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

@article{Zhang2006DecorinRA,
  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},
  year={2006},
  volume={98}
}
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… 
Decorin and biglycan are necessary for maintaining collagen fibril structure, fiber realignment, and mechanical properties of mature tendons.
  • K. Robinson, Mei Sun, +9 authors D. Birk
  • Chemistry, Medicine
    Matrix biology : journal of the International Society for Matrix Biology
  • 2017
TLDR
Structural and functional changes in response to an acute loss of decorin and biglycan expression in the mature tendon demonstrate a significant role for these SLRPs in adult tendon homeostasis.
Influence of decorin on the mechanical, compositional, and structural properties of the mouse patellar tendon.
TLDR
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
TLDR
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.
TLDR
The absence of collagen VI may alter the sequestering of regulatory molecules such as leucine rich proteoglycans and result in dysfunctional regulation of tendon fibrillogenesis indirectly mediated by collagen VI.
Collagen XII mediated cellular and extracellular mechanisms regulate establishment of tendon structure and function.
  • Y. Izu, Sheila Adams, +4 authors D. Birk
  • Medicine, Chemistry
    Matrix biology : journal of the International Society for Matrix Biology
  • 2020
TLDR
Dual roles for collagen XII in determination of tendon structure and function are indicated; intercellular communication necessary to coordinate long range order and feedback on tenocytes influencing collagen synthesis are indicated.
Coordinate roles for collagen VI and biglycan in regulating tendon collagen fibril structure and function
Highlights • Biglycan and collagen VI co-localize within nascent tendon matrix indicating possible synergy in tissue function.• Biglycan deficiency reduced tendon fibril size and mechanical
Regulation of Collagen Fibril Nucleation and Initial Fibril Assembly Involves Coordinate Interactions with Collagens V and XI in Developing Tendon*
TLDR
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
TLDR
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
TLDR
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
TLDR
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.
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References

SHOWING 1-10 OF 48 REFERENCES
Collagen fibrillogenesis in situ: Fibril segments become long fibrils as the developing tendon matures
TLDR
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
TLDR
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
TLDR
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.
TLDR
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
TLDR
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
TLDR
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*
TLDR
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
TLDR
Differential temporal and spatial expression patterns indicate that type XII collagen functions to integrate the developing tendon matrices and fascicles into a functional unit.
Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on unipolar fibrils and is regulated by collagen-proteoglycan interaction.
TLDR
The study showed that collagen fibrillogenesis is a hierarchical process that depends on the unique structure of unipolar fibrils and a novel function of proteoglycans.
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