Enzymic Control of Collagen Fibril Shape

Holmes, David; Watson, Rod B.; Chapman, John A.; Kadler, Karl E.

doi:10.1006/jmbi.1996.0443

Cited by 40 publications

(18 citation statements)

References 15 publications

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“…After completed assembly the collagen matrix covered the entire supporting surface, which could be several centimeter in diameter (Jiang et al, 2004a). The absence of self-regulation may be directly related to the absence of proteoglycans, which have been suggested to regulate the lateral fusion of Wbrils Kadler et al, 1996bKadler et al, , 2000 or to other enzymes controlling the collagen shape within organisms (Holmes et al, 1996;Myllyharju and Kivirikko, 2004). However, it has been previously shown, that under certain environmental conditions the pH and the electrolyte composition and concentration of the buVer solution can determine the spacing and width of the Wbrils as well (Jiang et al, 2004a).…”

Section: Collagen Assembly Observed By Tapping-mode Afmmentioning

confidence: 98%

Observing growth steps of collagen self-assembly by time-lapse high-resolution atomic force microscopy

Cisneros

Hung

Franz

et al. 2006

Journal of Structural Biology

146

110

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Section: Collagen Assembly Observed By Tapping-mode Afmmentioning

confidence: 98%

Observing growth steps of collagen self-assembly by time-lapse high-resolution atomic force microscopy

Cisneros

Hung

Franz

et al. 2006

Journal of Structural Biology

146

110

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“…For example, collagen I is known to be glycosylated in regions residing in the overlap domains of banded fibrils if the protein is a product of corneal, but not tendon fibroblasts. An attractive possibility of regulation of fibril morphology is that the availability of protomers by enzymatic cleavage may control fibril growth and shape [13]. However, it is not easy to see how a kinetic control can determine long-term stability of fibrillar assemblies.…”

Section: Influence Of Post-translational Processing Of Collagens On Fmentioning

confidence: 99%

Collagen Suprastructures

Birk

Brückner

2005

Topics in Current Chemistry

106

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“…The human prolysyl oxidase construct (proLOX inserted in frame with a C-terminal V5-(His) 6 tag in the pcDNA3 vector from Invitrogen) was a gift from P. Sommer (Lyon, France). XhoI and HindIII sites were used to introduce the LOX gene into the pCEP4 vector.…”

Section: Proteins-[mentioning

confidence: 99%

Substrate-specific Modulation of a Multisubstrate Proteinase

Moali

Font

Ruggiero

et al. 2005

Journal of Biological Chemistry

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Members of the bone morphogenetic protein-1/tolloid (BMP-1/Tld) family of metalloproteinases, also known as procollagen C-proteinases (PCPs), control multiple biological events (including matrix assembly, cross-linking, cell adhesion/migration and pattern formation) through enzymatic processing of several extracellular substrates. PCP activities on fibrillar procollagens can be stimulated by another family of extracellular proteins, PCP enhancers (PCPE-1, PCPE-2), which lack intrinsic enzymatic activity. While PCPs have multiple substrates, the extent to which PCPEs is involved in the processing of proteins other than fibrillar procollagens is unknown. In the experiments reported here, PCPE-1 was found to have no effect on the in vitro BMP-1 processing of procollagen VII, the procollagen V N-propeptide, the laminin 5 ␥2 chain, osteoglycin, prolysyl oxidase, or chordin. In contrast, PCPE-1 enhanced C-terminal processing of human fibrillar procollagen III but only when this substrate was in its native, disulfidebonded conformation. Surprisingly, processing of procollagen III continued to be enhanced when essentially all the triple-helical region was removed. These and previous results (Ricard-Blum, S., Bernocco, S., Font, B., Moali, C., Eichenberger, D., Farjanel, J., Burchardt, E. R., van der Rest, M., Kessler, E., and Hulmes, D. J. S. In recent years, it has become clear that members of the tolloid family of metalloproteinases (BMP-1, 1 mTld, mTLL-1, mTLL-2) are key players in morphogenesis through their ability to control and synchronize the processing of multiple extracellular substrates (1-25). Also called procollagen C-proteinases, tolloid proteinases trigger collagen fibril formation in the extracellular matrix (26) by cleaving the C-propeptide regions from the major fibrillar procollagens (I, II, and III). They are also involved in precursor processing of the minor fibrillar collagens V and XI, necessary for the regulation of heterotypic fibril assembly, in both the N-and C-propeptide regions (8,15,17,19,23,27). Tolloid proteinases also cleave precursor forms of small leucine-rich proteoglycans such as biglycan (13) and osteoglycin (24). While some of these proteoglycans have been shown to modulate the kinetics of assembly as well as fibril diameter (28), functional differences between mature and precursor forms are not yet clearly established (24). Biglycan is also important for bone formation (29) and more recently, dentin matrix protein-1, a protein involved in mineralization, has been found to be a substrate for tolloid proteinases (22).Another important function early attributed to tolloid proteinases is the maturation of the precursor form of lysyl oxidase (LOX) (5, 30), the enzyme responsible for the stabilization of collagen and elastin networks through the formation of covalent cross-links. This tolloid-dependent processing has recently gained in significance with the demonstration that the cleaved propeptide of proLOX accounts for the ras-recision gene activity of this protein (31). In addition, ...

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Enzymic Control of Collagen Fibril Shape

Cited by 40 publications

References 15 publications

Observing growth steps of collagen self-assembly by time-lapse high-resolution atomic force microscopy

Observing growth steps of collagen self-assembly by time-lapse high-resolution atomic force microscopy

Collagen Suprastructures

Substrate-specific Modulation of a Multisubstrate Proteinase

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