Function of collagen
collagen serve in To a significant degree within body for the preservation of The tissue and organs are structurally integrity, It’s real For all parenchymal organs in which they are the Big part of Matrix “interstitial” Including the membranes of the cellar, It is all the more important Obvious to all “connective” tissues, and particularly Bone and cartilage, of which collagen is the dominant Functional Structural Backbone, What’s more, the Defined pericellular micro environnement formation Is essential for the integrity of cells, as seen with Collagen VI but possibly also in articular cartilage and In bone (own undisclosed sighting) , Alongside the Most biomechanical elements are also collagens Involved in a variety of other roles,Specifications Receptors mediate collagen interactions, as Integrins, receptors witha discoidin domain, glycoprotein VI or advanced receptors for proteoglycines (5).
Such receptor signals identify adhesion, differentiation , growth, cellular reactivity and the Cell survival in many ways ,Collagens contribute to clogging, local storeage and availability of growth and cytokine factors and Therefore, perform important roles during development of the organ-Task, healing wounds and restoring tissue(6).
Type I collagen has been shown to bind the furniture and Therefore, it may
indirectly block TGF-h-action within Tissue, Tissue Collagens bind a number of others too Factors of development, and cytokines, IGF-I and -II, then are Bonded to the bone collagen matrix and thus bone is a big source of this growth Factors intrinsic to the body(7).
Degradation, in the bone Osteoclasts collagen network during bone Remodelling is considered to release matrix-bound IGFs And therefore, through stimulation, cause
new bone formation osteoblastic operation tion in paracrine shape, Specific effects on articular cartilage can be involved and Can be attributed to anabolizing chondrocyte activation Binding growth factors after cartilage release Degraded matrix, Collagen Type IIA was recently published Shown that TGFh and BMP-2 can be binding (8).
Therefore, collagen is most likely important for Many cellular reactions, That collagen potential These qualify to bind growth factors and cytokines Molecules, function as medical transport vehicles Factor delivery (9).
Disease associated with collagen
“Vascular collagen disease” is the name of a group of diseases affecting your
connective tissue , Vascular collagen disorder is an autoimmune disease, That
means your immune system is wrongly attacking the healthy tissue of your body,
No one knows what causes you to do this in the immune system, Sometimes, the attacks cause inflammation, If you have a vascular collagen disorder, your immune system causes inflammation of your collagen and nearby joints .
Some disorders that are classified as vascular collagen disorder affect your joints, skin, blood vessels, or other vital organs, Symptoms differ by particular disease.
Types of vascular disease include
Lupus Normally the immune system battles harmful viruses and bacteria in order to keep the body safe, When the immune system attacks the body, an autoimmune disease occurs, because it confuses it for something foreign.
is an autoimmune condition which can cause joint pain and damage in your entire body,
The joint damage caused by RA usually occurs at both sides of the body, And if a joint in one of the arms or legs is affected, the same joint in the other arm or leg is likely to be affected too ,This is one way doctors distinguish RA from other forms of arthritis, such as OA.
Systemic sclerosis (SS)
is an autoimmune disease, That means it’s a condition in which the body is attacked by the immune system ,Healthy tissue is damaged because, wrongly, the immune system believes it’s a foreign material or virus, There are several types of autoimmune disorders which can affect various systems of the body ,SS is distinguished by changes in skin texture and appearance , Increase in collagen production can occur this.
is a condition in which temporal arteries are inflamed or damaged which supply blood to the head and brain, It is also known as cranial arteritis, or arteritis of giant cells, While this disorder typically occurs in temporal arteries, it can occur in the body in nearly any medium to broad artery.
Types of hereditary collagen disease include
Ehlers-Danlos syndrome (EDS) is a
condition inherited which affects the body’s connective tissues.
Marfan syndrome is a connective tissue disorder inherited which affects normal
growth of the body, Connective tissue helps your bone system, and all the body’s organs.
Brittle bone disease is a disorder that leads to fragile bones breaking down easily.
It is usually present at birth but it only occurs in children who have a history of the disease in their family(10).
The role of vitamin c in collagen biosynthesis
Intracellular events involve Endoplasmic Protein Synthesis Three polypeptide
chains which make up the reticulum Protocollagen, is hydroxylated to form
procollagen, Which is glycosylated at reticulum endoplasm, degree of
hydroxylation of the lysine residue is essential in that it will Determine the number of cross-connections and hence the frequency of the Collagen, Until secretion, procollagen is transformed in a triple helix Procollagen helices are actually longer from cell by microtubules than amino-terminal and carboxy collagen molecules ,Terminal end pieces which keep collagen soluble in the cell, The intracellular processes need more than eight enzymes, leading to the production of More than 150 changes in each chain and one-tenth of changes Its amino acids, Collagen is produced by fibroblasts, which are skin cells specialized in the dermis, Fibroblasts
also give rise to Many structural proteins in the skin, such as elastin (a protein that
gives The skin has a snap-back capability) and glucosaminoglycans (GAGs), GAGs constitute the ground substance which holds the dermis Quite hydrated.
When the receptor is bound by the correct combination Signal molecules (called growth factors for fibroblasts or FGFs), The synthesis of collagen commences with
fibroblast, Initially fibroblasts Produce small subunits of collagen, called
procollagen , These are carried out from the fibroblast cells and then entered later
Together, to form a complete molecule of collagen,
Vitamin C is a part of In several stages of the cycle a cofactor, Without enough
The vitamin C levels, the production of collagen, are interrupted, Disturbance It
contributes to a number of illnesses, such as scurvy-an illness in which the disease The body can’t produce collagen, and therefore, It simply falls apart When these supporting (collagen) structures deteriorate.
Collagen protein needs hydroxylation by vitamin C, which is a process Which
gives the molecule the best possible structure and Impedes poor collagen and is vulnerable to damage .
In fact , there is evidence of vitamin C Rises the procollagen messenger RNA point, Collagen Coatings Subunits are shaped as procollagen within the fibroblasts Excreted in extracellular spaces Vitamin C is required for export The molecules out of the cell are procollagenm Synthesis of collagen forms Continuously fix and restore damaged over our lives Collagen tissue, or new structures of cells ,The Kill Recycling old or damaged collagen is a healthy , natural advantage ,Cessation used to build protein fragments required for new cellular construction , Structures, for example in healing process.
Collagen levels with age Decay due to reduced production and
increased degradation Date(11).
All 16 collagen forms contain a Gly-Pro-X repeat sequence and fold into a typical
The different collagens are distinguished by the ability of their helical and nonhelical regions to interact into fibrils, form sheets, or cross-link different forms of collagen. Most collagen is fibrillar and consists of type I molecules, the basal lamina is unique to a two-dimensional type IV collagen network.
Fibrous collagen molecules (e.g., types I, II , and III) are assembled into fibrils which are stabilized by covalent cross-links of aldol.
Procollagen chains in the ER are modified and assembled to form a triple helix. Helix formation is assisted by N- and C-terminal propeptide disulfide bonds which align the polypeptide chains in the register.
In general, after secretion the propeptides are removed, and then collagen fibrils form in the extracellular space.
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