Interaction of intact type VI collagen with hyaluronan

McDevitt, Cahir A.; Marcelino, José Roberto; Tucker, Lynne

doi:10.1016/0014-5793(91)80660-u

Cited by 95 publications

(53 citation statements)

References 17 publications

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“…The antibodies used were MAb CS-56 to native CS a, b anti-aggrecan G1 domain c anti-aggrecan G3 domain d, Mab 12C5 to versican G1 domain e and Mab 5D5 to versican G3 domain f aggrecan acting as lubricating agents is a new role for these proteoglycans in the IVD but consistent with roles proposed for CS-PGs in tendon. Furthermore, type VI collagen is capable of interacting with hyaluronan, a well known lubricating component of synovial fluids [28,29,31,44,52,53] and this association may also facilitate the lubrication of collagen bundles.…”

Section: Discussionmentioning

confidence: 99%

Aggrecan, versican and type VI collagen are components of annular translamellar crossbridges in the intervertebral disc

et al. 2007

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The aim of this study was to undertake a detailed analysis of the structure of the inter and intralamellar regions of the annulus fibrosus. A total of 30 newborn to 6 year-old lumbar ovine intervertebral discs (IVDs) were fixed and decalcified en-bloc to avoid differential swelling artifacts during processing and vertical midsagittal, and horizontal 4 lm sections were cut. These were stained with toluidine blue to visualise anionic proteoglycan (PG) species, H & E for cellular morphology and picrosirius red (viewed under polarized light) to examine collagenous organization. Immunolocalisations were also undertaken using anti-PG core-protein and glycosaminoglycan (GAG) side chain antibodies to native chondroitin sulphate (CS), D C-4-S and C-6-S unsaturated stubs generated by chondroitinase ABC digestion of CS, keratan sulphate (KS), and with antibodies to type I, II, VI, IX and X collagens. Trans-lamellar cross bridges (TLCBs), discontinuities in annular lamellae's which provide transverse interconnections, stained prominently with toluidine blue in the adult IVDs but less so in the newborn IVDs. In adult discs TLCBs were evident in both the posterior and anterior AF where they extended from the outermost annular lamellae almost to the transitional zone extending across as many as eight lamellar layers displaying a characteristic circuitous, meandering, serpentine type course. There were significantly fewer TLCBs in 2 week-old compared with skeletally mature sheep and there was a further increase from 2 to 6 years. Immunolocalisation of perlecan delineated blood vessels in the TLBs of the newborn but not adult IVDs extending into the mid AF. In contrast adult but not 2 week-old TLCBs were immunpositive for C-4-S, C-6-S, KS, aggrecan, versican and type VI collagen. The change in number and matrix components of the translamellar cross bridges with skeletal maturity and ageing suggest that they represent an adaptation to the complex biomechanical forces occurring in the annulus fibrosus.

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Section: Discussionmentioning

confidence: 99%

Aggrecan, versican and type VI collagen are components of annular translamellar crossbridges in the intervertebral disc

et al. 2007

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“…[1][2][3][4][5][6] In addition to the skin, hyaluronan is distributed ubiquitously throughout the body, and the list of functions of intra-and extracellular hyaluronan is expanding: vision, cancer, and diŠerentiation, to name a few.…”

mentioning

confidence: 99%

Dietary Protein as a Potent Regulator of the Hyaluronan Synthase Gene in Rat Skin

Oishi

Kato

Noguchi

2003

Bioscience, Biotechnology, and Biochemistry

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“…Intact type VI isolated from bovine cartilage (13), fetal bovine skin (14), and recombinant ␣3 chain A domains (9) were reported to bind hyaluronan. Furthermore, Kielty and co-workers (15) presented evidence for hyaluronan being required as a template for the assembly of type VI collagen tetramers into filaments and for the stability of the filaments once they are formed (15).…”

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confidence: 99%

Type VI Collagen Anchors Endothelial Basement Membranes by Interacting with Type IV Collagen

Kuo

Maslen

Keene

et al. 1997

Journal of Biological Chemistry

297

215

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Type VI collagen filaments are found associated with interstitial collagen fibers, around cells, and in contact with endothelial basement membranes. To identify type VI collagen binding proteins, the amino-terminal domains of the ␣1(VI) and ␣2(VI) chains and a part of the carboxyl-terminal domain of the ␣3(VI) chain were used as bait in a yeast two-hybrid system to screen a human placenta library. Eight persistently positive clones were identified, two coding the known matrix proteins fibronectin and basement membrane type IV collagen and the rest coding new proteins. The amino-terminal domain of ␣1(VI) was shown to interact with the carboxylterminal globular domain of type IV collagen. The specificity of this interaction was further studied using the yeast two-hybrid system in a one-on-one format and confirmed by using isolated protein domains in immunoprecipitation, affinity blots, and enzyme-linked immunosorbent assay-based binding studies. Co-distribution of type VI and type IV collagens in human muscle was demonstrated using double labeling immunofluorescent microscopy and immunoelectron microscopy. The strong interaction of type VI collagen filaments with basement membrane collagen provided a possible molecular pathogenesis for the heritable disorder Bethlem myopathy.Type VI collagen filaments are ubiquitous. They are present in all connective tissues that contain type I and type III collagen fibers and in cartilage, a tissue that contains predominantly type II collagen. The major functions that have been suggested for type VI collagen filamentous networks are as a substrate for cell attachment and as an anchoring meshwork that connects collagen fibers, nerves, and blood vessels to the surrounding matrix (1, 2). This implies that not only is there an interaction, either direct or indirect, with the type I/III collagen fibers but also that there is an interaction with components of endothelial basement membranes.Matrix components that have been shown to interact with type VI collagen in vitro include proteoglycans, collagens, hyaluronan, heparin, and integrins.Proteoglycans appear to be particularly important, since cell surface-, basement membrane-, and collagen fibril-associated proteoglycans have all been reported to bind to various forms of type VI collagen. Decorin is a small dermatan sulfate proteoglycan that binds to fibrillar collagens (3). It was shown that the leucine-rich module of the core protein bound to type VI and that the binding could be inhibited by the core proteins of fibromodulin and biglycan (4). The cell surface-associated membrane chondroitin sulfate proteoglycan NG2 was originally detected in cells from the rodent central nervous system but subsequently was also detected in blood vessels and cartilaginous structures of the head, neck, and spine. It interacts via its core protein with type VI collagen and is thought to provide machinery for transmembrane signaling (5). Since ␣1␤1 and ␣2␤1 integrins also bind type VI collagen (6, 7), the cell signaling potential of this molecule woul...

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Interaction of intact type VI collagen with hyaluronan

Cited by 95 publications

References 17 publications

Aggrecan, versican and type VI collagen are components of annular translamellar crossbridges in the intervertebral disc

Aggrecan, versican and type VI collagen are components of annular translamellar crossbridges in the intervertebral disc

Dietary Protein as a Potent Regulator of the Hyaluronan Synthase Gene in Rat Skin

Type VI Collagen Anchors Endothelial Basement Membranes by Interacting with Type IV Collagen

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