ArticleProceedings of the National Academy of Sciences of the United States of America1990
Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 66 citations in OpenAlex.
- Transglutaminase-mediated remodeling of the human erythrocyte membrane skeleton: relevance for erythrocyte diseases with shortened cell lifespan.Advances in enzymology and related areas of molecular biology · 2011Review
- Interactions of recombinant mouse erythrocyte transglutaminase with membrane skeletal proteins.The Journal of membrane biology · 2007Article
- Associations of protein 4.2 with band 3 and ankyrin.Molecular and cellular biochemistry · 2006Article
- Mapping of a spectrin-binding domain of human erythrocyte membrane protein 4.2.The Biochemical journal · 2002Article
- Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2.The Biochemical journal · 1999Article
- Molecular basis of bovine red-cell protein 4.2 polymorphism in Japanese black cattle.The Biochemical journal · 1998Article
- Association of a transglutaminase-related antigen with intermediate filaments.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Identification of a band-3 binding site near the N-terminus of erythrocyte membrane protein 4.2.The Biochemical journal · 1995Article
- Molecular cloning of mouse erythrocyte protein 4.2: a membrane protein with strong homology with the transglutaminase supergene family.Mammalian genome : official journal of the International Mammalian Genome Society · 1994Article
- An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells.The Journal of clinical investigation · 1993Article
- Cloning and expression of chicken erythrocyte transglutaminase.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- Organization and evolution of the human epidermal keratinocyte transglutaminase I gene.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- The gene for human erythrocyte protein 4.2 maps to chromosome 15q15.American journal of human genetics · 1992Article
- Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Primary structure of keratinocyte transglutaminase.Proceedings of the National Academy of Sciences of the United States of America · 1990Article
- New nucleotide sequence data on the EMBL File Server.Nucleic acids research · 1990Article
- Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2.Proceedings of the National Academy of Sciences of the United States of America · 1990Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Protein 4.2 (P4.2) comprises approximately 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. We 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-pair 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 approximately 77 and approximately 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.
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