Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development

  title={Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development},
  author={Guiyun Zhang and Yoichi Ezura and Inna Chervoneva and Paul S. Robinson and David P. Beason and Ehren T. Carine and Louis J Soslowsky and Renato V. Iozzo and David E. Birk},
  journal={Journal of Cellular Biochemistry},
Tendon function involves the development of an organized hierarchy of collagen fibrils. Small leucine‐rich proteoglycans have been implicated in the regulation of fibrillogenesis and decorin is the prototypic member of this family. Decorin‐deficient mice demonstrate altered fibril structure and mechanical function in mature skin and tail tendons. However, the developmental role(s) of decorin needs to be elucidated. To define these role(s) during tendon development, tendons (flexor digitorum… 

Biglycan has a major role in maintenance of mature tendon mechanics

The extensive changes to tendon structure and mechanics after knockdown of bigly can, but not decorin, provides evidence that biglycan plays a major role in the maintenance of tendon structureand mechanics in mature mice during homeostasis.

Influence of decorin on the mechanical, compositional, and structural properties of the mouse patellar tendon.

Decorin, a member of the SLRP family, plays a role in tendon viscoelasticity that cannot be completely explained by its role in collagen fibrillogenesis, suggesting that other factors contribute to these properties.

Pericellular Proteins of the Developing Mouse Tendon: A Proteomic Analysis

An unbiased set of cell surface-associated molecules are generated, providing a resource to identify novel or unexpected regulatory molecules involved in collagen fibril and matrix assembly.

Dysfunctional tendon collagen fibrillogenesis in collagen VI null mice.

Collagen XII mediated cellular and extracellular mechanisms regulate establishment of tendon structure and function.

Regulation of Collagen Fibril Nucleation and Initial Fibril Assembly Involves Coordinate Interactions with Collagens V and XI in Developing Tendon*

The data demonstrate coordinate roles for collagens V and XI in the regulation of fibril nucleation and assembly during tendon development and suggest roles for other related molecules.

Collagen V expression is crucial in regional development of the supraspinatus tendon

It is demonstrated that collagen V plays a crucial role in determining region‐specific differences in mouse supraspinatus tendon structure as well as in cell density and PYD content.

Relationships Between Decorin and Biglycan, Structure and Tendon Mechanics Using Mutant Mouse Models

Complex interactions between SLRPs and collagen were present in all models and demonstrate the importance of considering the amounts of other components in the tissue when examining structure-function relationships and suggest that decorin and biglycan play a role in tendon viscoelasticity.

The Tendon Injury Response is Influenced by Decorin and Biglycan

Results suggest that biglycan and decorin may have sequential roles in the tendon response to injury, and SLRP deficiency influenced the mechanical properties with a marked lack of improvement between 3 and 6 weeks in decorin-null tendons.

Decorin expression is important for age-related changes in tendon structure and mechanical properties.




Collagen fibrillogenesis in situ: Fibril segments become long fibrils as the developing tendon matures

The increase in fibril length is interpreted as being the result of a post‐depositional, regulated assembly of segments via a lateral association/fusion to form mature fibrils and predicts an increase in diameter at this stage of development.

Development of tendon structure and function: regulation of collagen fibrillogenesis.

In the tendon, the development of mature mechanical properties is dependent on the assembly of a tendon-specific extracellular matrix. This matrix is synthesized by the tendon fibroblasts and

Differential Expression of Lumican and Fibromodulin Regulate Collagen Fibrillogenesis in Developing Mouse Tendons

It is indicated that lumican and fibromodulin have different developmental stage and leucine-rich repeat protein specific functions in the regulation of fibrillogenesis.

Collagen fibrillogenesis in situ: Fibril segments undergo post‐depositional modifications resulting in linear and lateral growth during matrix development

The hypothesis that a decrease in fibril‐associated decorin is necessary for fibrils growth associated with tissue maturation is supported by the morphological data.

Influence of decorin and biglycan on mechanical properties of multiple tendons in knockout mice.

Results give mechanical support to previous biochemical data that tendons likely are uniquely tailored to their specific location and function and need to be further characterized and taken into account when designing therapies or replacements.

Abnormal collagen fibrils in tendons of biglycan/fibromodulin‐deficient mice lead to gait impairment, ectopic ossification, and osteoarthritis

It is shown that collagen fibrils in tendons from mice deficient in biglycan and/or fibromodulin are structurally and mechanically altered resulting in unstable joints and mutations in SLRPs may predispose to osteoarthritis.

Targeted Disruption of Decorin Leads to Abnormal Collagen Fibril Morphology and Skin Fragility

A fundamental role is demonstrated for decorin in regulating collagen fiber formation in vivo in mice harboring a targeted disruption of the decorin gene, which provides an explanation for the reduced tensile strength of the skin.

Fibromodulin-null Mice Have Abnormal Collagen Fibrils, Tissue Organization, and Altered Lumican Deposition in Tendon*

A role for fibromodulin is demonstrated in collagen fibrillogenesis and it is suggested that the orchestrated action of several leucine-rich repeat glycoproteins/proteoglycans influence the architecture of collagen matrices.

Differential expression of type XII collagen in developing chicken metatarsal tendons

Differential temporal and spatial expression patterns indicate that type XII collagen functions to integrate the developing tendon matrices and fascicles into a functional unit.

Investigating Tendon Fascicle Structure–Function Relationships in a Transgenic-Age Mouse Model Using Multiple Regression Models

Interestingly, glycosaminoglycan (GAG) content was observed to be the strongest predictor of mechanical properties, perhaps both through direct influence and indirectly through its correlation with collagen content and fibril structure.