Acquisition of type IX collagen by the developing avian primary corneal stroma and vitreous

Fitch, John M.; Mentzer, Anita; Mayne, Richard; Linsenmayer, Thomas F.

doi:10.1016/0012-1606(88)90301-6

Cited by 76 publications

(53 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A major portion of this long IX expression was localized to the presumptive ciliary epithelium, the source of the vitreous, a t stage 20 and 23. This is consistent with our previous immunohistochemical and in situ observations (Fitch et al, 1988;Linsenmayer et al, 1990b), and is confirmed by the results reported here. Further development of the vitreous, however, is characterized by another switch, beginning at about 7 days of development.…”

Section: Discussionsupporting

confidence: 94%

“…Previously, others have documented the presence of mRNA for mostly the short form of the al(1X) collagen polypeptide in 6-day (Svoboda et al, 1988) and 8-day (Nishimura et al, 1989) corneas, and we show here that the quantity of such transcripts is substantial during this period. But type IX protein has not been demonstrated in the avian cornea after 5 days, using antibodies in immunohistochemical analyses (Fitch et al, 1988. Whether the protein is indeed deposited during this time is clouded by the fact that the epitope recognized by antibody 2C2 (the one which detects both forms) appears to be largely masked when the type IX molecule becomes assembled onto the surface of type I1 collagencontaining fibrils (Vaughan et al, 1988;Fitch et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

“…For type IX, the major isoform of al (1X) mRNA present a t 6 days (Svoboda et al, 1988) and 8 days (Nishimura et al, 1989) is the short form (indeed, this form was originally termed "corneal type IX"). However, available antibodies have not detected type IX in the stroma after 5 days of development (stage 27; see Fitch et al, 1988Fitch et al, , 1994. Whether this is due to masking of type IX epitopes, to lack of translation of abundant transcripts, or to a post-translational control mechanism has not been determined.…”

Section: Developmental Changesmentioning

confidence: 99%

See 2 more Smart Citations

Analysis of transcriptional isoforms of collagen types IX, II, and I in the developing avian cornea by competitive polymerase chain reaction

Fitch

Gordon

Gibney

et al. 1995

Developmental Dynamics

Self Cite

View full text Add to dashboard Cite

The genes for the al(IX), al(II), and a2(I) collagen chains can give rise to different isoforms of mRNA, generated by alternative promotor usage [for al(1X) and &?(I)] or alternative splicing [for cyl(II)]. In this study, we employed competitive reverse transcriptase PCR to quantitate the amounts of transcriptional isoforms for these genes in the embryonic avian cornea from its inception (about 3 1/2 days of development) to 11 days. In order to compare values at different time points, the results were normalized to those obtained for the "housekeeping" enzyme, glycerol-3-phosphate dehydrogenase (G3PDH). These values were compared to those obtained from other tissues (anterior optic cup and cartilage) that synthesize different combinations of the collagen isoforms. We found that, in the cornea, transcripts from the upstream promotor of al(1X) collagen (termed "long IX") were predominant at stage 18-20 (about 3 1/2 days), but then fell rapidly, and remained at a low level. By 5 days (just before stromal swelling) the major mRNA isoform of al(1X) was from the downstream promotor (termed "short IX"). The relative amount of transcript for the short form of type IX collagen rose to a peak at about 6 days of development, and then declined. Throughout this period, the predominant transcriptional isoform of the collagen type I1 gene was IIA (i.e., containing the alternatively spliced exon 2). This indicates that the molecules of type I1 collagen that are assembled into heterotypic fibrils with type I collagen possess, at least transiently, an amino-terminal globular domain similar to that found in collagen types I, 111, and V. For type I, the "bone/tendon" mRNA isoform of the cy2(I) collagen gene was predominant; transcripts from the downstream promotor were at basal levels. In other tissues expressing collagen types IX and 11, long IX was expressed predominantly with the IIA form in the anterior optic cup at stage 22/23; in 14 112 day cartilage, long IX was expressed predominantly along with the IIB form of al(1I). The downstream transcript of the a2(I) gene (Icart) was found at high levels only in cartilage.

show abstract

Section: Discussionsupporting

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Section: Developmental Changesmentioning

confidence: 99%

See 1 more Smart Citation

Analysis of transcriptional isoforms of collagen types IX, II, and I in the developing avian cornea by competitive polymerase chain reaction

Fitch

Gordon

Gibney

et al. 1995

Developmental Dynamics

Self Cite

View full text Add to dashboard Cite

show abstract

“…The cross-links are formed through the lysyl oxidase mechanism (3)(4)(5)(6)(7). Collagen IX is found mostly in cartilages, but it also occurs in the eye (vitreum (8,9) and avian cornea (8)), ear (tectorial membrane (10)), and intervertebral disc (11,12), always in co-existence with type II collagen. A special role for collagen IX in the organization of type II collagen fibril networks has apparently evolved, which for articular cartilage seems to be essential for the long term normal functioning of joints.…”

mentioning

confidence: 99%

Covalent Cross-linking of the NC1 Domain of Collagen Type IX to Collagen Type II in Cartilage

Eyre

Pietka

Weis

et al. 2004

Journal of Biological Chemistry

120

View full text Add to dashboard Cite

From a study to understand the mechanism of covalent interaction between collagen types II and IX, we present experimental evidence for a previously unrecognized molecular site of cross-linking. The location relative to previously defined cross-linking sites predicts a specific manner of interaction and folding of collagen IX on the surface of nascent collagen II fibrils. The initial evidence came from Western blot analysis of type IX collagen extracted by pepsin from fetal human cartilage, which showed a molecular species that had properties indicating an adduct between the ␣1(II) chain and the C-terminal domain (COL1) of type IX collagen. A similar component was isolated from bovine cartilage in sufficient quantity to confirm this identity by N-terminal sequence analysis. Using an antibody that recognized the putative cross-linking sequence at the C terminus of the ␣1(IX) chain, cross-linked peptides were isolated by immunoaffinity chromatography from proteolytic digests of human cartilage collagen. They were characterized by immunochemistry, N-terminal sequence analysis, and mass spectrometry. The results establish a link between a lysine near the C terminus (in the NC1 domain) of ␣1(IX) and the known cross-linking lysine at residue 930 of the ␣1(II) triple helix. This cross-link is speculated to form early in the process of interaction between collagen IX molecules and collagen II polymers. A model of molecular folding and further cross-linking is predicted that can spatially accommodate the formation of all six known cross-linking interactions to the collagen IX molecule on a fibril surface. Of particular biological significance, this model can accommodate potential interfibrillar as well as intrafibrillar links between the collagen IX molecules themselves, so providing a mechanism whereby collagen IX could stabilize a collagen fibril network.Collagen type IX is a member of the fibril-associated collagen with interrupted triple helix (FACIT) 1 family of collagen molecules, which share homologous domains and are all believed to function in the extracellular matrix in association with collagen fibril surfaces (1, 2). Collagen IX is unique among the FACIT molecules in binding covalently to fibril surfaces. The cross-links are formed through the lysyl oxidase mechanism (3-7). Collagen IX is found mostly in cartilages, but it also occurs in the eye (vitreum (8, 9) and avian cornea (8)), ear (tectorial membrane (10)), and intervertebral disc (11, 12), always in co-existence with type II collagen. A special role for collagen IX in the organization of type II collagen fibril networks has apparently evolved, which for articular cartilage seems to be essential for the long term normal functioning of joints. The evidence for this comes from the study of genetic defects. Mutations in all three collagen IX genes have been linked to a chondrodysplasia syndrome (multiple epiphyseal dysplasia), which features early onset osteoarthritis (13).All three chains of the vertebrate collagen IX molecule, ␣1(IX), ␣2(IX), and ␣3(IX)...

show abstract

“…Immunocytochemistry was performed as described in Solursh and Jensen (1988). Antibodies used in this study were: (1) monoclonals: antitype I collagen I,B6 (generously provided by Dr. T. Linsenmayer), anti-type I1 collagen I16B3 (Linsenmayer and Hendrix, 1980) and anti-type 111 collagen 3B2 (Swasdison et al, 1992) (Developmental Studies, Hybridoma Bank), anti-type I1 2B1 (Fitch et al, 1988); and (2) polyclonal: a n affinity purified rabbit antibody to type I1 collagen (generously provided by Dr. T. Linsenmayer), a goat antibody to V collagen (Southern Biotechnology Corp., Inc., Birmingham, AL) following 0.1 mg/ml pepsin digestion in 0.1 M acetic acid for 10 min at room temperature (RT).…”

Section: Immunohis Tochemis Trymentioning

confidence: 99%

Type II collagen is transiently expressed during avian cardiac valve morphogenesis

Swiderski

Daniels

Jensen

et al. 1994

Developmental Dynamics

View full text Add to dashboard Cite

We present new evidence of the temporal and spatial expression of type I1 collagen in the embryonic chick heart during the very early stages of its development. In particular, we emphasize the distribution of its mRNA and protein during valve formation. Type I1 collagen as well as several other fibrillar collagens (types I, 111, and V) are present in stage 18 endocardial cushion mesenchymal cells. At stage 23, al(I1) collagen transcripts and the cognate polypeptide colocalize in the atrioventricular valves. As development proceeds, the relative abundance of al(I1) collagen transcripts decreases during the stages studied (stages 22 to 45; day 3.5 to day 19) as assayed by RNA blotting of extracts of whole hearts. Type I1 collagen protein was immunologically undetectable in stage 38 (day 12) hearts, although collagens I, 111, and V persisted and localize in the valve regions, in the endothelial lining of the heart, and in the epicardium. In keeping with other observations of type I1 collagen expression in non-chondrogenic regions of a variety of vertebrate embryos, the avian heart also exhibits transient type I1 collagen expression.

show abstract

Acquisition of type IX collagen by the developing avian primary corneal stroma and vitreous

Cited by 76 publications

References 38 publications

Analysis of transcriptional isoforms of collagen types IX, II, and I in the developing avian cornea by competitive polymerase chain reaction

Analysis of transcriptional isoforms of collagen types IX, II, and I in the developing avian cornea by competitive polymerase chain reaction

Covalent Cross-linking of the NC1 Domain of Collagen Type IX to Collagen Type II in Cartilage

Type II collagen is transiently expressed during avian cardiac valve morphogenesis

Contact Info

Product

Resources

About