structure and function of connective tissues Flashcards

1
Q

Describe the locomotor/musculoskeletal system created with Biorender by Dr. Falcon.

A

It includes bones, skeleton, tendons, muscles, and joints. Bones are hard and stiff, tendons attach muscles to bones and are viscoelastic, muscles enable movement, and joints connect two bones.

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2
Q

What is the function of tendons in the musculoskeletal system?

A

Tendons attach muscles to bones.

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3
Q

Define the term ‘viscoelastic’ in the context of the musculoskeletal system.

A

Viscoelastic refers to the property of tendons being able to deform slowly and recover.

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4
Q

How are muscles described in relation to movement in the locomotor system?

A

Muscles are described as enabling movement.

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5
Q

What is the role of joints in the musculoskeletal system?

A

Joints serve as connections between two bones.

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6
Q

Do different diseases/syndromes arising from defects of the same gene/protein have overlapping phenotypes?

A

Yes, overlapping phenotypes may arise from defects of different genes/proteins.

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7
Q

Describe the diseases mentioned in the content related to the locomotor system.

A

The diseases mentioned include osteogenesis imperfecta, Ehlers-Danlos syndrome, and congenital cervical kyphosis.

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8
Q

How can cells and matrices in bone formation be assessed according to the content?

A

Cells and matrices in bone formation can be assessed using light, polarization, and ultrastructural microscopy.

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9
Q

What type of microscopy can be used to assess cells and matrices in bone formation according to the content?

A

Light, polarization, and ultrastructural microscopy can be used.

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10
Q

Define the term ‘woven and lamellar bone formation’ as mentioned in the content.

A

It refers to the supramolecular assessment of cells and matrices in the context of bone formation.

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11
Q

Describe collagen’s role as a major structural protein in the human body.

A

Collagen is a ubiquitous protein found in humans and vertebrates, with 28 types and 43 genes contributing to various functions. Types I, II, and III are the most abundant, making collagen a major constituent of all connective tissues.

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12
Q

What is the significance of collagen in the body’s connective tissues?

A

Collagen accounts for 80-90% of all collagen forms fibrils, making it a crucial component of connective tissues.

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13
Q

Define the term ‘collagen’ and its importance in the human body.

A

Collagen is a major structural protein present in humans and vertebrates, playing essential roles in various bodily functions and serving as a key component of connective tissues.

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14
Q

How many types of collagens are there, and which ones are the most abundant?

A

There are 28 types of collagens, with Types I, II, and III being the most abundant in the human body.

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15
Q

What is the role of collagen in biomechanical analysis according to the provided content?

A

Collagen is crucial in biomechanical analysis, as it serves as the major structural protein in the human body and contributes to various functions and roles.

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16
Q

Do all 28 types of collagens contribute to an array of functions in the body?

A

Yes, all 28 types of collagens contribute to an array of functions and roles in the human body.

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17
Q

How does collagen contribute to the formation of fibrils in the body?

A

Collagen, accounting for 80-90% of all collagen forms, plays a significant role in forming fibrils in the body’s connective tissues.

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18
Q

Describe the structure of collagen.

A

Collagen consists of three polypeptide chains, α chains, wrapped around each other to form a right-handed triple helix.

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19
Q

What are the two types of collagen homotrimers mentioned in the content?

A

Collagen II and III are homotrim with three identical chains.

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20
Q

Explain what heterotrim are in collagen.

A

Heterotrimers in collagen, like Collagens I and V, consist of 2 or 3 different chains wrapped around each other.

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21
Q

How is the helix formation in collagen governed?

A

The helix in collagen is governed by the position of individual residues relative to each other, twisting around a central axis.

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22
Q

Define the genes responsible for coding each α chain in collagen.

A

Each α chain in collagen is coded by a specific gene, such as COL1A1 and COL1A2 for Collagen I.

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23
Q

What is the overall role of collagen in the body?

A

Collagen serves as the major structural protein in various tissues, providing strength and support.

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24
Q

What is the significance of the arrangement of amino acids in collagen structure?

A

The arrangement of amino acids in collagen, such as glycine, proline, and hydroxyproline, contributes to its unique structural properties as a major structural protein.

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25
Q

How is the structure of collagen related to its function?

A

The specific arrangement of amino acids in collagen, including glycine, proline, and hydroxyproline, is crucial for its function as a structural protein in tissues like skin, tendons, and bones.

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26
Q

What are telopeptides in collagen?

A

Telopeptides are short regions of processed collagen monomers that aid in the crosslinking of collagen molecules and other matrix elements.

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27
Q

How does the C-terminal of collagen contribute to its structure?

A

The C-terminal region promotes the formation of the triple helix during collagen biosynthesis.

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28
Q

What is the role of the N-terminal region in collagen structure?

A

The N-terminal region contributes to the diameter of collagen fibrils. In some collagens, this terminal is completely removed.

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29
Q

Define collagen.

A

Collagen is the major structural protein in the body, providing strength and structure to tissues such as skin, tendons, and bones.

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30
Q

Describe the process of collagen synthesis.

A

Collagen first transcribed and translated in the cell, forming pre-procollagen molecules. These molecules then move into the roughoplasmic reticulum with the help of signal peptides, contributing to the correct formation of fibrils and biomechanical properties.

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31
Q

What is the role of ribosomes in collagen synthesis?

A

Ribosomes attach to collagen mRNA and translate it into pre-procollagen molecules.

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32
Q

How are pre-procollagen molecules transported into the rough endoplasmic reticulum?

A

Pre-procollagen molecules are aided by signal peptides to move into the rough endoplasmic reticulum.

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33
Q

Define collagen synthesis.

A

Collagen synthesis is the process where collagen mRNA is translated into pre-procollagen molecules, which then undergo further steps to form collagen fibrils.

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34
Q

What contributes to the correct formation of collagen fibrils during synthesis?

A

All steps in collagen synthesis, including transcription, translation, and movement into the rough endoplasmic reticulum, contribute to the correct formation of collagen fibrils.

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35
Q

Describe the role of vitamin C in collagen synthesis.

A

Vitamin C is essential for collagen synthesis as it is required for collagen hydroxylation.

36
Q

What are the post-transl modifications involved in collagen synthesis?

A

Post-translational modifications include proline hydroxylation, N- and O-glycosylation, and triple helix folding.

37
Q

Define procollagen.

A

Procollagen is the precursor to collagen, formed during collagen synthesis.

38
Q

How is hydroxylation of collagen residues carried out?

A

Hydroxylation of collagen residues, specifically proline residues, is carried out with the help of specific cofactors like Fe2+ and pro-collagen lysine 5-dioxygenase.

39
Q

Describe the process of triple helix folding in collagen synthesis.

A

Triple helix folding in collagen synthesis initiates at the C-terminal and is crucial for the structural integrity of collagen.

40
Q

What is the role of molecular oxygen in collagen synthesis?

A

Molecular oxygen is essential for certain post-translational modifications in collagen synthesis.

41
Q

Do signal peptides play a role in collagen synthesis?

A

Yes, signal peptides are involved in collagen synthesis by initiating post-translational modifications of pre-procollagen.

42
Q

How does scurvy affect collagen synthesis?

A

Scurvy, a result of vitamin C deficiency, impacts collagen synthesis by affecting collagen hydroxylation.

43
Q

What is the role of the Golgi apparatus in collagen synthesis?

A

The Golgi apparatus is where the process of collagen synthesis takes place. It is responsible loading procollagen molecules into vesicles and facilitating their release for secretion into the extracellular space.

44
Q

How are the C-terminal and N-terminal propeptides involved in collagen synthesis?

A

In collagen synthesis, both the C-terminal and N-terminal propeptides are cleaved after the release of procollagen molecules to facilitate the formation of mature collagen fibers.

45
Q

Define collagen and its significance in the body.

A

Collagen is the major structural protein in the body, providing strength and structure to various tissues. It plays a crucial role in maintaining the integrity of skin, bones, tendons, and other connective tissues.

46
Q

What is the function of procollagen in collagen synthesis?

A

Procollagen serves as the precursor molecule that undergoes processing and modification in the Golgi apparatus before being secreted to form mature collagen fibers.

47
Q

How is collagen important for tissue integrity?

A

Collagen is essential for maintaining the structural integrity of tissues such as skin, bones, tendons, and ligaments. It provides strength and support to these tissues, contributing to overall body function and health.

48
Q

Describe the process of collagen outside the cell.

A

Collagen is processed outside the cell, where collagen fibrils interact with each other through covalent crosslinking, enhancing the molecule’s mechanical performance.

49
Q

What is the role of lysyl oxidase in collagen synthesis?

A

Lysyl oxidase is a copper-dependent enzyme that converts lysine and hydroxylysine residues at the N and C terminal telopeptides into aldehyde, which then spontaneously condense with other aldehydes to form covalent crosslinks.

50
Q

How do collagen fibrils interact with each other during synthesis?

A

Collagen fibrils interact with each other through covalent crosslinking, which contributes to the mechanical performance of the molecule.

51
Q

Define the role of lysyl oxidase in collagen synthesis.

A

Lysyl oxidase is an enzyme that converts specific residues in collagen into aldehyde, which then participate in forming covalent crosslinks.

52
Q

What are the key residues involved in collagen crosslinking by lysyl oxidase?

A

Lysyl oxidase targets lysine and hydroxylysine residues at the N and C terminal telopeptides for conversion into aldehyde during collagen synthesis.

53
Q

Describe the importance of analysing morphological and mechanical features a sample when diagnosing a musculoskeletal disease.

A

It is crucial to analyze the morphological and mechanical features of a sample such as skin, especially in collagen-related musculoskeletal diseases or syndromes.

54
Q

What are some methods used in the qualitative analysis of collagen samples?

A

Methods include Transmission Electron Microscopy (TEM) and Sc Electron Microscopy (SEM).

55
Q

Describe the findings of SEM in healthy tissues regarding rupture identification.

A

Longitudinal fractures, severe alteration of collagen network and organization, obvious areas with decreased fibril density.

56
Q

Describe the findings of OM in healthy tissues regarding rupture identification.

A

Alteration of collagen network, disappearance of undulations, increase in space between fibrils.

57
Q

Describe the process of low stress tendon fatigue in the context of overuse injuries.

A

Low stress tendon fatigue is a relatively rapid process that occurs in overuse injuries, as described by Gabriel Parent et al in the Annals of Biomedical Engineering, 2011.

58
Q

What is the significance of transversal sections in the molecular analysis of collagen using TEM?

A

Transversal sections provide insights into the structure of collagen, including increased space between fibrils with increased fatigue, disruption of the network, and potential changes in diameter that may require further magnification or quantification.

59
Q

How can healthy tissues rupture be identified in molecular analysis of collagen?

A

Healthy tissues can be identified by observing characteristics such as increased space between fibrils with fatigue, disruption of the network, and potential changes in diameter under TEM analysis.

60
Q

Define TEM in the context of molecular analysis of collagen.

A

TEM stands for Transmission Electron Microscopy, a technique used to study the ultrastructure of materials at a very high resolution.

61
Q

What insights can be gained from studying collagen using TEM in the context of low stress tendon fatigue?

A

Studying collagen using TEM can provide insights into changes such as increased space between fibrils, disruption of the network, and potential alterations in diameter that occur during low stress tendon fatigue.

62
Q

How does the diameter of collagen fibrils change in the context of low stress tendon fatigue?

A

The diameter of collagen fibrils may be affected during low stress tendon fatigue, requiring further magnification or quantification for accurate assessment.

63
Q

Describe the impact of increased fatigue on the structure of collagen fibrils.

A

Increased fatigue can lead to changes in the structure of collagen fibrils, including increased space between fibrils, disruption of the network, and potential alterations in diameter.

64
Q

What role does TEM play in identifying changes in collagen structure due to overuse injuries?

A

TEM plays a crucial role in identifying changes in collagen structure caused by overuse injuries, such as increased space between fibrils, disruption of the network, and potential changes in diameter.

65
Q

Describe the difference in collagen fibrils between healthy tissues and diseased patients.

A

Healthy tissues have tightly packed collagen fibrils with a uniform arrangement and pattern, while diseased patients show larger collagen fibrils diameters, star-shaped, irregular edges, or completely disrupted collagen cauliflowers.

66
Q

What is the significance of low stress tendon fatigue in the context of overuse injuries?

A

Low stress tendon fatigue is a relatively rapid process that can contribute to overuse injuries.

67
Q

How can the rupture of healthy tissues be identified?

A

The rupture of healthy tissues can be identified by examining the collagen fibrils for abnormalities such as larger diameters, star-shaped appearance, irregular edges, or complete disruption into collagen cauliflowers.

68
Q

Describe the process of Low Stress Tendon Fatigue in the context of overuse injuries.

A

Low Stress Tendon Fatigue is a relatively rapid process that can lead to overuse injuries.

69
Q

What can be a sign of decreased or poor mechanical properties in tissues according to the content?

A

Spacing in between the fibrils becoming very apparent and quantifiable.

70
Q

How can healthy tissues rupture and be identified based on the content?

A

Healthy tissues can rupture due to decreased mechanical properties, which can be identified by the spacing between fibrils.

71
Q

Define the significance of spacing in between fibrils in tissues according to the content.

A

The spacing between fibrils becoming very apparent and quantifiable can indicate decreased or poor mechanical properties in that tissue.

72
Q

What can the process of Low Stress Tendon Fatigue eventually lead to according to the content?

A

It can eventually involve a vast array of diseases, syndromes, and musculoskeletal problems.

73
Q

Describe the impact of Collagen3A1 mutations on clinical phenotypes.

A

Collagen3A1 mutations can lead to variable clinical phenotypes such as acrogeria and vascular rupture.

74
Q

What does SDS-PAGE electrophoresis stand for?

A

SDS-PAGE electrophoresis stands for Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis.

75
Q

Define the components represented by ‘M’ and ‘C’ in the context of SDS-PAGE electrophoresis.

A

In SDS-PAGE electrophoresis, ‘M’ represents Medium and ‘C’ represents Cell layer.

76
Q

How was the content created according to the information provided?

A

The content was created with Biorender by Dr. Falcon.

77
Q

Describe the tissue mainly affected in Osteogenesis imperfecta.

A

Bone

78
Q

What are the principal genes associated with Ehlers-Danlos syndrome (Type VII)?

A

COL1A1 COL1A2

79
Q

Define the tissue mainly affected in Ehlers-Danlos syndrome (Type VII).

A

Skin, joints, heart

80
Q

How is collagen affected in Stickler syndrome?

A

Various

81
Q

Do you know the tissue mainly affected in Alport syndrome?

A

Kidney, skin, basement membranes

82
Q

Describe the tissue mainly affected in Ehlers-Danlos syndrome (Type IV).

A

Blood vessels

83
Q

What are the principal genes associated with Alport syndrome?

A

COL4A3 COL4A4 COL4A5 COL4A6

84
Q

Define the tissue mainly affected in Ehlers-Danlos syndrome (Type I/II).

A

Skin, joints

85
Q

Describe the content of Lecture 1 onive tissues.

A

Lecture 1 the structure and function of connective tissues.

86
Q

What is the focus of Lecture 2 regarding connective tissues?

A

Lecture 2 focuses on molecular defects of connective tissues part I.

87
Q

What aspect of connective tissues is discussed in Lecture 3?

A

Lecture 3 discusses molecular defects of connective tissues part II.