Type VI collagen in mouse masseter tendon, from osseous attachment to myotendinous junction

Senga, Katsuhiro; Kobayashi, Miya; Hattori, Hiroyuki; Yasue, Kazuki; Mizutani, Hideki; Hoshino, Takao

doi:10.1002/ar.1092430303

Cited by 31 publications

(14 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It was speculated that Bethlem myopathy may also be caused by a disturbance of a type VI/laminin interaction (18), but our results (not shown) and those of others show that there is no interaction between type VI and laminin (49). However, type VI collagen is associated with the external lamina of muscle cells in the myotendinous junction (50), and this study demonstrates a co-distribution of type VI and type IV collagens in human skeletal muscle. These studies have demonstrated a direct protein/protein interaction of type VI collagen with basement membrane type IV collagen, indicating that type VI filaments provide a physical link between endothelial basement membranes and the surrounding matrix.…”

Section: Discussioncontrasting

confidence: 51%

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

Kuo

Maslen

Keene

et al. 1997

Journal of Biological Chemistry

299

215

View full text Add to dashboard Cite

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...

show abstract

Section: Discussioncontrasting

confidence: 51%

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

Kuo

Maslen

Keene

et al. 1997

Journal of Biological Chemistry

299

215

View full text Add to dashboard Cite

show abstract

“…This would suggest a disruption of the normal interconnecting meshwork between the cell and its pericellular matrix. While immunolocalization for Type VI collagen was not performed in the current study, previous investigations using electron microscopy have identified this loosely bound, fine, fibrillar material as Type VI collagen [43,51]. Additional studies are required to confirm that the material observed in our stress-deprived system is Type VI collagen.…”

Section: Discussionmentioning

confidence: 73%

Loss of Homeostatic Strain Alters Mechanostat “Set Point” of Tendon Cells In Vitro

Arnoczky

Lavagnino

Egerbacher

et al. 2008

Clinical Orthopaedics &Amp; Related Research

View full text Add to dashboard Cite

Tendon cells respond to mechanical loads. The character (anabolic or catabolic) and sensitivity of this response is determined by the mechanostat set point of the cell, which is governed by the cytoskeleton and its interaction with the extracellular matrix. To determine if loss of cytoskeletal tension following stress deprivation decreases the mechanoresponsiveness of tendon cells, we cultured rat tail tendons under stress-deprived conditions for 48 hours and then cyclically loaded them for 24 hours at 1%, 3%, or 6% strain at 0.17 Hz. Stress deprivation upregulated MMP-13 mRNA expression and caused progressive loss of cellmatrix contact compared to fresh controls. The application of 1% strain to fresh tendons for 24 hours inhibited MMP-13 mRNA expression compared to stress-deprived tendons over the same period. However, when tendons were stressdeprived for 48 hours and then subjected to the same loading regime, the inhibition of MMP-13 mRNA expression was decreased. In stress-deprived tendons, it was necessary to increase the strain magnitude to 3% to achieve the same level of MMP-13 mRNA inhibition seen in fresh tendons exercised at 1% strain. The data suggest loss of cytoskeletal tension alters the mechanostat set point and decreases the mechanoresponsiveness of tendon cells.

show abstract

“…Given its morphology and distribution in tendons, it has been attributed an integrative function, organizing collagen fibers and linking them to the cells (Bruns et al 1986). Type VI collagen has been found in the osseous attachment to the myotendinous junction of the masseter tendon (Senga et al 1995), and spatial interactions of type VI collagen, small proteoglycans, and collagen fibrils have been observed in tendons (Watanabe et al 1997). Nurminskaya and Birk (1998) have shown that type VI collagen is expressed after the fibrillogenesis phase.…”

Section: Introductionmentioning

confidence: 99%

Identification, content, and distribution of type VI collagen in bovine tendons

Carvalho

Felisbino

Keene³

et al. 2006

Cell Tissue Res

View full text Add to dashboard Cite

Tendon composition changes according to differentiation, mechanical load, and aging. In this study, we attempted to identify, localize, and quantify type VI collagen in bovine tendons. Type VI collagen was identified by the electrophoretic behavior of the alpha chains and Western blotting, and by rotary shadowing. Type VI collagen was extracted from powdered tendon with three sequential 24-h extractions with 4 M guanidine-HCl. The amount of type VI collagen was determined by enzyme-linked immunosorbent assay for purely tensional areas and for the compressive fibrocartilage regions of the deep flexor tendon of the digits, for the corresponding fetal and calf tendons, and for the extensor digital tendon. The distal fibrocartilaginous region of the adult tendon was richer in type VI collagen than the tensional area, reaching as much as 3.3 mg/g (0.33%) of the wet weight. Calf tendons showed an accumulation of type VI at the fibrocartilage site. Immunocytochemistry demonstrated that type VI collagen was evenly distributed in the tensional areas of tendons but was highly concentrated around the fibrochondrocytes in the fibrocartilages. The results demonstrate that tendons are variable with regard to the presence and distribution of type VI collagen. The early accumulation of type VI collagen in the region of calf tendon that will become fibrocartilage in the adult suggests that it is a good marker of fibrocartilage differentiation. Furthermore, the distribution of type VI collagen in tendon fibrocartilage indicates that it organizes the pericellular environment and may represent a survival factor for these cells.

show abstract

Type VI collagen in mouse masseter tendon, from osseous attachment to myotendinous junction

Abstract: The distribution of type VI collagen in mouse masseter tendon is different in different anatomical position. This may reflect the different functional demand for this collagen.

Cited by 31 publications

References 27 publications

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

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

Loss of Homeostatic Strain Alters Mechanostat “Set Point” of Tendon Cells In Vitro

Identification, content, and distribution of type VI collagen in bovine tendons

Contact Info

Product

Resources

About