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CHAPTER Cellular Membranes Membrane Structure

2 Two main roles


§  Isolate cells from the environment
Chemistry,
§  Control of intracellular conditions
Biochemistry, and Cell
Physiology §  Organize intracellular pathways into subcellular
Part 3 compartments

PowerPoint® Lecture Slides prepared by


Stephen Gehnrich, Salisbury University

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Lipid Profile Membrane Properties of Cholesterol Membrane Heterogeneity

§  Lipid bi-layer More PE and PS phosphoglycerides in inner leaflet


§  Phospholipids
More PC phosphoglycerides in the outer leaflet
§  Primarily phosphoglycerides
§  Other lipids Glycolipids only in the outer leaflet
§  Sphingolipids Lipid rafts
§  Alter electrical properties
§  Enriched in glycolipids and cholesterol
§  Glycolipids
§  Communication between cells §  More rigid and thicker
§  Cholesterol
§  Increase fluidity while decreasing permeability

Figure 2.44
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Membrane Heterogeneity Membrane Fluidity Temperature and Membrane Fluidity

§  Environmental conditions affect membrane fluidity


§  For example, low temperature increases van der Waals
forces between lipids and restricts movement
§  Homeoviscous adaptation
§  Cell keeps membrane fluidity constant by altering the
lipid profile

Figure 12.45 Figure 2.46


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Membrane Proteins Membrane Proteins Membrane Transport

§  Can be more than half of the membrane mass §  Cells must transport molecules across membranes
§  Structural and regulatory functions §  Three main types of transport:
§  Two main types §  Passive diffusion
§  Integral membrane proteins §  Facilitated diffusion
§  Tightly bound to the membrane §  Active transport
§  Embedded in bilayer or spanning the entire membrane Distinguished by direction of transport, nature of the
§  Peripheral membrane proteins carriers, and the role of energy
§  Weaker association with the lipid bilayer

Figure 2.47
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Membrane Transport Passive Diffusion Facilitated Diffusion

§  Lipid-soluble molecules §  Hydrophilic molecules


§  No specific transporters are needed §  Protein transporter is needed
§  Molecules cross lipid bilayer §  No energy is needed
§  No energy is needed §  Depends on concentration gradient
§  Depends on concentration gradient §  High concentration à low concentration
§  High concentration à low concentration §  Steeper gradient results in faster rates
§  Steeper gradient results in faster rates

Figure 2.48
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Facilitated Diffusion Ion Channels Active Transport

Three main types of protein carriers: §  Protein transporter is needed


§  Ion channels §  Energy is required
§  Small pores for specific ions
§  Molecules can be moved from low to high
§  Open and close in response to cellular conditions
§  “Gated” channels concentration
§  Porins
§  Like ion channels, but for larger molecules
§  Permeases
§  Function more like an enzyme
§  Carries molecule across membrane

Figure 2.49
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Active Transport Primary Active Transport Secondary Active Transport

Two main types of active transport §  Hydrolysis of ATP provides energy §  Use energy in electrochemical gradient of one
§  Primary active transport §  Transporters are ATPases molecule to drive another molecule against its
§  Direct use of an exergonic reaction §  Three types gradient
§  P-type §  Antiport or exchanger carrier: molecules move in
§  Secondary active transport
§  Pump specific ions (e.g., Na+, K+, Ca2+)
opposite directions
§  Couples the movement of one molecule to the
§  F-type and V-type §  Symport or cotransporter carrier: molecules move in
movement of a second molecule
the same direction
§  Pump H+
§  Distinguished by the source of energy
§  ABC type
§  Carry large organic molecules (e.g., toxins)

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Electrical Gradients Membrane Potential (Vm) Equilibrium Potential (Eion)

§  All transport processes affect chemical gradients §  Difference in charge inside and outside the cell Each ion has its own equilibrium potential
§  Some transport processes affect electrical gradients membrane §  Ion concentration gradient
§  Electroneutral carriers §  Concentration gradients formed by active transport
§  Ion diffuses down its concentration gradient
§  Transport uncharged molecules or exchange an equal §  Two main functions
number of particles with the same charge §  Eion is the Vm at which the ion is at electrochemical
§  Provide energy for membrane transport equilibrium
§  Electrogenic carriers
§  Changes in membrane potential used by cells in cell-
§  Transfer a charge §  Depends upon the size of the concentration gradient
to-cell signaling
§  For example, Na+/K+ATPase à exchanges 3Na+ for §  Eion can be calculated using the Nernst equation
2K+ §  Assumes electrochemical equilibrium

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Equilibrium Potential (Eion) Membrane Potential (Vm) Changes in Membrane Potential (Vm)

§  Cell membranes are not at equilibrium Changes in membrane permeability cause changes in
§  Varying permeability membrane potential
§  Multiple ion gradients §  Depolarization
§  Goldman equation §  Cell becomes more positive on the inside
§  Accounts for permeability and multiple ions §  For example, if Na+ ions enter
§  Vm is most dependent upon Na+, K+, and Cl– §  Hyperpolarization
§  Na+/K+ ATPase maintains Na+ and K+ gradients §  Cell becomes more negative on the inside
across membrane §  For example, if K+ ions leave

Figure 2.50
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Depolarization and Hyperpolarization Cellular Structures Mitochondria

§  Eukaryotic cells share many common cellular §  Produce most of the cell’s ATP
compartments §  Intricate network of internal membranes
§  Large surface area
§  Compartmentalization allows for regulation of
§  Mitochondrial reticulum
specific processes
§  Network of interconnected mitochondria
§  Mitochondrial DNA (mtDNA)
§  Some mitochondrial proteins
§  Required for mitochondrial biogenesis
§  Most genes for mitochondrial proteins are in the nucleus

Figure 2.51
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Mitochondria Cytoskeleton Functions of the Cytoskeleton

Network of protein-based fibers §  Maintains cell structure


§  Microfilaments §  External cell shape
§  Flexible chains of actin
§  Organization of intracellular membranes
§  Microtubules
§  Tubes of tubulin §  Cellular processes
§  Intermediate filaments §  Movement
§  Composed of many types of monomers §  Motor proteins
Maintains cell structure §  Signal transduction
§  External cell shape
§  Organization of intracellular membranes
Cellular processes
For example, movement, signal transmission

Figure 2.52
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Cytoskeleton Endoplasmic Reticulum and Golgi Apparatus Intracellular Traffic

§  Membranous organelles


§  Proteins are made on the ER
§  Proteins are modified and packaged into vesicles by the
Golgi apparatus
§  Vesicles carry proteins between compartments
§  Vesicles are carried throughout the cell by motor proteins
moving on cytoskeletal tracks
§  Contents of vesicles can be released from the cell via exocytosis
§  Extracellular substances can be taken into the cell via
endocytosis

Figure 2.23a,b Figure 2.54


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Extracellular Matrix Extracellular Matrix Extracellular Matrix

§  Gel-like “cement” between cells Molecules of the extracellular matrix


§  Cell membranes are bonded to the matrix §  Proteins
§  Insect exoskeleton, vertebrate skeleton, and mollusc §  Glycoproteins
shells are modified extracellular matrices
§  Glycosaminoglycans
§  Molecules of the matrix are synthesized within the
§  Proteoglycans
cells and secreted by exocytosis

Figure 2.55
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Extracellular Matrix Extracellular Matrix Physiological Genetics and Genomics

Cells can break down the extracellular matrix with Physiological diversity resides in genes
matrix metalloproteinases §  How genes differ between species
Cells can move through tissues by controlling the §  How genes are regulated in individual cells
production and breakdown of the matrix Homeostatic regulation depends upon having
§  For example, blood vessel growth and penetration §  the right protein,
§  in the proper place,
§  at the proper time,
§  with the appropriate activity

Figure 2.56
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Nucleic Acids Nucleic Acids DNA

Two types: §  DNA and RNA are polymers of nucleotides §  Double-stranded α-helix
§  DNA – deoxyribonucleic acid §  linked by phosphodiester bonds §  Two strands of nucleotides linked by hydrogen bonds
§  Genetic blueprint §  Complementary strands
§  Nucleotide
§  Genes in nucleus §  Antiparallel
§  Nitrogenous base
§  RNA – ribonucleic acid §  Nucleotides can form bonds with only one other
§  Cytosine, Adenine, Guanine,Thymine (DNA only), Uracil
§  Read and interpret DNA to make protein nucleotide
(RNA only)
§  Three main forms §  A + T: two hydrogen bonds
§  Transfer RNA (tRNA)
§  Sugar
§  Deoxyribose (DNA), ribose (RNA) §  G + C: three hydrogen bonds
§  Ribosomal RNA (rRNA)
§  Messenger RNA (mRNA) §  Phosphate

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Structure of DNA Histones DNA Organization

§  Mammalian DNA is several meters long §  Genome


§  Entire collection of DNA within a cell
§  DNA is compressed by DNA-binding proteins
(histones) §  Chromosome
§  Separate segments of DNA
§  DNA in this form is referred to as chromatin
§  Genes
§  Advantages of compression by histones §  DNA sequence within a chromosome
§  Large amounts of DNA fit into small volumes §  Used to produce RNA
§  Reduces damage caused by radiation and chemicals §  Exons
§  Must be uncompressed for DNA and RNA §  Segments of DNA that encode RNA
synthesis §  Introns
§  Interspersed DNA sections between exons

Figure 2.57
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DNA Organization Genome Size Transcription

Synthesis of messenger RNA (mRNA)


§  DNA is wrapped by histones
§  Must be unwrapped to allow transcription
§  Transcription regulators form regulatory complexes
at promoter
§  Region of the gene where transcription begins
§  mRNA synthesis begins

Figure 2.58 Figure 2.59


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Transcription Mature mRNA Protein Synthesis (Translation)

§  Primary mRNA transcript §  Ribosomes


§  Exons – sequences that will code for the protein §  Made of rRNA and proteins
§  Introns – noncoding sequences
§  Bound to endoplasmic reticulum
§  Introns are removed and exons are spliced together
§  Catalyze the formation of peptide bonds between
§  mRNA is polyadenylated
amino acids
§  200+ adenosines are added to the 3´ end
§  poly A+ tail §  Transfer RNA (tRNA)
§  mRNA is exported from the nucleus to the cytoplasm §  Carry the amino acids that bind to a codon (three
§  mRNA is ultimately degraded by nucleases (RNases) nucleotides on mRNA)

Figure 2.60
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Protein Degradation Protein Isoforms Origins of Protein Isoforms

§  Proteins may have structural changes that result in §  Variations in protein structure
dysfunction §  Genetic rearrangements
§  Structural changes recruit enzymes that mark the §  Alternative splicing of exons
protein with a small protein called ubiquitin §  Alleles
§  Ubitquitin-labeled protein is then bound by a large §  Gene duplications
enzyme complex called a proteasome §  Subsequent mutation of some copies
§  Enzymes degrade the protein to amino acids

Figure 2.61
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Genome Duplication

Figure 2.62
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