.2 has significant homology with human factor XIII subunit a and guinea pig liver transglutaminase. Sequence alignment of P4.2 with these two transglutaminases, however, revealed that P4.2 lacks the critical cysteine residue required for the enzymatic crosslinking of substrates.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.87.3.955