Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

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

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
; ;  [1]; ;  [2]; ; ; ;  [3]
  1. Univ. of California at San Diego, La Jolla (USA)
  2. Princeton Univ., NJ (USA)
  3. Albert Einstein College of Medicine/Montefiore Medical Center, Bronx, NY (USA)

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.

OSTI ID:
6719299
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 87:3; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English

Similar Records

Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4. 2
Journal Article · Sun Dec 31 23:00:00 EST 1989 · Proceedings of the National Academy of Sciences of the United States of America; (USA) · OSTI ID:6700166

Organization of the gene for human erythrocyte membrane protein 4. 2: Structural similarities with the gene for the a subunit of factor XIII
Journal Article · Sat Jun 01 00:00:00 EDT 1991 · Proceedings of the National Academy of Sciences of the United States of America; (United States) · OSTI ID:5933793

Primary structure of keratinocyte transglutaminase
Journal Article · Fri Nov 30 23:00:00 EST 1990 · Proceedings of the National Academy of Sciences of the United States of America; (United States) · OSTI ID:5044523