Low-Density Lipoprotein Receptor–Related Protein 5–Deficient Rats Have Reduced Bone Mass and Abnormal Development of the Retinal Vasculature

Humans carrying homozygous loss-of-function mutations in the Wnt co-receptor, low-density lipoprotein receptor–related protein 5 (LRP5), develop osteoporosis and a defective retinal vasculature known as familial exudative vitreoretinopathy (FEVR) due to disruption of the Wnt signaling pathway.

Diabetic Conditions Confer Metabolic and Structural Modifications to Tissue-Engineered Skeletal Muscle

Skeletal muscle is a tissue that is directly involved in the progression and persistence of type 2 diabetes (T2D), a disease that is becoming increasingly common. Gaining better insight into the mechanisms that are affecting skeletal muscle dysfunction in the context of T2D has the potential to lead to novel treatments for a large number of patients.

Comparison of Dehydrated Human Amnion-Chorion and Type 1 Bovine Collagen Membranes in Alveolar Ridge Preservation: A Clinical and Histological Study

Alveolar ridge preservation maintains ridge dimensions and bone quality for implant placement. The aim of this randomized controlled clinical study is to compare the use of a human amnion-chorion membrane to a collagen membrane in an exposed-barrier ridge preservation technique. Furthermore, this study will determine if intentional membrane exposure compromises ridge dimensions and bone vitality. Forty-three patients requiring extraction and delayed implant placement were randomly assigned into either the experimental or control group.

Force dependent effects of chronic overuse on fibrosis-related genes and proteins in skeletal muscles

Of eight fibrosis-related mRNAs examined, only FGF2 demonstrated a consistent significant increase in the HFHR group, compared to the FRC group. However, protein amounts of collagen type 1, collagen type 3, and TGFβ1 were significantly higher in the HFHR, compared to the FRC and LFHR groups, while CCN2 and FGF2 were higher in both HFHR and LFHR, compared to the FRC group.

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

Tendons have a uniaxially aligned structure with a hierarchical organization of collagen fibrils crucial for tendon function. Collagen XII is expressed in tendons and has been implicated in the regulation of fibrillogenesis. It is a non-fibrillar collagen belonging to the Fibril-Associated Collagens with Interrupted Triple Helices (FACIT) family.