HomeCoursesMEDSCI 201: Human Structure and FunctionLecture 3 Lecture 3 0% Question 1 of 33 What are the different types of load? (6) = Compression , torsion , bending , sheer , tension , combined What are the different types of load? (6) = Compression , torsion , bending , sheer , tension , combinedQuestion 1 of 33Question 2 of 33 "What is the most abundant collagen fibre? = Type I (90%)" "What is the most abundant collagen fibre? = Type I (90%)" Question 2 of 33Question 3 of 33 Where is type I collagen found (3) = Tendons, ligaments, bone Where is type I collagen found (3) = Tendons, ligaments, boneQuestion 3 of 33Question 4 of 33 Where is type II collagen found? (3) = Cartilage eye (vitrous humour), intravertebral discs Where is type II collagen found? (3) = Cartilage eye (vitrous humour), intravertebral discs Question 4 of 33Question 5 of 33 Where is type III collagen found? (2) = Reticular fibres, skin Where is type III collagen found? (2) = Reticular fibres, skinQuestion 5 of 33Question 6 of 33 What do type IV collagen fibres form? = Basal lamina of epithelial tissue What do type IV collagen fibres form? = Basal lamina of epithelial tissue Question 6 of 33Question 7 of 33 What are the major steps of collagen fibre formation? (4) = Synthesis of pro-alpha protein chain, assembly of three pro-alpha chains into procollagen triple helix, assembly into fibril, aggregation of fibrils into fibre What are the major steps of collagen fibre formation? (4) = Synthesis of pro-alpha protein chain, assembly of three pro-alpha chains into procollagen triple helix, assembly into fibril, aggregation of fibrils into fibre Question 7 of 33Question 8 of 33 What does the pro-alpha chain contain? (3) = Glysine, proline, lysine What does the pro-alpha chain contain? (3) = Glysine, proline, lysineQuestion 8 of 33Question 9 of 33 What happens to pro collagen to allow it to form triple helices? = Hydroxylation (formation of H bonds) What happens to pro collagen to allow it to form triple helices? = Hydroxylation (formation of H bonds) Question 9 of 33Question 10 of 33 What prevents pro-collagen triple helices from bind with other pro-collagen triple helices? = Propeptides bind to the ends of the helices What prevents pro-collagen triple helices from bind with other pro-collagen triple helices? = Propeptides bind to the ends of the helices Question 10 of 33Question 11 of 33 What happens to the pro-collagen after it leaves the cell? = Propeptides cleaved What happens to the pro-collagen after it leaves the cell? = Propeptides cleaved Question 11 of 33Question 12 of 33 Which amino acid is most important in collagen? = Glysine Which amino acid is most important in collagen? = Glysine Question 12 of 33Question 13 of 33 Where does the strength of collagen come from? (3) = Glysine enables light coiling, hydroxylation forms helices, covalent bonds Where does the strength of collagen come from? (3) = Glysine enables light coiling, hydroxylation forms helices, covalent bondsQuestion 13 of 33Question 14 of 33 What causes scurvey? = Vitamin C deficiency What causes scurvey? = Vitamin C deficiency Question 14 of 33Question 15 of 33 What does a vitamin C deficiency result in? = Downregulated production of lysyl hydroxylase (for hydroxylation of proline and lysine) What does a vitamin C deficiency result in? = Downregulated production of lysyl hydroxylase (for hydroxylation of proline and lysine) Question 15 of 33Question 16 of 33 What is the result of downregulation of production of lysyl hydroxylase? = Collagen does not form it’s essential coiled structure and loses its strength What is the result of downregulation of production of lysyl hydroxylase? = Collagen does not form it’s essential coiled structure and loses its strength Question 16 of 33Question 17 of 33 What are the symptoms of weakened collagen fibres caused by vit C deficiency? (3) = Rotting teeth, bleeding from mucous membranes, bowed legs What are the symptoms of weakened collagen fibres caused by vit C deficiency? (3) = Rotting teeth, bleeding from mucous membranes, bowed legs Question 17 of 33Question 18 of 33 What is osteogenesis imperfecta? = Mutation of genes that encode collagen type I fibres What is osteogenesis imperfecta? = Mutation of genes that encode collagen type I fibresQuestion 18 of 33Question 19 of 33 What are the symptoms of osteogenesis imperfecta? ((2) = Brittle bones, Weak tendons What are the symptoms of osteogenesis imperfecta? ((2) = Brittle bones, Weak tendons Question 19 of 33Question 20 of 33 What is stickler syndrome? = An autosomal dominant inherited mutation of genes that encode collagen type II fibres What is stickler syndrome? = An autosomal dominant inherited mutation of genes that encode collagen type II fibresQuestion 20 of 33Question 21 of 33 What are the symptoms of stickler syndrome? (4) = Flat face, vision impairment, hearing loss, osteoarthritis What are the symptoms of stickler syndrome? (4) = Flat face, vision impairment, hearing loss, osteoarthritis Question 21 of 33Question 22 of 33 What is a proteoglycan? (2) = Core protein, Covalently attached glysosaminoglyan chain (GAG) What is a proteoglycan? (2) = Core protein, Covalently attached glysosaminoglyan chain (GAG) Question 22 of 33Question 23 of 33 What determines the properties of proteoglycans? (2) = Number of GAGs, type of GAGs What determines the properties of proteoglycans? (2) = Number of GAGs, type of GAGs Question 23 of 33Question 24 of 33 What are the types of proteoglycans? (4) = Aggrecan, Biglycan, Perlecan, Versican What are the types of proteoglycans? (4) = Aggrecan, Biglycan, Perlecan, VersicanQuestion 24 of 33Question 25 of 33 What GAG is not sulphated? = Hyaluronan What GAG is not sulphated? = HyaluronanQuestion 25 of 33Question 26 of 33 What are the properties of GAGs? (2) = Negatively charged, hydrophilic What are the properties of GAGs? (2) = Negatively charged, hydrophilicQuestion 26 of 33Question 27 of 33 What binds proteoglycans to hyaluron molecules? = Link proteins What binds proteoglycans to hyaluron molecules? = Link proteinsQuestion 27 of 33Question 28 of 33 What is GAG is aggrecan rich in? = chondroitin sulfate What is GAG is aggrecan rich in? = chondroitin sulfate Question 28 of 33Question 29 of 33 Where is aggrecan commonly found? (2) = Cartilage, invertebral discs Where is aggrecan commonly found? (2) = Cartilage, invertebral discsQuestion 29 of 33Question 30 of 33 What enzymes are active in collagen degradation? (2) = Metalloproteases (MMPs), Collagenases What enzymes are active in collagen degradation? (2) = Metalloproteases (MMPs), CollagenasesQuestion 30 of 33Question 31 of 33 Which enzyme breaks down proteoglycans? = ADAMTS Which enzyme breaks down proteoglycans? = ADAMTS Question 31 of 33Question 32 of 33 What are examples of collagenases? (2) = MMP1, MMP13 What are examples of collagenases? (2) = MMP1, MMP13Question 32 of 33Question 33 of 33 What are examples of aggrecanases? (2) = ADAMTS-4, AMDAMTS-5 What are examples of aggrecanases? (2) = ADAMTS-4, AMDAMTS-5Question 33 of 33 Loading...