Expression of type XIV collagen in developing chicken tendons: Association with assembly and growth of collagen fibrils

Young, Blanche; Gordon, Marion K.; Birk, David E.

doi:10.1002/(sici)1097-0177(200004)217:4<430::aid-dvdy10>3.0.co;2-5

Cited by 91 publications

(83 citation statements)

References 35 publications

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“…Together with other studies, our results demonstrate that chicken collagen XIV contains at least three regions, which are subject to alternative splicing: the first F3 domain at the N terminus (4, 11, this report), a 3-amino acid segment in the center of the molecule (22), and a 31-amino acid segment in the C-terminal NC1 domain (4,30). Theoretically, alternative splicing of these three regions could give rise to eight different collagen XIV isoforms.…”

Section: Discussionsupporting

confidence: 79%

“…Because collagen XIV seems to interact with interstitial collagen fibrils via its COL1 and NC1 domains, alternative splicing within the NC1 domain may affect this interaction. The longer NC1 isoform contains an uncharged region inserted into the otherwise highly charged NC1 domain (4,30). It was therefore speculated that the longer NC1 variant may favor a strong interaction with the surface of the collagen fibrils and their tapered ends, whereas the shorter isoform may have a lower affinity (30).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Alternative Splicing of the First F3 Domain from Chicken Collagen XIV Affects Cell Adhesion and Heparin Binding

Imhof

Trüeb

2001

Journal of Biological Chemistry

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Section: Discussionsupporting

confidence: 79%

Section: Discussionmentioning

confidence: 99%

Alternative Splicing of the First F3 Domain from Chicken Collagen XIV Affects Cell Adhesion and Heparin Binding

Imhof

Trüeb

2001

Journal of Biological Chemistry

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“…In this model the embryonic fibrils would act as a template for the formation of mature tendons with mechanical properties suitable for the demands placed on the tissue after birth/hatching. Interestingly, immunoreactivity for type XIV collagen, which is located on the surface of collagen fibrils (49), disappears from developing chick tendons at hatching (50). This corresponds to the time when fibril diameters switch from a unimodal (narrow diameter) to a multimodal distribution (51).…”

Section: Discussionmentioning

confidence: 99%

Actin Filaments Are Required for Fibripositor-mediated Collagen Fibril Alignment in Tendon

Canty

Starborg

et al. 2006

Journal of Biological Chemistry

128

117

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Cells in tendon deposit parallel arrays of collagen fibrils to form a functional tissue, but how this is achieved is unknown. The cellular mechanism is thought to involve the formation of intracellular collagen fibrils within Golgi to plasma membrane carriers. This is facilitated by the intracellular processing of procollagen to collagen by members of the tolloid and ADAMTS families of enzymes. The carriers subsequently connect to the extracellular matrix via finger-like projections of the plasma membrane, known as fibripositors. In this study we have shown, using three-dimensional electron microscopy, the alignment of fibripositors with intracellular fibrils as well as an orientated cable of actin filaments lining the cytosolic face of a fibripositor. To demonstrate a specific role for the cytoskeleton in coordinating extracellular matrix assembly, cytochalasin was used to disassemble actin filaments and nocodazole or colchicine were used to disrupt microtubules. Microtubule disruption delayed procollagen transport through the secretory pathway, but fibripositor numbers were unaffected. Actin filament disassembly resulted in rapid loss of fibripositors and a subsequent disappearance of intracellular fibrils. Procollagen secretion or processing was not affected by cytochalasin treatment, but the parallelism of extracellular collagen fibrils was altered. In this case a significant proportion of collagen fibrils were found to no longer be orientated with the long axis of the tendon. The results suggest an important role for the actin cytoskeleton in the alignment and organization of the collagenous extracellular matrix in embryonic tendon.

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“…To identify genes regulated by Scx that could be responsible for Scx function in tendon formation, we therefore examined the expression of genes known to be expressed specifically in all tendons [e.g. tenomodulin (Brandau et al, 2001); collagen I and collagen XIV (Walchli et al, 1994;Young et al, 2000); collagen XII (Dublet and van der Rest, 1987); tenascin C (Chiquet and Fambrough, 1984); fibromodulin, lumican and decorin (Ezura et al, 2000)] or genes described as being specifically expressed in tendons within the context of the limb bud [e.g. Six2 (Oliver et al, 1995), Eya1 (Xu et al, 1997) and Fgf18 (Liu et al, 2002)].…”

Section: Molecular Characterization Of the Scxmentioning

confidence: 99%

Regulation of tendon differentiation by scleraxis distinguishes force-transmitting tendons from muscle-anchoring tendons

et al. 2007

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The scleraxis (Scx) gene, encoding a bHLH transcription factor, is expressed in the progenitors and cells of all tendon tissues. To determine Scx function, we produced a mutant null allele. Scx -/-mice were viable, but showed severe tendon defects, which manifested in a drastically limited use of all paws and back muscles and a complete inability to move the tail. Interestingly, although the differentiation of all force-transmitting and intermuscular tendons was disrupted, other categories of tendons, the function of which is mainly to anchor muscles to the skeleton, were less affected and remained functional, enabling the viability of Scx -/-mutants. The force-transmitting tendons of the limbs and tail varied in the severity to which they were affected, ranging from dramatic failure of progenitor differentiation resulting in the loss of segments or complete tendons, to the formation of small and poorly organized tendons. Tendon progenitors appeared normal in Scx -/-embryos and a phenotype resulting from a failure in the condensation of tendon progenitors to give rise to distinct tendons was first detected at embryonic day (E)13.5. In the tendons that persisted in Scx -/-mutants, we found a reduced and less organized tendon matrix and disorganization at the cellular level that led to intermixing of tenocytes and endotenon cells. The phenotype of Scx -/-mutants emphasizes the diversity of tendon tissues and represents the first molecular insight into the important process of tendon differentiation.

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Expression of type XIV collagen in developing chicken tendons: Association with assembly and growth of collagen fibrils

Cited by 91 publications

References 35 publications

Alternative Splicing of the First F3 Domain from Chicken Collagen XIV Affects Cell Adhesion and Heparin Binding

Alternative Splicing of the First F3 Domain from Chicken Collagen XIV Affects Cell Adhesion and Heparin Binding

Actin Filaments Are Required for Fibripositor-mediated Collagen Fibril Alignment in Tendon

Regulation of tendon differentiation by scleraxis distinguishes force-transmitting tendons from muscle-anchoring tendons

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