week 3

basal

basal

desmosomes

<p>formation</p> Signup and view all the answers

<p>skin</p> Signup and view all the answers

<p>epidermolysis bullosa simplex</p> Signup and view all the answers

<p>desmosomes</p> Signup and view all the answers

<p>intermediate filament</p> Signup and view all the answers

<p>II</p> Signup and view all the answers

<p>V</p> Signup and view all the answers

<p>secondary</p> Signup and view all the answers

<p>III</p> Signup and view all the answers

<p>adhesion</p> Signup and view all the answers

<p>V</p> Signup and view all the answers

<p>intermediate</p> Signup and view all the answers

<p>I</p> Signup and view all the answers

<p>cell</p> Signup and view all the answers

<p>dissolve</p> Signup and view all the answers

<p>II</p> Signup and view all the answers

<p>acidic</p> Signup and view all the answers

<p>II</p> Signup and view all the answers

<p>adhesion</p> Signup and view all the answers

<p>types</p> Signup and view all the answers

<p>nuclear</p> Signup and view all the answers

<p>stratified</p> Signup and view all the answers

<p>filaments</p> Signup and view all the answers

<p>simple</p> Signup and view all the answers

<p>soluble</p> Signup and view all the answers

<p>epithelia</p> Signup and view all the answers

<p>parallel</p> Signup and view all the answers

<p>stretching</p> Signup and view all the answers

<p>lamins</p> Signup and view all the answers

<p>blistering</p> Signup and view all the answers

<p>epithelia</p> Signup and view all the answers

<p>vimentin</p> Signup and view all the answers

<p>neurofilaments</p> Signup and view all the answers

<p>lamins</p> Signup and view all the answers

<p>lamins</p> Signup and view all the answers

<p>55</p> Signup and view all the answers

<p>skeletal</p> Signup and view all the answers

<p>mitosis</p> Signup and view all the answers

<p>sequence</p> Signup and view all the answers

<p>keratin</p> Signup and view all the answers

<p>Vimentin-like (A)</p> Signup and view all the answers

<p>Type V lamins (C)</p> Signup and view all the answers

<p>Due to length and sequence characteristics of α-helix (A)</p> Signup and view all the answers

<p>Desmin (A)</p> Signup and view all the answers

<p>They form the nuclear lamina structure (A)</p> Signup and view all the answers

<p>They are the most resilient structures in the cell. (D)</p> Signup and view all the answers

<p>They are composed of α-helical coiled-coils. (C)</p> Signup and view all the answers

<p>Vimentin (C)</p> Signup and view all the answers

<p>Lamins (B)</p> Signup and view all the answers

<p>It includes a large multigene family with several types. (B)</p> Signup and view all the answers

<p>The requirement for denaturants to dissolve them. (D)</p> Signup and view all the answers

<p>They provide mechanical support. (C)</p> Signup and view all the answers

<p>Cardiac muscle (A)</p> Signup and view all the answers

<p>Acidic isoelectric points and lower molecular weight (B)</p> Signup and view all the answers

<p>K4 and K13 (D)</p> Signup and view all the answers

<p>Equimolar association of Type I and Type II proteins (A)</p> Signup and view all the answers

<p>K6a and K16 (C)</p> Signup and view all the answers

<p>Type I and Type II (C)</p> Signup and view all the answers

<p>K3 (A)</p> Signup and view all the answers

<p>α-helical coiled-coils (C)</p> Signup and view all the answers

<p>Stratified, barrier tissues (C)</p> Signup and view all the answers

<p>Providing structural integrity (A)</p> Signup and view all the answers

<p>It becomes dynamic and participates in filament assembly (A)</p> Signup and view all the answers

<p>Mutations in K5 or K14 (C)</p> Signup and view all the answers

<p>K5 (A)</p> Signup and view all the answers

<p>Desmosomes (D)</p> Signup and view all the answers

<p>Immunofluorescence (C)</p> Signup and view all the answers

<p>Development of blistering disorders (A)</p> Signup and view all the answers

<p>They assemble into antiparallel tetramers (D)</p> Signup and view all the answers

<p>Keratins (A)</p> Signup and view all the answers

<p>They are often found in mesenchymal tissues. (B)</p> Signup and view all the answers

<p>Providing structural support (D)</p> Signup and view all the answers

<p>Blistering disorders resembling epidermolysis bullosa simplex (B)</p> Signup and view all the answers

<p>Dimers - Tetramers - Higher oligomers (C)</p> Signup and view all the answers

<p>They resist stretching but are easily bent. (B)</p> Signup and view all the answers

<p>They facilitate the formation of coiled coils. (C)</p> Signup and view all the answers

<p>Keratin (B)</p> Signup and view all the answers

<p>They are critical for assembly. (D)</p> Signup and view all the answers

<p>It occurs spontaneously and quickly without any energy source. (C)</p> Signup and view all the answers

<p>Primarily by electron microscopy. (B)</p> Signup and view all the answers

<p>They assemble into parallel dimers and then antiparallel tetramers. (D)</p> Signup and view all the answers

<p>They are primarily located in mesenchyme. (B)</p> Signup and view all the answers

<p>It contributes to filament assembly. (D)</p> Signup and view all the answers

A protein found in the basal cells of the epidermis (skin).

A protein found in buccal epithelium.

A protein found in suprabasal cells of the epidermis, staining positive in immunofluorescence.

Cytoskeletal components that provide structural support to cells.

Cell-to-cell junctions that link intermediate filaments.

A genetic skin blistering disorder caused by mutations in keratin genes.

Gene changes in keratin proteins that cause skin blistering.

Cells at the bottom of the epidermis (skin) layer containing K5 & K14 keratins.

Strongest cell structures; resist stress and strain.

Different types, like lamins, keratins, and neurofilaments, with varying roles.

Support cell integrity, forming networks through the cell.

Support and organize the nucleus.

Alpha-helical coiled-coils give strength and resilience.

A common cytoplasmic intermediate filament type.

Intermediate filaments crucial for nerve cell structure.

A type of nuclear intermediate filament.

A large number of similar genes coding for intermediate filaments

Intermediate filaments assemble spontaneously in vitro without requiring energy, cofactors, or associated proteins. The process involves the formation of dimers, tetramers, and higher oligomers, driven by the interactions of heptad repeats within alpha-helical rod domains.

Patterns of seven amino acids within the alpha-helical rod domain of intermediate filaments. These repeats are crucial for the formation of coiled-coils, which are the building blocks of the filament structure.

Intermediate filaments provide structural support to cells, giving them tensile strength and resistance to stretching. They are essential for maintaining cell shape, anchoring organelles, and connecting cells through junctions.

Unlike microtubules and actin filaments, intermediate filaments do not require energy-consuming processes like hydrolysis of ATP or GTP for their assembly and disassembly. Their assembly is primarily driven by interactions between protein subunits.

Different types of IF have specific tissue expression patterns. This allows pathologists to identify cell origins and differentiate between normal and diseased tissue based on their presence or absence.

Fibrous proteins forming strong, rope-like structures that support cells and tissues.

Two families of proteins that form keratin intermediate filaments. Type I are acidic and smaller, while Type II are neutral to basic and larger.

Keratin filaments require an equal combination of Type I and Type II keratins for assembly.

Specific pairs of Type I and II keratins are found in different tissues, suggesting specialized functions.

Soluble keratin molecules assemble into filaments, building a strong, dynamic network within cells.

These Type I and II keratins are found in the basal layer of the epidermis, providing anchoring strength.

These keratins are present in the upper layers of the epidermis, contributing to skin's protective barrier and preventing water loss.

These keratins are found in the basal layer and are involved in rapid skin cell turnover and repair.

Found in simple epithelial tissues like those lining internal organs, these keratins provide structural support.

A diverse group of protein filaments that play a crucial role in maintaining cell shape, anchoring organelles, and providing mechanical strength.

A mesh-like network of lamins that lines the inner membrane of the nucleus, providing structural support, regulating nuclear shape, and controlling DNA replication and transcription.

A structural motif in intermediate filaments where two or more alpha-helical segments intertwine to form a stable, rope-like structure.

A specific amino acid sequence that directs proteins to the nucleus, allowing them to enter and function within the nuclear environment.

A process that adds a phosphate group to a molecule, often regulating its activity or function.

A family of acidic keratin proteins that are smaller in size and have lower molecular weight.

A family of neutral to basic keratin proteins that are larger in size and have higher molecular weight.

Specific pairs of Type I and Type II keratins are found in different tissues, suggesting specialized functions.

Keratin K5 and K14 are found in the basal layer of the epidermis, providing anchoring strength.

Keratin K10 and K1 are present in the upper layers of the epidermis, contributing to skin's protective barrier and preventing water loss.

Keratin K6a and K16 are found in the basal layer and are involved in rapid skin cell turnover and repair.

Found in simple epithelial tissues like those lining internal organs, these keratins provide structural support.

Keratin intermediate filaments are fibrous proteins that form strong, rope-like structures that support cells and tissues.

Keratin filaments are dynamic, as soluble keratin is incorporated into filaments, constantly building and rebuilding the network.

Different types of IFs are expressed in various tissues, including keratins (skin), vimentin (connective tissue), neurofilaments (nerves), and lamins (nucleus).

IFs self-assemble from subunits, forming a strong, dynamic network within cells. Their assembly is driven by protein subunit interactions, unlike other cytoskeletal filaments that need energy.

Mutations in IF genes can cause diseases, such as epidermolysis bullosa simplex (EBS), a skin blistering disorder. Different IF disruptions lead to varying cellular and tissue dysfunction.

IFs are composed of protein subunits that assemble into a strong, rope-like structure. This structure is highly resistant to stretching and tension, making IFs essential for providing mechanical strength to cells and tissues.

IFs, unlike actin filaments and microtubules, don't require energy-consuming processes (ATP or GTP hydrolysis) for assembly/disassembly. Their assembly is driven by protein-protein interactions.

Intermediate filaments are classified into five main types: Type I & II (keratins), Type III (vimentin-like), Type IV (neurofilaments), and Type V (lamins). Each type has a specific tissue distribution and function.

Tough, fibrous proteins that form the intermediate filaments found in epithelial cells. They provide structural support and mechanical strength to the skin, hair, and nails.

A type of intermediate filament found in mesenchymal cells, such as fibroblasts, muscle cells, and glial cells. They play a role in cell migration, wound healing, and maintaining cell shape.

There are several types of IFs, each with specific locations and functions: Keratins, Vimentin-like, Neurofilaments, Lamins, and others.

Nuclear IFs that form a mesh-like framework called the nuclear lamina, supporting the nuclear envelope, regulating nuclear shape, and involved in DNA replication and transcription.

Lamins are unique because they are intranuclear (located inside the nucleus) and have a longer alpha-helical rod domain compared to cytoplasmic IFs.

A mesh-like network of Lamin IFs lining the inner membrane of the nucleus, providing structure, regulating nuclear shape, and controlling DNA processes.

A genetic skin disorder where the skin is easily blistered due to mutations in the genes for keratin K5 or K14. This severely weakens the structural integrity of the skin.

Mutations in keratin genes, especially those affecting K5 and K14, weaken the structural integrity of the basal layer of the skin. This makes the skin fragile and prone to blistering.

These are specialized cell junctions that act like 'glue' between skin cells, holding them tightly together and helping to form the strong barrier of the epidermis.

Keratin intermediate filaments connect to desmosomes, providing a strong link between cells. This network of filaments and junctions gives the skin its incredible strength and resilience.

These are rope-like protein structures found within skin cells that provide strength and support. They are crucial for the integrity and function of the epidermis.

These mice carry a modified gene for keratin, which allows researchers to study the effects of mutations on skin integrity and potentially develop treatments for skin disorders like epidermolysis bullosa simplex.

Intermediate filaments form interconnected networks within cells and tissues, allowing cells to work together and maintain tissue integrity. They are essential for tissue function.