The location of three collagen types in skeletal muscle

Duance, Victor Colin; Restall, D. J.; Beard, Helen; Bourne, F.J.; Bailey, Allen J.

doi:10.1016/0014-5793(77)80797-7

Cited by 225 publications

(81 citation statements)

References 9 publications

(9 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In immunofluorescence of mouse skeletal muscle both type III procollagen (fig3a), flbronectin (fig3b) and type IV collagen ( fig.3c) but no type I procollagen (fIg.3d) were seen in the endomysium. Similar data have been reported on bovine muscle [27]. The biosynthetic data presented here suggests that the muscle cells themselves may produce components of the endomysium.…”

Section: Resultssupporting

confidence: 89%

Type III procollagen is the major collageneous component produced by a continuous rhabdomyosarcoma cell line

et al. 1979

View full text Add to dashboard Cite

Section: Resultssupporting

confidence: 89%

Type III procollagen is the major collageneous component produced by a continuous rhabdomyosarcoma cell line

et al. 1979

View full text Add to dashboard Cite

“…In normal tendon, most type III collagen is found in the endotenon and epitenon (Ref. 48), although it is also found intercalated into the type I collagen fibril bundles, particularly in ageing tendons and at the insertion (Ref. 49).…”

Section: The Molecular Composition Of Tendonmentioning

confidence: 99%

Chronic tendon pathology: molecular basis and therapeutic implications

Riley

2005

Expert Rev. Mol. Med.

103

View full text Add to dashboard Cite

Tendons are frequently affected by chronic pain or rupture. Many causative factors have been implicated in the pathology, which until relatively recently was under-researched and poorly understood. There is now a greater knowledge of the molecular basis of tendon disease. Most tendon pathology (tendinopathy) is associated with degeneration, which is thought to be an active, cell-mediated process involving increased turnover and remodelling of the tendon extracellular matrix. Degradation of the tendon matrix is mediated by a variety of metalloproteinase enzymes, including matrix metalloproteinases and 'aggrecanases'. Neuropeptides and other factors released by stimulated cells or nerve endings in or around the tendon might influence matrix turnover, and could provide novel targets for therapeutic intervention.Tendons are dense, fibrous connective tissues that connect muscle to bone and are essential for the transmission of force and the generation of movement at a joint. They are highly ordered composite materials consisting of collagens, proteoglycans and various glycoproteins, many of which have been poorly characterised. Tendon problems such as tendon rupture and chronic tendon pain are common, although the underlying pathology is not well understood and the conditions are often difficult to treat (Ref.

show abstract

“…The solubilized collagens were then separated by the salt fractionation technique in [6,10]. The 2 M NaCl precipitate was subjected to the thermal gelation technique [ 1 l] to remove the contaminating type I and type III fibres.…”

Section: L Pepsin Digestionmentioning

confidence: 99%

“…The preparation of ~tibodies in rabbits, the ~muno~uores~ent staining, and the passive haemagglutination techniques were carried out as detailed in [6].…”

Section: Antibody Productionmentioning

confidence: 99%