COLLAGEN France
120 Capsules
750 mg
Collagen is a group of naturally occurring proteins.
In nature, it is found exclusively in animals, especially in the flesh and connective tissues of mammals. It is the main component of connective tissue, and is the most abundant protein in mammals, making up about 25% to 35% of the whole-body protein content.
Collagen, in the form of elongated fibrils, is mostly found in fibrous tissues such as tendon, ligament and skin, and is also abundant in cornea, cartilage, bone, blood vessels, the gut, and intervertebral disc.
In muscle tissue it serves as a major component of endomysium.
Collagen constitutes 1% to 2% of muscle tissue, and accounts for 6% of the weight of strong, tendinous muscles. Gelatin, which is used in food and industry, is collagen that has been irreversibly hydrolyzed.
The molecular and packing structures of collagen have eluded scientists over decades of research. The first evidence that it possesses a regular structure at the molecular level was presented in the mid-1930s.
Since that time many prominent scholars, including Nobel laureates Crick, Pauling, Rich and Yonath and others including Brodsky, Berman, and Ramachandran, concentrated on the conformation of the collagen monomer.
Several competing models, although correctly dealing with the conformation of each individual peptide chain, gave way to the triple-helical โMadrasโ model which provided an essentially correct model of the moleculeโs quaternary structure although this model still required some refinement.
The packing structure of collagen has not been defined to the same degree outside of the fibrillar collagen types, although it has been long known to be hexagonal โฆor quasi-hexagonal.
As with its monomeric structure, several conflicting models alleged that either the packing arrangement of collagen molecules is โsheet-likeโ or microfibrillar. The microfibrillar structure of collagen fibrils in tendon, cornea and cartilage has been directly imaged by electron microscopy.
In 2006, it was confirmed that the microfibrillar structure of adult tendon as described by Fraser, Miller, Wess (amongst others) was closest to the observed structure, although it over-simplified the topological progression of neighboring collagen molecules and hence did not predict the correct conformation of the discontinuous D-periodic pentameric arrangement termed simply: the microfibril.
Further Reading
- Collagen Molecular Structure
- Collagen Fibrillar Structure
- Collagen Types and Linked Disorders
- Collagen Synthesis
- Collagen Uses
- Collagen Medical Uses
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Recent Collagen News
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- Cathepsins may attack one another instead of the bodily proteinsResearchers for the first time have shown that members of a family of enzymes known as cathepsins โ which are implicated in many disease processes โ may attack one another instead of the bodily proteiโฆ
- Scientists identify key factor that drives resistance to cancer drugDeveloping resistance to chemotherapy is a nearly universal, ultimately lethal consequence for cancer patients with solid tumors โ such as those of the breast, prostate, lung and colon โ that have metโฆ
- FibroGen receives FDA Orphan Drug Designation for FG-3019 to treat IPFFibroGen, Inc., today announced that FG-3019, the Companyโs human monoclonal antibody against connective tissue growth factor (CTGF), has been granted Orphan Drug Designation by the U.S. Food and Drugโฆ
- Burn wound MSCs potential source for skin graftingStudy findings suggest that burn wound eschar-derived mesenchymal cells represent a population of multipotent stem cells, which could be a new resource for engineering approaches to heal burn wounds.
