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Collagen ( / ˈkɒlədʒən /) is the main structural protein in the extracellular matrix found in the body's various connective tissues. As the main component of connective tissue, it is the most abundant protein in mammals, [1] making up from 25% to 35% of the whole-body protein content.
Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates.
Contents. hide. (Top) See also. References. External links. Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage.
Type III collagen is one of the fibrillar collagens whose proteins have a long, inflexible, triple-helical domain. [5] Protein structure and function. Type III collagen is synthesized by cells as a pre-procollagen. [6] The signal peptide is cleaved off producing a procollagen molecule.
Clinical significance. References. Plasma proteins, sometimes referred to as blood proteins, are proteins present in blood plasma. They serve many different functions, including transport of lipids, hormones, vitamins and minerals in activity and functioning of the immune system.
Methicillin-resistant Staphylococcus aureus (MRSA, often pronounced / ˈmɜːrsə / or / ɛm ɑːr ɛs eɪ / ), is one of a number of greatly feared strains of S. aureus which have become resistant to most β-lactam antibiotics. For this reason, vancomycin, a glycopeptide antibiotic, is commonly used to combat MRSA.
Collagen. Hydroxyproline is a major component of the protein collagen, [3] comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5]
