Embryonic expression of type XIX collagen is transient and confined to muscle cells

Sumiyoshi, Hideaki; Laub, Friedrich; Yoshioka, Hidekatsu; Ramirez, Francesco

doi:10.1002/1097-0177(2000)9999:9999<::aid-dvdy1099>3.0.co;2-w

Cited by 38 publications

(6 citation statements)

References 43 publications

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“…It was initially characterized by its implication in muscle differentiation and morphogenesis (6,7). This role, however, does not exclude other functions.…”

Section: Discussionmentioning

confidence: 99%

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The NC1 domain of type XIX collagen inhibits in vivo melanoma growth

Ramont

Brassart‐Pasco

Thévenard

et al. 2007

Molecular Cancer Therapeutics

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Type XIX collagen is a minor collagen that localizes to basement membrane zones, together with types IV, XV, and XVIII collagens. Because several NC1 COOH-terminal domains of other chains from basement membrane collagens were reported to exhibit antitumor activity, we decided to study the effects of the NC1(XIX) collagen domain on tumor progression using an experimental in vivo model of mouse melanoma. We observed a 70% reduction in tumor volume in NC1(XIX)-treated mice compared with the corresponding controls. Histologic examination of the tumors showed a strong decrease in tumor vascularization in treated mice. In vitro, NC1(XIX) inhibited the migrating capacity of tumor cells and their capacity to invade Matrigel. It also inhibited the capacity of human microvascular endothelial cells to form pseudotubes in Matrigel. This effect was accompanied by a strong inhibition of membrane type-1 matrix metalloproteinase (matrix metalloproteinase-14) and vascular endothelial growth factor expression. Collectively, our data indicate that the NC1 domain of type XIX collagen exerts antitumor activity. This effect is mediated by a strong inhibition of the invasive capacities of tumor cells and antiangiogenic effects. NC1(XIX) should now be considered as a new member of the basement membrane collagen-derived matrikine family with antitumor and antiangiogenic activity. [Mol Cancer Ther 2007;6(2):506 -14]

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“…It was initially characterized by its implication in muscle differentiation and morphogenesis (6,7). This role, however, does not exclude other functions.…”

Section: Discussionmentioning

confidence: 99%

“…The a1(XIX) chain is constituted of a 268-residue NH 2 -terminal domain, an 858-residue discontinuous collagenous domain, and a short 19-residue COOH-terminal noncollagenous NC1 domain. It seems to be involved in muscle differentiation, esophageal muscle physiology, and morphogenesis, but other functions cannot be excluded (6,7).…”

Section: Introductionmentioning

confidence: 99%

The NC1 domain of type XIX collagen inhibits in vivo melanoma growth

Ramont

Brassart‐Pasco

Thévenard

et al. 2007

Molecular Cancer Therapeutics

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“…Expression studies during early development in mice show that ColXIX transcripts are restricted in the developing muscle at embryonic day 11.5 and decrease by embryonic day 16.5 4267 RESEARCH ARTICLE Collagen XIX in motor axon outgrowth DEVELOPMENT (Sumiyoshi et al, 2001). Expression was also observed in smooth muscle cells in the stomach and around the jaw (Sumiyoshi et al, 2001). ColXIX-null mice are normal at birth but, ~95% of pups die within the first 3 weeks, presumably caused by their inability to feed.…”

Section: Collagen XIX During Developmentmentioning

confidence: 99%

Collagen XIXa1 is crucial for motor axon navigation at intermediate targets

2010

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SUMMARYDuring development, motor axons navigate from the spinal cord to their muscle targets in the periphery using stereotyped pathways. These pathways are broken down into shorter segments by intermediate targets where axon growth cones are believed to coordinate guidance cues. In zebrafish stumpy mutants, embryonic development proceeds normally; however, as trunk motor axons stall at their intermediate targets, suggesting that Stumpy is needed specifically for motor axon growth cones to proceed past intermediate targets. Fine mapping and positional cloning revealed that stumpy was the zebrafish homolog of the atypical FACIT collagen collagenXIXa1 (colXIX). colXIX expression was observed in a temporal and spatial pattern, consistent with a role in motor axon guidance at intermediate targets. Knocking down zebrafish ColXIX phenocopied the stumpy phenotype and this morpholino phenotype could be rescued by adding back either mouse or zebrafish colXIX RNA. The stumpy phenotype was also partially rescued in mutants by first knocking down zebrafish ColXIX and adding back colXIX RNA, suggesting that the mutation is acting as a dominant negative. Together, these results demonstrate a novel function for a FACIT collagen in guiding vertebrate motor axons through intermediate targets.

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“…Type XIX RNA and protein were dramatically up-regulated in RMS cells cultured in growth factor-depleted serum (20); this induction was restricted to a small subpopulation of cells that also expressed structural proteins characteristic of skeletal muscle differentiation. In a subsequent report, it was shown that during mouse embryonic development, spatial and temporal expression of type XIX RNA was essentially coincident with the myf-5 transcription factor (21). Most recently, type XIX null mice with a perinatal lethal phenotype were used to establish that this collagen is required for complete esophageal muscle transdifferentiation.…”

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confidence: 99%

Type XIX Collagen Purified from Human Umbilical Cord Is Characterized by Multiple Sharp Kinks Delineating Collagenous Subdomains and by Intermolecular Aggregates via Globular, Disulfide-linked, and Heparin-binding Amino Termini

Myers

Amenta

et al. 2003

Journal of Biological Chemistry

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Type XIX collagen was discovered from the sequence of rhabdomyosarcoma cDNA clones. The chain is composed of a 268-residue amino terminus, an 832-residue discontinuous collagenous region, and a 19-residue carboxyl peptide. Light microscopy immunohistochemistry of adult human tissues demonstrated that type XIX is localized in vascular, neuronal, mesenchymal, and some epithelial basement membrane zones. It also appears to be involved in events linked to skeletal myogenesis. In this report, we have presented the first direct evidence for the molecular structure of type XIX collagen. Using human umbilical cord, native type XIX was purified by neutral salt extraction and by ion exchange and antibody affinity chromatography. Type XIX was found to represent only ϳ10 ؊6 % of the dry weight of tissue, making it by far the least abundant collagen ever isolated. Transmission electron microscopy after rotary shadowing revealed the appearance of rodlike structures with multiple sharp bends, a small nodule at one end of the molecule, and a total length of 240 nm. Domain-specific antibodies were used to identify the nodule as the noncollagenous amino terminus, whereas the location of most kinks corresponds to major interruptions separating the five collagenous subdomains. More than half of the type XIX molecules observed were present in oligomers of different size and complexity, resulting from association of the amino-terminal domains. Biochemical analysis demonstrated that these supramolecular aggregates are dependent upon and/or stabilized by intermolecular disulfide cross-links and that the globular amino terminus contains a high affinity, heparin-binding site. The polymorphic conformational states of this rare collagen, and its ability to self-assemble into a higher order structure provide focal points for future determination of biologically significant functions in cell-cell and/or cell-matrix interactions.Twenty-six collagen types have currently been designated; seven of these are recent discoveries, and several have yet to be described (1-7). With the diversity that this family has presented, one of the few defining elements is the existence of one or more triple-helical regions, regardless of size and relative proportion to the entire protein. In the most general sense, therefore, collagens have been divided into the classic fibrillar group (i.e. those containing the ϳ333 continuous Gly-X-Y triplets and involved in the formation of cross-striated fibrils) and the nonfibrillar group, a highly heterogeneous class exhibiting a spectrum of sizes, supramolecular assemblies, and chain organization, with the one commonality being the presence of noncollagenous sequences interrupting and/or flanking collagenous domains (1, 2, 8 -10). Understanding the complex structure and function of these many proteins has proven to be a formidable task despite, in many instances, extensive knowledge of disease phenotypes directly attributable to the respective collagen gene mutations (1, 11, 12). A major complication in this process has b...

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Embryonic expression of type XIX collagen is transient and confined to muscle cells

Cited by 38 publications

References 43 publications

The NC1 domain of type XIX collagen inhibits in vivo melanoma growth

The NC1 domain of type XIX collagen inhibits in vivo melanoma growth

Collagen XIXa1 is crucial for motor axon navigation at intermediate targets

Type XIX Collagen Purified from Human Umbilical Cord Is Characterized by Multiple Sharp Kinks Delineating Collagenous Subdomains and by Intermolecular Aggregates via Globular, Disulfide-linked, and Heparin-binding Amino Termini

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