rigid collagen is found in bone.
rigid collagen is found in bone.
which type of collagen is found in bone?
rigid
depending upon the degree of mineralization, collagen tissues may be rigid (bone), compliant (tendon), or have a gradient from rigid to compliant (cartilage). it is also abundant in corneas, blood vessels, the gut, intervertebral discs, and the dentin in teeth. in muscle tissue, it serves as a major component of the endomysium. collagen constitutes one to two percent of muscle tissue and accounts for 6% of the weight of strong, tendinous, muscles. the fibroblast is the most common cell that creates collagen. gelatin, which is used in food and industry, is collagen that has been irreversibly hydrolyzed. collagen has many medical uses in treating complications of the bones and skin.
collagen
osteogenesis imperfecta is a genetic disorder that causes increased bone fractures and collagen defects. the main causes for developing the disorder are a result of mutations in the col1a1 and col1a2 genes which are responsible for the production of collagen type 1. approximately 90% of people with oi are heterozygous for mutations in both the col1a1 and col1a2 genes. there are several factors that are results of the dominant form of the oi disorder. these factors include; intracellular stress, abnormal tissue mineralization, abnormal cell to cell interactions, abnormal cell-matrix interactions, a compromised cell matrix structure, and disturbances between non-collagenous proteins and collagen. previous research lead to the belief that oi was an autosomal dominant disorder with few other variations in genomes. however, in the past several years, there has been the identification of autosomal recessive forms of the disorder. recessive forms of oi relate heavily to defects in the collagen chaperones responsible for production of pro-collagen and the assembly of the related proteins. examples of collagen chaperones that are defective in oi patients include chaperone hsp47 (cole-carpenter syndrome) and fkbp65. mutations in these chaperones result in an improper folding pattern in the collagen 1 proteins which causes the recessive form of the disorder. there are three significant types of oi that are a result of mutations in the collagen prolyl 3-hydroxylation complex (components crtap, p3h1, and cypb). these components are responsible for the modification of collagen a1(l)pro986. mutations in other genes such as sp7, serpinf1, tmem38b and bmp1 can also lead to irregularly formed proteins and enzymes that result in the recessive form of osteogenesis imperfecta. there are now links to defects in other proteins caused by genetic mutations ranging in function from structural proteins to enzymatic proteins. a link between proteins such as pigment epithelium-derived factor (pedf) and bone-restricted interferon-induced transmembrane protein (bril) are causes for type v and vi osteogenesis imperfecta. defects in these proteins lead to defective bone mineralization which aids in the formation of the brittle bone symptom of osteogenesis imperfecta. additionally, mutations in the col1a1 and col1a2 genes can result in signal disruptions of the extracellular matrix signaling that is present within the collagen proteins, causing worsened symptoms of the disorder. a single point mutation in the untranslated 5' region of the ifitm5 gene was recently discovered and linked directly to oi type v. another single point mutation in the region that codes for collagen proteins on the ifitm5 gene was also found to be present in patients with substantially more severe versions of oi than just type v. osteogenesis imperfecta has also been seen as an x-linked related genetic disorder in some rare cases but continues to be a primarily heterozygous dominant disorder
osteogenesis imperfecta