Characterization of the human and mouse genes for the α subunit of type II prolyl 4-hydroxylase: Identification of a previously unknown alternatively spliced exon and its expression in various tissues

European Journal of Biochemistry

Volumn 268, Issue 20, 2001, Pages 5300-5309

  Nokelainen, Minna ^a   Nissi, Ritva ^a   Kukkola, Liisa ^a   Helaakoski, Tarja ^a   Myllyharju, Johanna ^a  

^a UNIVERSITY OF OULU   (Finland)

Author keywords

Collagen biosynthesis; Extracellular matrix; Isoenzyme; Prolyl 4 hydroxylase; Protein disulfide isomerase

Indexed keywords

AMINO ACID; COLLAGEN; COLLAGEN TYPE 11; COLLAGEN TYPE 2; COLLAGEN TYPE 9; ISOENZYME; MESSENGER RNA; NUCLEOTIDE; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; TATA BINDING PROTEIN; TRANSCRIPTION FACTOR;

ALPHA CHAIN; AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL GENETICS; ARTICLE; BETA CHAIN; BINDING SITE; CARTILAGE CELL; CATALYSIS; COLLAGEN SYNTHESIS; CONTROLLED STUDY; DNA FLANKING REGION; EXON; GENETIC CODE; HUMAN; HUMAN CELL; HUMAN GENETICS; INTRON; LEUKOCYTE; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; TATA BOX; TRANSLATION INITIATION;

ALTERNATIVE SPLICING; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; EXONS; GENE EXPRESSION PROFILING; HUMANS; INTRONS; MICE; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; PROCOLLAGEN-PROLINE DIOXYGENASE; PROMOTER REGIONS (GENETICS); PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; RNA SPLICE SITES; RNA, MESSENGER; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, NUCLEIC ACID; TRANSCRIPTION INITIATION SITE;

EID: 0034786387     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.0014-2956.2001.02464.x     Document Type: Article

References (23)

1. Collagens and collagen-related diseases
2. Prolyl 4-hydroxylases and their protein disulicde isomerase subunit
3. Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases
4. 2 tetramer
5. 2 tetramer with the protein disulfide-isomerase/β subunit
6. Structure and expression of the human gene for the α subunit of prolyl 4-hydroxylase. The two alternatively spliced types of mRNA correspond to two homologous exons the sequences of which are expressed in a variety of tissues
7. Molecular cloning of the α-subunit of human prolyl 4-hydroxylase: The complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts
8. Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide isomerase subunit synthesized in a baculovirus expression system
9. The novel type II prolyl 4-hydroxylase is the main enzyme form in chondrocytes and capillary endothelial cells, whereas the type I enzyme predominates in most cells
10. Prolyl 4-hydroxylase isoenzymes I and II have different expression patterns in several human tissues
11. DNA sequencing with chain-terminating inhibitors
12. Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes
13. Assignment of the gene coding for the α-subunit of prolyl 4-hydroxylase to human chromosome region 10q21.3-23.1
14. The order and transcriptional orientation of the human COL13A1 and P4HA genes on chromosome 10 long arm determined by high-resolution FISH
15. Transcriptional mechanisms of chondrocyte differentiation
16. One short well conserved region of Alu-sequences is involved in human gene rearrangements and has homology with prokaryotic chi
17. The partial tandem duplication of ALL1 (MLL) is consistently generated by Alu-mediated homologous recombination in acute myeloid leukemia
18. Structure and expression of the human lysyl hydroxylase gene (PLOD): Introns 9 and 16 contain Alu sequences at the sites of recombination in Ehlers-Danlos syndrome type VI patients
19. Duplication of seven exons in the lysyl hydroxylase gene is associated with longer forms of a repetitive sequence within the gene and is a common cause for the type VI variant of Ehlers-Danlos syndrome
20. Modification of vertebrate and algal prolyl 4-hydroxylases and vertebrate lysyl hydroxylase by diethyl-pyrocarbonate: Evidence for histidine residues in the catalytic site of 2-oxoglutarate coupled dioxygenases
21. Characterization of the iron-and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase