Cytology Flashcards
Integral membrane proteins
have a hydrophobic region which is embedded into the hydrophobic core of the membrane
Transmembrane proteins
are integral membrane proteins that extend all the way through the membrane.
Peripheral Membrane Proteins
are not embedded within the lipid bilayer and attach either to integral proteins or to the hydrophilic heads of the membrane lipids.
Transport proteins
The lipid bilayer forms a barrier which is impassible for charged and polar molecules. Transport proteins selectively allow such molecules to cross the membranes
channel/carrier/pump
Channel proteins
form “pores”, which allow passage of small molecules across the membrane via passive diffusion. Channels are ion-selective.
Carrier proteins
“drag” other molecules through the membrane by hiding them in a cleft in the protein
Pumps
use ATP energy to pump ions actively through the membrane
Receptors
Some transmembrane proteins bind to specific molecules in the extracellular matrix. This specific binding can result in a conformational change in the transmembrane protein that can serve as a signal that allows the cell to adapt to its environment
Structural or anchoring proteins
serve to attach cell to its surroundings. These transmembrane proteins use their cytoplasmic domains to link to the elements of the cytoskeleton, and their extracellular domains to link to the extracellular proteins
Carbohydrates
mostly oligosaccharides are often attached to the extracellular domains of membrane proteins and lipids to form glycoproteins and glycolipids. Because of the large amount of carbohydrates attached to proteins and lipids on the external surface many cells exhibit a “fuzzy” coating called the glycocalyx, which can be visualized in an electron microscope.
Particles and inclusions
used for synthesis and storage. The two main types are ribosomes and glycogen particles.
Ribosomes
are RNA/protein particles that catalyze protein synthesis. They bring together mRNA and tRNA to synthesize a polypeptide.
a. Ribosomes are 15-25 nm in size and consist of a small subunit and a large subunit. Each subunit consists of one or more ribosomal RNA (rRNA) and many specialized proteins.
b. Ribosomes in eukaryotic cells exist as either free ribosomes, mitochondrial ribosomes, or ribosomes bound to rough endoplasmic reticulum (RER). The majority of cellular proteins are synthesized on free ribosomes, except those in Golgi apparatus, lysosomes, secretory granules, and plasma membrane, which are synthesized on RER ribosomes. 20 % of mitochondrial proteins are synthesized on mitochondrial ribosomes, the rest are synthesized on free ribosomes in the cytoplasm.
c. Polysomes. During protein synthesis many ribosomes attach to a single mRNA molecule. This string of ribosomes connected to mRNA is known as a polysome.
Glycogen particles
are a storage form of polysaccharides
Endoplasmic reticulum (ER)
consists of series of membrane-formed anastomosing tubules and cisternae (flattened, pancake-like vesicles). The ER is subdivided into smooth and rough endoplasmic reticulum. The cytoplasmic side of the rough ER has a large number of ribosomes bound to it.
Smooth endoplasmic reticulum (SER)
does not have ribosomes bound to its surface and it also has a more tubular appearance than the rough ER. SER has several functions:
a. One of the most important functions of SER is lipid and steroid metabolism. Phospholipids for all cell’s membranes are produced here, so the SER is involved in membrane synthesis and recycling. SER is rather inconspicuous in most cells, but becomes prominent in steroid-secreting cells.
b. SER plays an important role in detoxification of noxious substances. It is very well-developed in liver cells and contains enzymes that can modify and detoxify such toxins as carcinogens, pesticides, etc.
c. SER is involved in glycogen metabolism.
Rough endoplasmic reticulum (RER)
has ribosomes bound to its surface, which creates its “roughened” appearance. RER is formed mostly of cisternae. RER is prominent in cells specialized for protein secretion, so it is the principal site of synthesis of proteins destined for export out of the cell. Proteins found in the Golgi apparatus, lysosomes, and in the plasma membrane are also synthesized in the RER.
Golgi apparatus
consists of series of stacked, flattened, membrane-limited cisternae and tubular extensions. Golgi receives proteins synthesized in the RER. The stack of Golgi cisternae is polarized. The side receiving vesicles from the RER is cis Golgi. The middle cisternae form the medial Golgi, and the cisternae from which the mature proteins are transported form the trans Golgi. The Golgi apparatus functions in the posttranslational modification, sorting, and packaging of proteins.
Functions of Golgi
- The modification of proteins, such as adding or removing sugar residues, sulfate or phosphate groups, occurs in the Golgi apparatus. The early stages of this process occur in the cis Golgi, intermediate steps occur in the medial Golgi, and the final modifications are made in the trans Golgi.
- Sorting and packaging of proteins into transport vesicles is another important function of the Golgi apparatus that occurs mainly in the trans Golgi network. From here there are three main destinations for the proteins. Most proteins coming from the Golgi apparatus bear specific signal sequences, which direct them to their destination.
3 destinations of golgi
secretory vesicles
lysosomes
constitutive pathway
Secretory vesicles
Many cells, e.g. pancreatic acinar cells, store proteins and other products in secretory vesicles. These vesicles undergo a maturation process in which secretory proteins are retained within the vesicle. Mature secretory vesicles eventually fuse with the plasma membrane to release the secretory product into the extracellular space in response to a certain signal.
Lysosomes
are spherical organelles of variable size produced by the Golgi. Lysosomes are involved in digesting the material taken up from outside the cell and in degradation of senescent organelles. They are characterized by a low pH and presence of hydrolytic enzymes. The principal sorting signal which directs proteins from the trans Golgi network to the lysosome is mannose-6-phosphate.
Mannose-6-Phosphate deficiency
Mutation of one of the enzymes that creates this signal causes the lysosomal proteins to be secreted into the intercellular space. The resulting condition is the so-called I-cell disease (or mucolipidosis), which is one of the lysosomal storage diseases.
Primary Lysosomes
are lysosomes which have not yet received substrates for digestion.
Secondary Lysosomes
result from the fusion of primary lysosomes with their target.
Lipofuscin Granules
or residual bodies are senescent lysosomes with undigestible material.
Constitutive pathway
Proteins in the trans Golgi, which are not destined for either lysosomes or secretory granules are sorted into small vesicles, which are transported directly to the plasma membrane, where the vesicle fuses with the plasma membrane. Integral membrane proteins and proteins that are secreted continuously into the extracellular space (e.g. collagen) reach the plasma membrane by this route