Inhibitory effects of PG‐H/aggrecan and PG‐M/versican on avian neural crest cell migration

Perris, Roberto; Perissinotto, Daniela; Pettway, Zoé; Bronner‐Fraser, Marianne; Mörgelin, Matthias; Kimata, Koji

doi:10.1096/fasebj.10.2.8641562

Cited by 84 publications

(64 citation statements)

References 8 publications

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“…Hyaluronan is crucial for proper trunk NCC migration XHas2-deprived embryos showed altered trunk NCC migration, corroborating a proposed pivotal role of HA during NCC development (Perris et al, 1996;Perris, 1997;Perris and Perissinotto, 2000;Epperlein et al, 2000). In fact, previous experimental evidence from our group have indicated that different local accumulations of HA-versican complexes may define migration-permissive and non-permissive environments for NCC migrating in the trunk region of the embryo (Perris et al, 1991;Perissinotto et al, 2000).…”

Section: Hypaxial Muscle Cells Migration Is Controlled By Xhas2 and Csupporting

confidence: 67%

XHas2 activity is required during somitogenesis and precursor cell migration inXenopusdevelopment

et al. 2006

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In vertebrates, hyaluronan biosynthesis is regulated by three transmembrane catalytic enzymes denoted Has1, Has2 and Has3. We have previously cloned the Xenopus orthologues of the corresponding genes and defined their spatiotemporal distribution during development. During mammalian embryogenesis, Has2 activity is known to be crucial, as its abrogation in mice leads to early embryonic lethality. Here, we show that, in Xenopus, morpholino-mediated loss-of-function of XHas2 alters somitogenesis by causing a disruption of the metameric somitic pattern and leads to a defective myogenesis. In the absence of XHas2, early myoblasts underwent apoptosis, failing to complete their muscle differentiation programme. XHas2 activity is also required for migration of hypaxial muscle cells and trunk neural crest cells (NCC). To approach the mechanism whereby loss of HA, following XHas2 knockdown, could influence somitogenesis and precursor cell migration, we cloned the orthologue of the primary HA signalling receptor CD44 and addressed its function through an analogous knockdown approach. Loss of XCD44 did not disturb somitogenesis, but strongly impaired hypaxial muscle precursor cell migration and the subsequent formation of the ventral body wall musculature. In contrast to XHas2, loss of function of XCD44 did not seem to be essential for trunk NCC migration, suggesting that the HA dependence of NCC movement was rather associated with an altered macromolecular composition of the ECM structuring the cells' migratory pathways. The presented results, extend our knowledge on Has2 function and, for the first time, demonstrate a developmental role for CD44 in vertebrates. On the whole, these data underlie and confirm the emerging importance of cell-ECM interactions and modulation during embryonic development.KEY WORDS: Has2, CD44, Hyaluronan, Somitogenesis, Myogenesis, Cell migration, Neural crest, ECM, Xenopus Development 133, 631-640 doi:10.1242/dev.02225 1 Laboratori di Biologia Cellulare e dello Sviluppo, Dipartimento di Fisiologia e Biochimica, Università di Pisa, Via Carducci 13, Ghezzano, Pisa (PI) 56010, Italy. ). These findings have prompted us to investigate the possible role of XHas2 in somitogenesis, myogenic differentiation and trunk NCC migration, which, thus far, have not been possible to elucidate in Has2-null mice. To this end, we have also cloned the Xenopus orthologue of CD44, known to be the principal cell surface receptor of HA (Wheatley et al., 1993;Ponta et al., 2003) for which the precise role during vertebrate development still remains to be elucidated. MATERIALS AND METHODS Embryo manipulations and whole mount in situ hybridizationXenopus laevis embryos obtained by hormone induced laying, were in vitro fertilized, dejelled, washed and incubated in 0.1ϫMMR. Embryos were staged according to Nieuwkoop and Faber (Nieuwkoop and Faber, 1967), fixed and stained for ␤-galactosidase (200-300 pg injected per embryo) as previously described (Sive et al., 2000) using alternatively a red or light-blue substrate for ...

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Section: Hypaxial Muscle Cells Migration Is Controlled By Xhas2 and Csupporting

confidence: 67%

XHas2 activity is required during somitogenesis and precursor cell migration inXenopusdevelopment

et al. 2006

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“…4). Because the bottle-brush structure of monomeric PG-M/versican (46) was not clearly apparent after rotary shadowing electron microscopy of microfibrils (Fig. 2B), perhaps only a portion of versican (containing the mAb 2B1 epitope) remained undegraded and associated with microfibrils following digestion of tissues with crude collagenase.…”

Section: Resultsmentioning

confidence: 99%

Versican Interacts with Fibrillin-1 and Links Extracellular Microfibrils to Other Connective Tissue Networks

Isogai¹,

Aspberg²,

Keene³

et al. 2002

Journal of Biological Chemistry

204

140

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Fibrillin-containing microfibrils are polymeric structures that are difficult to extract from connective tissues. Proteolytic digestion of tissues has been utilized to release microfibrils for study. Few of the molecules that connect microfibrils to other elements in the matrix have been identified. In this study, electron microscopic immunolocalization of anti-versican antibodies in tissues and in extracted microfibrils demonstrated that the C-terminal region of versican is found associated with fibrillin microfibrils. Extraction of microfibrils followed by treatment of microfibrils under dissociating conditions suggested that the versican C terminus is covalently bound to microfibrils. Binding assays using recombinant fibrillin-1 polypeptides and recombinant lectican lectin domains indicated that the versican lectin domain binds to specific fibrillin-1 polypeptides. The versican lectin domain also bound to molecules comigrating with authentic fibrillin-1 monomers in an assay using cell culture medium. In assays using microfibrils, the versican lectin domain demonstrated preferential binding compared with other lecticans. Binding was calcium-dependent. The binding site for versican in microfibrils is most likely within a region of fibrillin-1 between calcium-binding epidermal growth factor-like domains 11 and 21. Human mutations in this region can result in severe forms of the Marfan syndrome ("neonatal" Marfan syndrome). The connection between versican and fibrillin microfibrils may be functionally significant, particularly in cardiovascular tissues.

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“…Versican has been implicated in the regulation of neural crest migration and cardiovascular development (Dutt et al, 2006;Henderson et al, 1997;Landolt et al, 1995;Perissinotto et al, 2000;Perris et al, 1996). Splotch, a Pax3 mutant, is believed to result in part from the overexpression of versican, which results in skin pigmentation and craniofacial defects (Henderson et al, 1997).…”

Section: Genetic Interaction Of Vcan With Adamts20 Implies An Active mentioning

confidence: 99%

Cooperation of two ADAMTS metalloproteases in closure of the mouse palate identifies a requirement for versican proteolysis in regulating palatal mesenchyme proliferation

et al. 2010

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SUMMARYWe have identified a role for two evolutionarily related, secreted metalloproteases of the ADAMTS family, ADAMTS20 and ADAMTS9, in palatogenesis. Adamts20 mutations cause the mouse white-spotting mutant belted (bt), whereas Adamts9 is essential for survival beyond 7.5 days gestation (E7.5). Functional overlap of Adamts9 with Adamts20 was identified using Adamts9 +/-;bt/bt mice, which have a fully penetrant cleft palate. Palate closure was delayed, although eventually completed, in both Adamts9 +/-;bt/+ and bt/bt mice, demonstrating cooperation of these genes. Adamts20 is expressed in palatal mesenchyme, whereas Adamts9 is expressed exclusively in palate microvascular endothelium. Palatal shelves isolated from Adamts9;bt/bt mice fused in culture, suggesting an intact epithelial TGF3 signaling pathway. Cleft palate resulted from a temporally specific delay in palatal shelf elevation and growth towards the midline. Mesenchyme of Adamts9;bt/bt palatal shelves had reduced cell proliferation, a lower cell density and decreased processing of versican (VCAN), an extracellular matrix (ECM) proteoglycan and ADAMTS9/20 substrate, from E13.5 to E14.5. Vcan haploinsufficiency led to greater penetrance of cleft palate in bt mice, with a similar defect in palatal shelf extension as Adamts9 +/-;bt/bt mice. Cell density was normal in bt/bt;Vcan hdf/+ mice, consistent with reduced total intact versican in ECM, but impaired proliferation persisted in palate mesenchyme, suggesting that ADAMTScleaved versican is required for cell proliferation. These findings support a model in which cooperative versican proteolysis by ADAMTS9 in vascular endothelium and by ADAMTS20 in palate mesenchyme drives palatal shelf sculpting and extension. KEY WORDS: ADAMTS, Cleft palate, Versican, MouseCooperation of two ADAMTS metalloproteases in closure of the mouse palate identifies a requirement for versican proteolysis in regulating palatal mesenchyme proliferation

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Inhibitory effects of PG‐H/aggrecan and PG‐M/versican on avian neural crest cell migration

Cited by 84 publications

References 8 publications

XHas2 activity is required during somitogenesis and precursor cell migration inXenopusdevelopment

XHas2 activity is required during somitogenesis and precursor cell migration inXenopusdevelopment

Versican Interacts with Fibrillin-1 and Links Extracellular Microfibrils to Other Connective Tissue Networks

Cooperation of two ADAMTS metalloproteases in closure of the mouse palate identifies a requirement for versican proteolysis in regulating palatal mesenchyme proliferation

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