Co-expression of collagens II and XI and alternative splicing of exon 2 of collagen II in several developing human tissues.
Northern analyses, RNAase protection assays and in situ hybridizations were used to study the expression of the mRNA for the alpha 2 chain of collagen XI and the two different mRNAs generated from the collagen II gene through alternative splicing of exon 2 in several different tissues of 15-19-week-old fetuses. The highest expression levels of procollagen alpha 2(XI) and alpha 1(II) mRNAs were detected in cartilage, but, using long exposure times, Northern hybridization revealed the presence of the approximately 5.3 kb procollagen alpha 1(II) mRNA in most tissues analysed: calvarial and diaphyseal bone, striated and cardiac muscle, skin, brain, lung, kidney, liver, small intestine and colon. Both alternatively spliced forms of the mRNA were present in these tissues. In cartilage, the short form of the procollagen alpha 1(II) mRNA (without exon 2 sequences) was clearly more abundant, whereas in most of the non-cartilaginous tissues the long form was the predominant one. Low levels of procollagen alpha 2(XI) mRNA were also seen in non-cartilaginous tissues: calvarial and diaphyseal bone, kidney, skin, muscle, intestine, liver, brain, and lung. In all the other positive tissues except brain cortex, both collagen II and XI transcripts were observed. The localization of collagen II and XI signals was identical in cartilage, kidney and skin. However, in cartilage the signal with collagen II probe was much higher than that with the collagen alpha 2(XI) probe. In epidermis the situation was reversed. Our results show considerable co-expression and co-localization of procollagen alpha 1(II) and alpha 2(XI) mRNAs in many tissues of developing human fetuses. Since the collagen alpha 1(II) gene also codes for the alpha 3(XI) chain of collagen XI we propose that some, but not all, of the expression of the collagen II gene in non-cartilaginous tissues relates to collagen XI production.
Department of Medical Biochemistry, University of Turku, Finland.
M M
MM
Sandberg
H E
HE
Hirvonen
K J
KJ
Elima
E I
EI
Vuorio
D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D003094:Collagen / Q000235:genetics*; D004247:DNA / Q000737:chemistry; D015342:DNA Probes; D005091:Exons; D005333:Fetus / Q000378:metabolism*; D015870:Gene Expression; D006132:Growth Plate / Q000196:embryology / Q000378:metabolism; D006801:Humans; D017403:In Situ Hybridization; D007668:Kidney / Q000737:chemistry / Q000196:embryology; D008969:Molecular Sequence Data; D009928:Organ Specificity; D016133:Polymerase Chain Reaction; D012326:RNA Splicing; D012333:RNA, Messenger / Q000032:analysis / Q000378:metabolism; D012260:Ribonucleases; D012867:Skin / Q000737:chemistry / Q000196:embryology
D015342:DNA Probes; D012333:RNA, Messenger; D003094:Collagen; D004247:DNA; D012260:Ribonucleases