Northern blot hybridization, reverse-transcription polymerase chain reaction (RT-PCR), and RNase protection assays were used to examine the expression of two alpha 1(IX) collagen mRNA species (long and short form) in developing mouse tissues. Furthermore, in situ hybridization was used to identify cells expressing the Col9a1 gene during eye development. The results indicate that during embryonic development eye and heart preferentially express the short form; lung and cartilage express the long form; whereas liver expresses a very low level of long form alpha 1(IX) mRNA which can only be detected by RT-PCR. In situ hybridization demonstrated that at 10.5 day postcoitum (d.p.c.), the alpha 1(IX) collagen mRNAs were first expressed in optic cup (neural ectoderm) but not in lens vesicle (surface ectoderm). By 13.5 d.p.c., the cells that express the alpha 1(IX) mRNA progressively were concentrated toward the anterior part of the neural retina. By 16.5-18.5 d.p.c., the hybridization signals were found exclusively in the inner non-pigmented layer of the presumptive ciliary epithelium. As ciliary epithelial cells become well differentiated 3 weeks after birth, cells expressing the Col9a1 gene were limited to the junction between mature ciliary folds and the neural retina. No hybridization signal could be detected in ocular tissues of mouse older than 6 weeks. It is of interest to note that a hybridization signal was not detected in cornea at the various developmental stages examined, suggesting that mouse cornea does not significantly express alpha 1(IX) mRNA during embryonic development. This differs from that of chick cornea development. In summary, the expression of the Col9a1 gene shows a temporospatial pattern throughout mouse eye development.(ABSTRACT TRUNCATED AT 250 WORDS)
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Novartis Found Symp
June 2001
Joint Diseases Laboratory, Shriners Hospitals for Children and Division of Surgical Research, Department of Surgery, McGill University, 1529 Cedar Avenue, Montreal, Quebec, Canada H3G 1A6.
Chondrocytes assemble an extracellular matrix in which the relative composition of type IX versus type II collagen and aggrecan changes during assembly. On maturation and differentiation into hypertrophic cells type IX collagen first loses the NC4 globular domain of the alpha 1(IX) chain that protrudes from the collagen fibril. Subsequently, collagenase 3 (matrix metalloproteinase 13; MMP13) is up-regulated as type X collagen is expressed leading to extensive cleavage and removal of type II collagen and of the remaining COL2 domain of type IX collagen alpha 1(IX) chain.
View Article and Find Full Text PDFMatrix Biol
March 1998
Wellcome Trust Center for Cell-Matrix Research, School of Biological Sciences, University of Manchester, UK.
Collagen IX, a structural component of the extracellular matrix of connective tissues, is synthesized as long and short forms which contain or lack, respectively, a 27 kDa non-collagenous (NC) 4 domain at the N-terminus of the alpha 1(IX) chain of the molecule. The long form occurs in cartilage and developing cornea, but not in vitreous, suggesting a specialized function for the NC4 domain, perhaps by interacting with other macromolecules. To test this hypothesis, embryonic chick cartilage was treated with DTSSP, dissociated with bacterial collagenase, and the NC4-containing DTSSP-cross-linked protein complexes examined and purified.
View Article and Find Full Text PDFGenomics
April 1997
Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129-2017, USA.
Overlapping cDNA clones that encode the full-length human alpha 1(XII) collagen polypeptides were isolated. The long variant molecule cDNA of 9750 nucleotides (nt) contains a 9189-nt open reading frame encoding 3063 amino acid residues. The short variant molecule cDNA of 6258 nt contains a 5697-nt open reading frame encoding 1899 amino acid residues.
View Article and Find Full Text PDFJ Prosthet Dent
April 1997
Department of Restorative Dentistry, Harvard School of Dental Medicine, Boston, Mass., USA.
Statement Of Problem: Osteoporosis and edentulism are two disease processes that affect a large group of elderly people in the United States (24 and 25 million, respectively). These two diseases are independent of each other; however, they have several pathologic symptoms in common, such as reduction in bone mass.
Purpose: The purpose of this study was to determine whether estrogen deficiency or its replacement therapy have any effect on the phenomenon of residual ridge remodeling.
Biochim Biophys Acta
June 1996
Department of Internal Medicine, School of Medicine, University of California, Davis 95616-8542, USA.
Rats were intratracheally instilled with bleomycin or with silica (quartz) dust to induce lung fibrosis. Several weeks later, purified collagen chains (or collagen digests) were isolated from the lungs of these animals and from age-matched controls instilled intratracheally with saline solution, and the ratios of hydroxylysine to lysine and of the dysfunctional cross-links DHLNL to HLNL were quantified. Collagen from fibrotic lungs had significantly higher ratios of DHLNL:HLNL than did control lungs, 15.
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