Cell- och Molekylärbiologi Flashcards
Example of cell functionality in multicellular organisms
differentiation, apoptosis, gene regulation, cell division, coordination, sensing environment
What are intracellular signals also called?
Second Messengers
Name all forms of intercellular signaling methods
Contact dependent, Endocrine, Paracrine, Autocrine, Synaptic, Gap junction
Explain and name all parts of G-protein and GPCRs
GPCR = G-protein coupled receptor, is a transmembrane protein with seven transmembrane alpha-helices and a binding site on extracellular side.
G-protein, have three parts, alpha, beta, gamma. GPCR changes confirmation –> G-alpha part binds to GPCR and releases GDP. New GTP comes in and GPCR, G-alpha and G-beta/gamma produces each a signaling pathway.
What are enzyme coupled receptors?
Transmembrane enzyme that changes confirmation when ligand signal activates receptor. Usually a heterodimer that gets brought together to create a catalytic site in cytosolic side of cell.
Name different types of signaling reaction speeds
All-or-none, hyperbolic and sigmoidal.
Describe pros and cons of positive feedback and negative feedback in signaling pathways
Positive feedback –> no off button, good for differentiation.
Negative feedback –> switch that can sense change in concentration, and can work as an oscillator depending on length of delay
What is a Protein Kinase and Protein Phosphatase?
Protein Kinase adds a phosphate group to a specifik amnio acid. Protein Phosphatase removes a phosphate group.
Name enzymes that can regulate GTP
GAP = GTPase-activating protein which increases hydrolysis of GTP to become GDP.
GEF = guanine nucleotide exchange factors that promotes release of GDP from G-protein.
Describe cAMP and how it is catalyzed in cells.
Activated alpha-G-protein activates Adenylyl cyclase that catalyzes reaction that turns ATP into cAMP. (cyclic AMP)
Describe PKA and how it reacts with cAMP
cAMP-dependant Protein Kinase A (PKA) gets activated once cAMP reacts with it. Leads to release of two catalytic site units that travel through nucleus and activate CREB (CRE-binding protein). Cyclic AMP response elemet (CRE) is a sequence of nucleotides on DNA.
Name example of enzyme coupled receptor
Receptor tyrosine kinase have tyrosine kinase domain that can phophorylate tyrosine creating phophotyrosine docking sites.
Describe some general features of signaling pathways
Scaffold, amplify, integrate, spread, anchor, modulate
Describe nucleus receptors
They typically have ligand binding domain that has an inhibitory protein which releases when ligand attaches. Coactivator protein then attaches and makes it possible for receptor to bind to DNA-segment.
Name the sides of epithelial cells
Apex side towards extracellular medium and lateral surfaces that are attached to basal lamina.
Name the types of cell-cell junctions
Tight junction, adherence junctions. desmosome, gap junctions
Name the types of cell-matrix junctions
Actin-linked-cell-matrix junction and hemidesmosome
Name the overall 4 categories of junctions
tight junctions, cell-cell anchoring junction, channel forming junction and cell-matrix junction.
Name the transmembrane adhesion protein associated with cell-cell junctions and cell-matrix junctions.
Cadherin (cell-cell) and Integrin (cell-matrix)
Describe in detail what cadherins are
They are homophillic and sorts themselves out by only binding to their counterpart.
Have several domains with hinge region where Ca2+ can bind to make more rigid. Works a bit like velcro.
More cadherins = stronger connection between cells, they become more centered when in clusters. Binding occurs at N-terminal tips.
Intercellular part binds to alpha-catenin which binds to actin filament. If there is tension alpa-catenin stretches out and vinculin protein can bind wich then binds to more actin filaments.
Forms adhesion belts around epithelial cells.
What are non-classical cadherins?
Cadherins that are used in desmosomes and binds to intermediate filaments instead of actin filament.
What are adaptor proteins?
Proteins in between filaments and junction protein such as vinculin and alpha-catenin.
What are gap junctions made of and what are the different types?
6 connexins that form a connexon and two connexons form a channel. There can be homomeric and heteromeric connexons and homotypic and heterotypic channels.
What is the extracellular matrix usually made of?
GAG or glycosaminoglycans which are large charged polysaccharides that are made of the repeating disaccharide amino sugar + uronic acid.
ECM is also made of collagens which are three tripple alpha helices where every third amino acid is glycerin. Provides connective tissue with mechanical strength.
Glycoproteins which are GAG + protein and are used to attach epithelial to basal lamina.
Describe the components used to attach epithelial to the basal lamina.
Laminin which is a glycoprotein that connects to itself and perlecan and integrin aswell as nidogen. Type IV collagen binds to itself and nidogen aswell as perlecan. This creates a mesh in which cell cans adhere to the basal lamina.
What are integrins and how do they work?
Integrins are transmembrane receptors that are split into two parts, alpha and beta. Once activated from the cytosolic side, the two chains will “split” and they can then connect to laminin. Can be activated by signal molecule kindlin or other intra/extracellular signals. They are used in hemidesmosome and actin-linked-cell-matrix junction. In actin-linked-cell-matrix junction integrins bind to the protein Talin which then binds to actin filament by vinculin.