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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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| Published in: | Proceedings of the National Academy of Sciences - PNAS 1990-02, Vol.87:3 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 87:3 |
| creator | Sung, L.A. Chien, Shu Lambert, K. Chang, Longsheng Bliss, S.A. Bouhassira, E.E. Nagel, R.L. Schwartz, R.S. Rybicki, A.C. |
| description | 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. |
| doi_str_mv | 10.1073/pnas.87.3.955 |
| format | article |
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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.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.87.3.955</identifier><language>eng</language><publisher>United States</publisher><subject>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</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1990-02, Vol.87:3</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.osti.gov/biblio/6719299$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Sung, L.A.</creatorcontrib><creatorcontrib>Chien, Shu</creatorcontrib><creatorcontrib>Lambert, K.</creatorcontrib><creatorcontrib>Chang, Longsheng</creatorcontrib><creatorcontrib>Bliss, S.A.</creatorcontrib><creatorcontrib>Bouhassira, E.E.</creatorcontrib><creatorcontrib>Nagel, R.L.</creatorcontrib><creatorcontrib>Schwartz, R.S.</creatorcontrib><creatorcontrib>Rybicki, A.C.</creatorcontrib><title>Molecular cloning of human protein 4. 2: A major component of the erythrocyte membrane</title><title>Proceedings of the National Academy of Sciences - PNAS</title><description>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.</description><subject>AMINO ACID SEQUENCE</subject><subject>ANEMIAS</subject><subject>ANIMALS</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BETA-MINUS DECAY RADIOISOTOPES</subject><subject>BIOLOGICAL MATERIALS</subject><subject>BLOOD</subject><subject>BLOOD CELLS</subject><subject>BLOOD COAGULATION FACTORS</subject><subject>BODY FLUIDS</subject><subject>CELL CONSTITUENTS</subject><subject>CELL MEMBRANES</subject><subject>CLONING</subject><subject>COAGULANTS</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>DISEASES</subject><subject>DNA</subject><subject>DNA HYBRIDIZATION</subject><subject>DNA SEQUENCING</subject><subject>DNA-CLONING</subject><subject>DRUGS</subject><subject>ERYTHROCYTES</subject><subject>GUINEA PIGS</subject><subject>HEMATOLOGIC AGENTS</subject><subject>HEMIC DISEASES</subject><subject>HYBRIDIZATION</subject><subject>ISOTOPES</subject><subject>LIGHT NUCLEI</subject><subject>MAMMALS</subject><subject>MATERIALS</subject><subject>MEMBRANES</subject><subject>MOLECULAR STRUCTURE</subject><subject>NUCLEI</subject><subject>NUCLEIC ACIDS</subject><subject>ODD-ODD NUCLEI</subject><subject>ORGANIC COMPOUNDS</subject><subject>PATIENTS</subject><subject>PHOSPHORUS 32</subject><subject>PHOSPHORUS ISOTOPES</subject><subject>PROTEINS</subject><subject>RADIOISOTOPES</subject><subject>RECOMBINANT DNA</subject><subject>RODENTS</subject><subject>STRUCTURAL CHEMICAL ANALYSIS</subject><subject>SYMPTOMS</subject><subject>VERTEBRATES 550201 -- Biochemistry-- Tracer Techniques</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><recordid>eNqNyj1PwzAQAFCrAqkBOnY_scec89HE3RACdWGrulbGujap4rvIdof-e0DiBzC95Sm1NqgNdvXLzC7pvtO1tm27UIVBa8pNY_FOFYhVV_ZN1SzVQ0oXRLRtj4U6fMpE_jq5CH4SHvkMcoLhGhzDHCXTyNBoqLbwCsFd5KdJmIWJ82_MAwHFWx6i-FsmCBS-omN6UvcnNyVa_fmonj_e92-7UlIej8mPmfzghZl8Pm46Yytr63-lb6_QRto</recordid><startdate>19900201</startdate><enddate>19900201</enddate><creator>Sung, L.A.</creator><creator>Chien, Shu</creator><creator>Lambert, K.</creator><creator>Chang, Longsheng</creator><creator>Bliss, S.A.</creator><creator>Bouhassira, E.E.</creator><creator>Nagel, R.L.</creator><creator>Schwartz, R.S.</creator><creator>Rybicki, A.C.</creator><scope>OTOTI</scope></search><sort><creationdate>19900201</creationdate><title>Molecular cloning of human protein 4. 2: A major component of the erythrocyte membrane</title><author>Sung, L.A. ; Chien, Shu ; Lambert, K. ; Chang, Longsheng ; Bliss, S.A. ; Bouhassira, E.E. ; Nagel, R.L. ; Schwartz, R.S. ; Rybicki, A.C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-osti_scitechconnect_67192993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>AMINO ACID SEQUENCE</topic><topic>ANEMIAS</topic><topic>ANIMALS</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BETA-MINUS DECAY RADIOISOTOPES</topic><topic>BIOLOGICAL MATERIALS</topic><topic>BLOOD</topic><topic>BLOOD CELLS</topic><topic>BLOOD COAGULATION FACTORS</topic><topic>BODY FLUIDS</topic><topic>CELL CONSTITUENTS</topic><topic>CELL MEMBRANES</topic><topic>CLONING</topic><topic>COAGULANTS</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>DISEASES</topic><topic>DNA</topic><topic>DNA HYBRIDIZATION</topic><topic>DNA SEQUENCING</topic><topic>DNA-CLONING</topic><topic>DRUGS</topic><topic>ERYTHROCYTES</topic><topic>GUINEA PIGS</topic><topic>HEMATOLOGIC AGENTS</topic><topic>HEMIC DISEASES</topic><topic>HYBRIDIZATION</topic><topic>ISOTOPES</topic><topic>LIGHT NUCLEI</topic><topic>MAMMALS</topic><topic>MATERIALS</topic><topic>MEMBRANES</topic><topic>MOLECULAR STRUCTURE</topic><topic>NUCLEI</topic><topic>NUCLEIC ACIDS</topic><topic>ODD-ODD NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>PATIENTS</topic><topic>PHOSPHORUS 32</topic><topic>PHOSPHORUS ISOTOPES</topic><topic>PROTEINS</topic><topic>RADIOISOTOPES</topic><topic>RECOMBINANT DNA</topic><topic>RODENTS</topic><topic>STRUCTURAL CHEMICAL ANALYSIS</topic><topic>SYMPTOMS</topic><topic>VERTEBRATES 550201 -- Biochemistry-- Tracer Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sung, L.A.</creatorcontrib><creatorcontrib>Chien, Shu</creatorcontrib><creatorcontrib>Lambert, K.</creatorcontrib><creatorcontrib>Chang, Longsheng</creatorcontrib><creatorcontrib>Bliss, S.A.</creatorcontrib><creatorcontrib>Bouhassira, E.E.</creatorcontrib><creatorcontrib>Nagel, R.L.</creatorcontrib><creatorcontrib>Schwartz, R.S.</creatorcontrib><creatorcontrib>Rybicki, A.C.</creatorcontrib><collection>OSTI.GOV</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sung, L.A.</au><au>Chien, Shu</au><au>Lambert, K.</au><au>Chang, Longsheng</au><au>Bliss, S.A.</au><au>Bouhassira, E.E.</au><au>Nagel, R.L.</au><au>Schwartz, R.S.</au><au>Rybicki, A.C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning of human protein 4. 2: A major component of the erythrocyte membrane</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><date>1990-02-01</date><risdate>1990</risdate><volume>87:3</volume><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>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.</abstract><cop>United States</cop><doi>10.1073/pnas.87.3.955</doi></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1990-02, Vol.87:3 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_osti_scitechconnect_6719299 |
| source | PubMed Central (Open Access); JSTOR Archival Journals and Primary Sources Collection |
| 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 |
| title | Molecular cloning of human protein 4. 2: A major component of the erythrocyte membrane |
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