Collagen Suprastructures

Birk, David E.; Brückner, Peter

doi:10.1007/b103823

Cited by 106 publications

(94 citation statements)

References 63 publications

(82 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In addition, variations in ECM composition likewise have a profound effect on the biomechanical properties of a tissue. 66 For instance, collagen and elastin fibers are the main structural components in pulmonary connective tissue, but their elastic properties are substantially different. The elastic modulus of collagen fibrils is in the range of 1200 MPa, whereas the elastic modulus of elastin is closer to 1 MPa.…”

Section: Cellular Response To Ecm Stiffness During Disease Progressionmentioning

confidence: 99%

Tissue Stiffness Dictates Development, Homeostasis, and Disease Progression

et al. 2015

View full text Add to dashboard Cite

ABSTRACT. Tissue development is orchestrated by the coordinated activities of both chemical and physical regulators. While much attention has been given to the role that chemical regulators play in driving development, researchers have recently begun to elucidate the important role that the mechanical properties of the extracellular environment play. For instance, the stiffness of the extracellular environment has a role in orienting cell division, maintaining tissue boundaries, directing cell migration, and driving differentiation. In addition, extracellular matrix stiffness is important for maintaining normal tissue homeostasis, and when matrix mechanics become imbalanced, disease progression may ensue. In this article, we will review the important role that matrix stiffness plays in dictating cell behavior during development, tissue homeostasis, and disease progression.

show abstract

Section: Cellular Response To Ecm Stiffness During Disease Progressionmentioning

confidence: 99%

Tissue Stiffness Dictates Development, Homeostasis, and Disease Progression

et al. 2015

View full text Add to dashboard Cite

show abstract

“…The intermediates undergo linear growth to generate mature fibrils, but no lateral growth. These later steps involve SLRP interactions with stromal collagen fibrils (9,(17)(18)(19). These structural features are essential for corneal transparency.…”

mentioning

confidence: 99%

Genetic Evidence for the Coordinated Regulation of Collagen Fibrillogenesis in the Cornea by Decorin and Biglycan

Zhang

Chen

Goldoni

et al. 2009

Journal of Biological Chemistry

Self Cite

188

177

View full text Add to dashboard Cite

Decorin and biglycan are class I small leucine-rich proteoglycans (SLRPs) involved in regulation of collagen fibril and matrix assembly. We hypothesize that tissue-specific matrix assembly, such as in the cornea, requires a coordinate regulation involving multiple SLRPs. To this end, we investigated the expression of decorin and biglycan in the cornea of mice deficient in either SLRP gene and in double-mutant mice. Decorin and biglycan exhibited overlapping spatial expression patterns throughout the corneal stroma with differential temporal expression. Whereas decorin was expressed at relatively high levels in all developmental stages, biglycan expression was high early, decreased during development, and was present at very low levels in the mature cornea. Ultrastructural analyses demonstrated comparable fibril structure in the decorin-and biglycan-null corneas compared with wild-type controls. We found a compensatory up-regulation of biglycan gene expression in the decorindeficient mice, but not the reverse. Notably, the corneas of compound decorin/biglycan-null mice showed severe disruption in fibril structure and organization, especially affecting the posterior corneal regions, corroborating the idea that biglycan compensates for the loss of decorin. Fibrillogenesis assays using recombinant decorin and biglycan confirmed a functional compensation, with both having similar effects at high SLRP/collagen ratios. However, at low ratios decorin was a more efficient regulator. The use of proteoglycan or protein core yielded comparable results. These findings provide firm genetic evidence for an interaction of decorin and biglycan during corneal development and further suggest that decorin has a primary role in regulating fibril assembly, a function that can be fine-tuned by biglycan during early development.The characteristic architecture of different connective tissues is established through tissue-specific regulation of collagen fibrillogenesis and matrix assembly. Multiple steps are involved in collagen fibrillogenesis, including the nucleation of collagen assembly, assembly of immature fibril intermediates, and linear and lateral fibril growth of preformed intermediates (1-5). Each step is independently regulated through interactions of extracellular macromolecules with fibrils. Heterotypic interactions involving different fibril-forming collagens regulate fibril nucleation during development (1, 6). In contrast, interactions involving fibrils and small leucine-rich proteoglycans (SLRPs) 2 are implicated in the regulation of linear and lateral growth of mature fibrils from preformed intermediates (5, 7-10). The focus of this work is to elucidate the differential regulatory role(s) of decorin and biglycan in fibrillogenesis.SLRPs compose a family of five classes of structurally related, but genetically distinct molecules. The members within each class exhibit high protein homology and primary structure identity (11). Decorin and biglycan are class I SLRPs; and fibromodulin, keratocan, and lumican are class II ...

show abstract

“…43 The triple helical regions of collagens are comprised of tandem repeats of Gly-Xaa-Yaa tripeptide units. Isolated polyproline-II helices are not stable if the polypeptide chains also incorporate residues other than proline and hydroxyproline, 31,[44][45][46][47] and therefore these hydrogen bonds have a major contribution to the stability of triple helix peptides. It should be noted that the right-handed a-helices with left-handed polyproline-II helices are relatively rare structural elements in proteins with the striking exception of collagens.…”

Section: Conformation Of Triple Helix Peptides From Collagenmentioning

confidence: 99%