Regular ArticleVersican Modulates Embryonic Chondrocyte Morphology via the Epidermal Growth Factor-like Motifs in G3
References (43)
- et al.
cDNA cloning of PG-M, a large chondroitin sulfate proteoglycan expressed during chondrogenesis in chick limb buds. Alternative spliced multiforms of PG-M and their relationships to versican
J. Biol. Chem.
(1993) - et al.
Characterization of the complete genomic structure of the human versican gene and functional analysis of its promoter
J. Biol. Chem.
(1994) - et al.
A large chondroitin sulfate proteoglycan (PG-M) synthesized before chondrogenesis in the limb bud of chick embryo
J. Biol. Chem.
(1986) - et al.
FGF-4 replaces the apical ectodermal ridge and directs outgrowth and patterning of the limb
Cell
(1993) - et al.
Autosomal dominant and recessive osteochondrodysplasias associated with the COL11A2 locus
Cell
(1995) - et al.
Proteochondroitin sulfate synthesis and chondrogenic expression
Exp. Cell Res.
(1974) - et al.
The occurrence of a new type of proteochondroitin sulfate in the developing chick embryo
FEBS Lett.
(1976) - et al.
Chemical and physical changes in proteoglycans during development of chick limb bud chondrocytes grown in vitro
J. Biol. Chem.
(1977) - et al.
Morphological and biochemical differentiation of limb bud cells cultured in chemically defined medium
Dev. Biol.
(1979) - et al.
Physical and immunochemical characterization of proteoglycans synthesized during chondrogenesis in the chick embryo
J. Biol. Chem.
(1980)
Chondroitin sulfate proteoglycan (PG-M-like proteoglycan) is involved in the binding of hyaluronic acid to cellular fibronectin
J. Biol. Chem.
Regulation of cell–substrate adhesion by proteoglycans immobilized on extracellular substrates
J. Biol. Chem.
A fibroblast chondroitin sulfate proteoglycan core protein contains lectin-like and growth factor-like sequences
J. Biol. Chem.
Tandem repeats are involved in G1 domain inhibition of versican expression and secretion and the G3 domain enhances glycosaminoglycan modification and secretion via the complement-binding protein motif
J. Biol. Chem.
Link protein is ubiquitously expressed in non-cartilaginous tissues where it enhances and stabilizes the interaction of proteoglycans with hyaluronic acid
J. Biol. Chem.
Chondrocyte apoptosis induced by aggrecan G1 domain as a result of decreased cell adhesion
Exp. Cell Res.
beta-Integrin–collagen interaction reduces chondrocyte apoptosis
Matrix Biol.
The G3 domain of versican inhibits mesenchymal chondrogenesis via the epidermal growth factor-like motifs
J. Biol. Chem.
In vitro differentiation potential of the periosteal cells from a membrane bone, the quadratojugal of the embryonic chick
Dev. Biol.
Abnormal occurrence of a large chondroitin sulfate proteoglycan, PG-M/versican in osteoarthritic cartilage
Osteoarthritis Cartilage
Aggrecan and link protein affect cell adhesion to culture plates and to type II collagen
Matrix Biol.
Cited by (41)
Promotion of tumor progression by exosome transmission of circular RNA circSKA3
2022, Molecular Therapy Nucleic AcidsBones and Cartilage: Developmental and Evolutionary Skeletal Biology
2015, Bones and Cartilage: Developmental and Evolutionary Skeletal BiologyVersican 3'-untranslated region (3'UTR) promotes dermal wound repair and fibroblast migration by regulating miRNA activity
2014, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :Versican is the principal chondroitin sulfate proteoglycan in blood vessels, as well as in the intima and adventitia of most arteries and veins [10]. In vitro studies have shown that versican modulates cell adhesion [11], aggregation [12], migration [13], proliferation [14], morphogenesis [15,16], and tissue angiogenesis [17]. This study was designed to explore the roles of versican in the process of dermal wound repair.
Proteoglycan degradation by the ADAMTS family of proteinases
2011, Biochimica et Biophysica Acta - Molecular Basis of DiseaseCitation Excerpt :There is continuing intrigue and speculation amongst the research community that this fragment, and other catalytic fragments of proteoglycan substrates, might have unique biological properties that are not invested in the parent molecules. Indeed, recombinant single domains of versican appear to have bioactivity in cell culture systems [182–184]. Proteoglycans in extracellular matrices are degraded by ADAMTS enzymes in many and varied biological situations.
Tumour cell adhesion and integrin expression affected by Ganoderma lucidum
2006, Enzyme and Microbial Technology
- 1
To whom correspondence and reprint requests should be addressed at Research Building, Sunnybrook & Women's College Health Sciences Centre, 2075 Bayview Avenue, Toronto M4N 3M5, Canada. Fax: (416) 480-5737. E-mail: [email protected].