Collagen type IX and developmentally regulated swelling of the avian primary corneal stroma

Fitch, John M.; Fini, M. Elizabeth; Beebe, David C.; Linsenmayer, Thomas F.

doi:10.1002/(sici)1097-0177(199805)212:1<27::aid-aja3>3.0.co;2-4

Cited by 31 publications

(9 citation statements)

References 35 publications

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“…Clearly collagen IX has evolved to be a highly specialized covalent adapter of polymeric collagen type II fibrillar networks in cartilages and certain other tissues of higher vertebrates. During avian corneal development, selective proteolysis of collagen IX has been observed coincident with matrix swelling (33). A similar mechanism for the swelling of cartilage collagen after joint injury is suspected, and stromelysin-1 (matrix metalloproteinase-3), a candidate protease, is known to cleave at a specific site in all three chains of the NC2 domain of type IX collagen (23).…”

Section: Discussionmentioning

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

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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)...

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Section: Discussionmentioning

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

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“…During development of the avian eye, the primary corneal stroma swells in anticipation of its invasion by mesenchymal cells from the periphery (Hay, 1980). This swelling has been found to be controlled by tissue-specific, developmentally regulated proteolysis of collagen IX (Fitch et al, 1998). Vertebrate limb chondrogenesis is an example of a developmental process in which cellular rearrangement occurs as a result of matrix deposition.…”

Section: Matrix Swelling Deposition and Lossmentioning

confidence: 99%

Mechanisms of pattern formation in development and evolution

2003

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We present a classification of developmental mechanisms that have been shown experimentally to generate pattern and form in metazoan organisms. We propose that all such mechanisms can be organized into three basic categories and that two of these may act as composite mechanisms in two different ways. The simple categories are cell autonomous mechanisms in which cells enter into specific arrangements ('patterns') without interacting, inductive mechanisms in which cell communication leads to changes in pattern by reciprocal or hierarchical alteration of cell phenotypes ('states') and morphogenetic mechanisms in which pattern changes by means of cell interactions that do not change cell states. The latter two types of mechanism can be combined either morphostatically, in which case inductive mechanisms act first, followed by the morphogenetic mechanism, or morphodynamically, in which case both types of mechanisms interact continuously to modify each other's dynamics. We propose that this previously unexplored distinction in the operation of composite developmental mechanisms provides insight into the dynamics of many developmental processes. In particular, morphostatic and morphodynamic mechanisms respond to small changes in their genetic and microenvironmental components in dramatically different ways. We suggest that these differences in 'variational properties' lead to morphostatic and morphodynamic mechanisms being represented to different extents in early and late stages of development and to their contributing in distinct ways to morphological transitions in evolution.

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“…The second wave begins at E6 and invades the primary corneal stroma. The cells populate the entire stroma and give rise to the corneal stromal fibroblasts [10]. The cells of a third wave contribute to the formation of the stromal component of the iris [3].…”

Section: Basic Embryologymentioning

confidence: 99%

Update on Anterior Segment Development with Emphasis on Genetics and Correlation with Pathogenesis of Developmental & Primary Open Angle Glaucoma

Alkatan¹

2017

AOVS

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The ocular anterior segment structures are derived from periocular mesenchyme, which consists of neural crest cells and cranial paraxial mesoderm. Many embryological facts have been developed based on the fates of neural crest and mesoderm in mice and in chick. The interactions between the ocular mesenchyme and the surface ectoderm derived cells are also essential for the coordination of anterior segment development. These interactions are mediated by several transcription factors expressed in both the epithelial and mesenchymal cells and are being extensively studied. Anterior Segment dysgenesis (ASD) is a spectrum of disorders of variable phenotypic expressions caused by abnormal migration and differentiation of neural crest cells. Patients with ASD are susceptible to develop infantile glaucoma, congenital endothelial dystrophy, sclerocornea and aniridia. There has been an evident overlapping observation in the genetic mutations between the ASD phenotypic spectrum and glaucoma especially the primary congenital glaucoma (PCG) since it involves abnormal development of Schlemm's canal and the drainage structures. In this review, we are highlighting the steps in the embryological development of the anterior segment chamber structures. We also present the role of various transcription factors and link the above information to some of the genetic abnormalities, which are known in association with the pathogenesis of glaucoma.

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Collagen type IX and developmentally regulated swelling of the avian primary corneal stroma

Cited by 31 publications

References 35 publications

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

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

Mechanisms of pattern formation in development and evolution

Update on Anterior Segment Development with Emphasis on Genetics and Correlation with Pathogenesis of Developmental & Primary Open Angle Glaucoma

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