Characterization of cDNA coding for human factor XIIIa.

Grundmann, U.; Amann, Egon; Zettlmeissl, Gerd; Küpper, Hans

doi:10.1073/pnas.83.21.8024

Cited by 119 publications

(93 citation statements)

References 33 publications

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“…A comparison of the inferred amino acid sequence of guinea pig liver type II transglutaminase (13,14) with that of human factor XIIIa (10)(11)(12)35) revealed a conserved sequence of 8 amino acids at the active sites of these two enzymes. We reasoned that type I transglutaminase should also contain this sequence.…”

Section: Resultsmentioning

confidence: 99%

Regulation of type I (epidermal) transglutaminase mRNA levels during squamous differentiation: down regulation by retinoids.

Floyd¹,

Jetten²

1989

Mol. Cell. Biol.

114

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Section: Resultsmentioning

confidence: 99%

Regulation of type I (epidermal) transglutaminase mRNA levels during squamous differentiation: down regulation by retinoids.

Floyd¹,

Jetten²

1989

Mol. Cell. Biol.

114

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“…4, b) (24,26,27) and LTG (25), especially around their active sites. XIIIa, the final component in the coagulation pathway, plays an important role in the stabilization of fibrin clots by covalently crosslinking fibrin monomers through y-glutamyl-E-lysine bridges and by preventing proteolysis (35).…”

Section: Methodsmentioning

confidence: 99%

Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane.

Sung¹,

Chien²,

Chang³

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

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Protein 4.2 (P4.2) comprises -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 -77 and =80 kDa, respectively, and the authenticity was confimed by sequence identity with 46 amino acids of three cyanogen bromide-cleaved peptides of P4. Subcloning and Sequence Analysis. cDNA inserts from positive phage clones were subcloned into pBS(+) plasmids (Stratagene). Unidirectional deletion clones were generated by using BAL-31 exonuclease (13), and cDNA fragments were sequenced with T3 and T7 primers by the dideoxynucleotide chain-termination method (14). Sequence analysis and GenBank data base searches were performed by IBI Pustell sequence analysis software (International Biotechnologies). 5'-End Extension of cDNA. Three oligonucleotides were prepared in a technique based on the polymerase chain reaction (PCR) to synthesize the missing 5' sequence of the partial cDNA clone: pl was composed of nucleotides (nt) 7-23 of clone 7 (c.7); p2 was complementary to nt 36-52 of c.7 plus an EcoRI restriction site at its 5' end; p3 was composed of the EcoRI polylinker and the poly(dC) originally used for the first-strand cDNA synthesis when the library was constructed. The sequences of pl, p2, and p3 were, respectively, 5'-dTGAGGATGCTGTGTTCC-3', 5'-dTCGAAlJCGTACTC-CATGCGCTGAG-3', and 5'-dGCGGLAAlTCCCCCCCCCC-CCCC-3', with the EcoRI sites underlined. p2 and p3 were used as PCR primers, and the reticulocyte cDNA library (5 ,u with 106 phages per pl) was used as a template. The reaction product was electrophoresed and stained with ethidium bromide. The major band was excised and subcloned into pGEM 3zf plasmids (Promega). From >500 transformants, 24 colonies were randomly chosen to make minipreparations of plasmid DNA, of which 80%o were positive when hybridized with 32P-labeled pl. tTo whom reprint requests should be addressed. IThe sequences reported in this paper have been deposited in the GenBank data base (accession nos. M30646 and M30647). 955The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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“…The primary structure of human F XIII A has been elucidated from the amino acid sequence (22,23) and cDNA sequence obtained from the human placental library (24). F XIII A cDNA consists of 3,902 bases, which include 2,196 bases of coding region for 732 amino acids, 81 bases of 5', and 1,625 bases of 3' nontranslated regions (22)(23)(24).…”

Section: Introductionmentioning

confidence: 99%

Deficiency of coagulation factor XIII A subunit caused by the dinucleotide deletion at the 5' end of exon III.

Kamura¹,

Okamura²,

Murakawa³

et al. 1992

J. Clin. Invest.

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A congenital deficiency of the coagulation Factor XIII A subunit (F XIII A) is a rare autosomal recessive disorder that is characterized by a life-long bleeding tendency complicated by a difficulty in healing. Thus far, no molecular genetic analysis of this disorder has been reported. In this study, we demonstrate the molecular abnormalities in a family with this disorder. We performed Northern blot analysis of peripheral blood monocytes obtained from the propositus and found a 4-kb single band of F XIII A mRNA whose size was identical with that of normal subjects. Exons II-XV, which encode all the amino acids, were individually amplified by a polymerase chain reaction (PCR). All PCR products from the propositus had lengths indistinguishable from those of the wild type on agarose gel, suggesting that this defect results from either a point mutation or a short deletion/insertion. The sequencing of F XIII A cDNA from the propositus revealed a deletion of the dinucleotide AG within the AGAG repeat at the position of 210 to 213. Concerning the genomic sequence, a deletion of dinucleotide AG was also demonstrated in the intron B-exon III boundary. This deletion appeared to cause a frameshift mutation making a new stop codon shortly thereafter, and leading to a deficiency of plasma F XIII A. The heterozygosity of the F XIII A deficiency in the patient's offspring was documented by the nucleotide sequences of their exon III. (J. Clin. Invest. 1992. 90:315-319.)

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Characterization of cDNA coding for human factor XIIIa.

Cited by 119 publications

References 33 publications

Regulation of type I (epidermal) transglutaminase mRNA levels during squamous differentiation: down regulation by retinoids.

Regulation of type I (epidermal) transglutaminase mRNA levels during squamous differentiation: down regulation by retinoids.

Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane.

Deficiency of coagulation factor XIII A subunit caused by the dinucleotide deletion at the 5' end of exon III.

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