Literature DB >> 6572010

Primary structures of bovine liver low molecular weight kininogen precursors and their two mRNAs.

H Nawa, N Kitamura, T Hirose, M Asai, S Inayama, S Nakanishi.   

Abstract

By using a mixture of synthetic oligodeoxyribonucleotides as a probe, cloned cDNA sequences specific for low molecular weight (LMW) kininogen have been isolated from a cDNA library of bovine liver mRNA sequences. Nucleotide sequence analyses of cloned cDNA inserts have revealed that bovine liver LMW kininogens are encoded by at least two very similar but distinct mRNAs. The corresponding amino acid sequences show that the LMW kininogen precursors of the two types, composed of 436 and 434 amino acid residues, both contain two internally homologous sequences in the amino-terminal portion between a signal peptide and a bradykinin moiety. The two mRNAs exhibit 15 nucleotide substitutions and 6 nucleotide deletions/additions in their protein-coding regions. The replacement of 13 amino acid residues and the deletions/additions of 2 amino acid residues in the two LMW kininogen precursors are all localized within the internally homologous regions, implying that these regions may be biologically significant in relation to the existence of two LMW kininogens. The nucleotide changes in the two mRNAs also occur in the limited portions that principally encode the internally homologous amino acid sequences. This suggests that the mRNAs are transcribed from the same gene to generate two LMW kininogen precursors differing only in the internally homologous sequences.

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Year:  1983        PMID: 6572010      PMCID: PMC393315          DOI: 10.1073/pnas.80.1.90

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  23 in total

1.  Bovine plasma HMW and LMW kininogens. Structural differences between heavy and light chains derived from the kinin-free proteins.

Authors:  H Kato; Y N Han; S Iwanaga; T Suzuki; M Komiya
Journal:  J Biochem       Date:  1976-12       Impact factor: 3.387

2.  Studies on the primary structure of bovine high-molecular-weight kininogen. Amino acid sequence of a fragment ("histidine-rich peptide") released by plasma kallikrein.

Authors:  Y N Han; M Komiya; S Iwanaga; T Suzuki
Journal:  J Biochem       Date:  1975-01-01       Impact factor: 3.387

3.  Primary structure of bovine plasma high-molecular-weight kininogen. The amino acid sequence of a glycopeptide portion (fragment 1) following the C-terminus ot the bradykinin moiety.

Authors:  Y N Han; H Kato; S Iwanaga; T Suzuki
Journal:  J Biochem       Date:  1976-06       Impact factor: 3.387

4.  Primary structure of bovine plasma low-molecular-weight kininogen. The complete amino acid sequence of COOH-terminal portion following the bradykinin moiety.

Authors:  H Kato; Y N HAN; S Iwanaga
Journal:  J Biochem       Date:  1977-08       Impact factor: 3.387

5.  The conversion of prothrombin to thrombin. IV. The function of the fragment 2 region during activation in the presence of factor V.

Authors:  C T Esmon; C M Jackson
Journal:  J Biol Chem       Date:  1974-12-25       Impact factor: 5.157

6.  A complementation analysis of the restriction and modification of DNA in Escherichia coli.

Authors:  H W Boyer; D Roulland-Dussoix
Journal:  J Mol Biol       Date:  1969-05-14       Impact factor: 5.469

7.  3' non-coding region sequences in eukaryotic messenger RNA.

Authors:  N J Proudfoot; G G Brownlee
Journal:  Nature       Date:  1976-09-16       Impact factor: 49.962

8.  Substrates for plasma kinin-forming enzymes in human, dog and rabbit plasmas.

Authors:  S Jacobsen
Journal:  Br J Pharmacol Chemother       Date:  1966-02

9.  Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose.

Authors:  H Aviv; P Leder
Journal:  Proc Natl Acad Sci U S A       Date:  1972-06       Impact factor: 11.205

10.  Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components.

Authors:  G Blobel; B Dobberstein
Journal:  J Cell Biol       Date:  1975-12       Impact factor: 10.539

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  10 in total

1.  Evolution of proteins of the cystatin superfamily.

Authors:  N D Rawlings; A J Barrett
Journal:  J Mol Evol       Date:  1990-01       Impact factor: 2.395

2.  Purification and characterization of kininogens from sheep plasma.

Authors:  Shahid P Baba; Sadaf Zehra; Bilqees Bano
Journal:  Protein J       Date:  2005-02       Impact factor: 2.371

Review 3.  Molecular biology of tissue kallikrein.

Authors:  R J MacDonald; H S Margolius; E G Erdös
Journal:  Biochem J       Date:  1988-07-15       Impact factor: 3.857

4.  Internally repeated sequences in ras gene products.

Authors:  T Hiwasa
Journal:  Biochem J       Date:  1988-09-01       Impact factor: 3.857

5.  High molecular weight kininogen is an inhibitor of platelet calpain.

Authors:  A H Schmaier; H Bradford; L D Silver; A Farber; C F Scott; D Schutsky; R W Colman
Journal:  J Clin Invest       Date:  1986-05       Impact factor: 14.808

Review 6.  Compilation of published signal sequences.

Authors:  M E Watson
Journal:  Nucleic Acids Res       Date:  1984-07-11       Impact factor: 16.971

7.  Cloning and sequence analysis of cDNA for rat angiotensinogen.

Authors:  H Ohkubo; R Kageyama; M Ujihara; T Hirose; S Inayama; S Nakanishi
Journal:  Proc Natl Acad Sci U S A       Date:  1983-04       Impact factor: 11.205

8.  Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases.

Authors:  G Salvesen; C Parkes; M Abrahamson; A Grubb; A J Barrett
Journal:  Biochem J       Date:  1986-03-01       Impact factor: 3.857

9.  General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding.

Authors:  T Hildmann; M Ebneth; H Peña-Cortés; J J Sánchez-Serrano; L Willmitzer; S Prat
Journal:  Plant Cell       Date:  1992-09       Impact factor: 11.277

10.  Analysis of the distribution of charged residues in the N-terminal region of signal sequences: implications for protein export in prokaryotic and eukaryotic cells.

Authors:  G von Heijne
Journal:  EMBO J       Date:  1984-10       Impact factor: 11.598

  10 in total

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