The Importance Of The Extracellular Matrix

Protein is obviously what everyone’s body part is made up of protein and so the fibrous tissue which is result to healing if low protein this tissue is not synthesized and high protein can increase it rates. Carbohydrates, as they are provide the main structural materials required for growth, repair, and maintenance of tissue. A&P 9th ed. Pg.50

58) Connective tissues that possess a large quantity of collagen fibers often provide the framework for organs such

Skin repair is an important physiological process which is essential for homeostasis, restoring barrier function and preventing infection (Martin, 2009; Boateng and Catanzano, 2015). Wound healing is defined as a complex, dynamic and the specific biological process associated with the phenomena of tissue regeneration and growth (Mazumder et al., 2016). Regeneration can be defined as a tissue that significantly damaged either completely or partially removed and tissue's original function and cell types must be functional and structurally restored (Mazumder et al., 2016). The process of healing comprises a cytokine, blood cells, extracellular matrix and growth factor (Joao De Masi et al., 2016). The growth factor is a protein that activates and

The second type of tissue found in the body is connective tissue. They lie beneath the epithelial tissue helping to connect different part of the internal structure, the cells are more widely separated from each other then in epithelial tissue. The intercellular substance known as the matrix is found in considerably large amounts. Within the matrix there are usually fibres which may be a jelly like consistency or dense and rigid depending on the type, function and positioning of the tissue. Theses fibres form a supporting system for cells to attach to. The major functions of connective tissue are to transport materials, give structural support and protection. The types of connective tissue that will be explained are blood, bone, cartilage, bone, areolar tissue and adipose tissue.

Integra is a synthetic wound dressing frequently used to treat burn wounds (Figure 5). It is a bilayer composed of bovine tendon collagen glycosaminoglycan (chondroitin-6-sulphate) cross-linked to it, onto which a silicone (synthetic polysiloxane polymer) membrane is sealed to the upper surface to act as a protective temporary epidermis. The silicone layer is applied as a liquid monomer; curing occurs on the surface of the collagen at room temperature. It serves to control moisture loss from the wound. Water flux across this silicone membrane is the same as that across normal epidermis. The collagen-GAG matrix contains pores ranging from 70 to 200 µm that are invaded by host fibroblasts upon application to an excised wound bed. The pore size was carefully designed by adjusting the collagen-GAG mixture. In GAG-free collagen, the resulting structure was more closed than in collagen-GAG matrices. Smaller pores can delay, or even prevent, biointegration, whereas larger pores would provide an insufficient attachment area for invading host cells. Freeze-drying procedures followed by slow sublimation are used to control pore size too. The degradation rate of 30 days of the collagen-GAG sponge is controlled by glutaraldehyde-induced cross-links. The polypeptide collagen is used for its low levels of antigenicity (it has minimal rejection potential) and because it exerts a hemostatic effect on vascular wounds. Collagen is already found in skin. It is degraded by collagenase deposited

Proliferative phase occurs within a few days of injury in which cells that were involved in the battle need to tend to their wounds and the regenerate to restore itself to its formal glory as best as possible. The body’s way of restoring itself is through use of angiogenesis, granulation tissue formation, wound contraction and epithelialization. This combination acts of getting new blood vessels to the damage area, aid in the formation of cells to fill in the area which leads to scar tissue, allow the skin to flexible in the repair process and finally resurface the wound with new epithelial

This paper will be a research critique on the article “Frequent Application of the New Gelatin-Collagen Nonwoven Accelerates Wound Healing”, by Schiefer, J.L. and Rath, R, and each section will be examined using our textbook “Understanding Evidence-Based Practice”. The article’s main focus was on determining the effect of healing when using multiple collagen nonwoven applications to chronic wounds. Twelve mini-pigs where used to test this technique and the findings indicated that this method was promising, because the wounds had a faster healing rate when multiple application of gelatin-collagen nonwoven was used as treatment. Analyzing the articles components, we can see that although it does contain preliminary

The muscles and the sensory organs also show changes such as shrinkage of cells, thickening

They include keratin found in hair and nails, and collagen found in connective tissue. Collagen under a microscope look like long fibres that are woven together to create extra strength, it is a fibrous protein. Collagen is made up of three polypeptide chains wound around each other. Hydrogen bonds forms between the chains and this gives the structure strength.The collagen account for around a quarter of all proteins in the body. The function of collagen is to give mechanical strength. In the walls of arteries, a layer of collagen prevents blood that is being pumped from the heart at high pressure from bursting the walls. Tendons connect skeletal muscles to the bones. Tendons are mostly collagen and form a strong connection that allows muscles to pull bones for movement. Collagen is also responsible for the elasticity of the skin, which is why the skin becomes wrinkled when it lacks collagen . It also makes the skin waterproof. The functions of collagen in the connective tissue include nutrient transport and inflammation.

Fibroblasts are mesenchymal cells that play an important role in the wound healing process. These cells are responsible for releasing inflammatory agents that recruit white blood cells to areas of damaged tissue. Fibroblasts also respond to these chemicals and differentiate into myofibroblasts. These myofibroblasts are characterized by their up-regulated rate of extracellular matrix component production and their ability to physically manipulate the extracellular matrix. When the wound healing process becomes unregulated, this results in what is referred to as a fibrotic response (Kendall). As a result fibrosis, or the thickening and scarring of connective tissues, occurs. Fibrosis is the excess deposition of ECM components like collagen and

Table 3: Wound healing in treatment groups. Wound healing Sucralfate group N= 50 Lidocaine group N=48 Placebo group N=45 P value 21st day 31(62%) 19 (39.5%) 17 (37.7%) 0.028

In-vitro cultured MSCs can be induced to synthesize matrices with some of the characteristics of normal tendons. Equine MSCs can synthesize a surprisingly well-structured matrix when cultured in a bioreactor within the coagulated supernatant. However, the differentiation of these cells has been hindered by a lack of a definitive tenocytic marker. Several key factors can influence the differentiation of MSCs; implanted cells can be influenced by their mechanical environment, contact with other resident cells, and soluble growth mediators. Also, culturing MSCs on different substrates has been shown to induce differentiation into different lineages, including osteogenic, chondrogenic, and neurogenic lineages. MSCs survive well on decellularized tendon matrices, and equine MSCs that are cultured on fresh acellular equine tendon sections not only survive, but proliferate and invade the matrix. They upregulate the COMP gene expression while downregulating collagen I and III gene expression. Also, longer contact time appears to change the morphology of implanted cells, with culture times of three weeks or more resulting in greater similarities between the way in which tenocytes and MSCs lined up with collagen fascicles within the tendon. Tendon regeneration requires four separate but synergistic elements; there must be a scaffold (matrix), an appropriate mix of anabolic factors, and an appropriate mechanical environment to provide a source of cells

Collagen is a fibrous protein which functions in the extracellular matrix and connective tissue. This protein strengthens and supports tissues in the body, such as bone, cartilage, skin, and tendons. Collagen 1 (alpha 1) is the most abundant type of collagen and is vastly distributed in connective tissue, except in hyaline cartilage. Type I collage is found throughout the body in the skin, tendon, vascular, organs, and it is responsible for strength and sturdiness. It is a triple helix formed by two copies of the alpha chain and one copy of the alpha 2 chain. Type II collagen is the main element of cartilage and it is formed by two or more collagens. Type III collagen makes up elastic tissues (skin, lungs, blood vessels). Type IV forms the

The COL7A1 gene contains the instruction manual for making proteins that are used for strengthening and supporting the connective tissue in the body which includes tendons, ligaments, bones and skin. “The proteins produced from the COL7A1 gene, called pro-α1 (VII) chains, are the components of type VII collagen.” (http://ghr.nlm.nih.gov/gene/COL7A1) When three pro-α1 (VII) chains twist together, they form a triple-stranded molecule called a procollagen, these molecules are secreted by the cell and are processed by enzymes which remove extra protein segments. When these procollagen molecules are processed by getting rid of the extra segment on the ends, they then can arrange themselves into longer, thinner bundles of mature type VII collagen.

All proteins are composed of amino acids, organic molecules made from Carbon, Hydrogen, Oxygen and Nitrogen. Collagen is the most ample protein in mammals, in fact collagen constitutes around 25 % of a mammals entire protein content, Collagen is more precisely a family of proteins rather than one particular protein. Fibroblasts are the cells that usually produce collagen. Collagen is a complex molecules so doesn’t have a simple chemical structure for it; diagrams usually show collagen as a fiber.(Helmenstine 2015). There are 19 types of collagen in the collagen family, the 5 most abundant are type I collagen, found in connective tissue of skin, bones, teeth, tendons, ligaments, fascia and organ capsules, type II found in joint cartilage, type III, found in connective tissue of our organs such as liver, spleen and kidneys and type IV & V are the separating layer between epithelial and endothelial cells as well as between skeletal or smooth muscle cells , lens capsule, Schwann & glial cells of the nervous system.(Cellbone® technology 2007) Collagen is fibrous, fibrous proteins tend to have the hydrophilic R groups brought to the inside of the molecule and the hydrophobic R groups tend to be pushed to the outside of the molecule making it insoluble due to the hydrophobic and hydrophilic interactions . Collagen is also a strong structural protein thus Collagen suits its function in animal connective tissues such as bone skin and muscle. (Fullick et al 2015)