Documenti di Didattica
Documenti di Professioni
Documenti di Cultura
Rina Susilowati
Department of Histology and Cell Biology
Faculty of Medicine Gadjah Mada University
Macromolecule
Organ
Organism
Organelle
Cell
Tissue
Contents
Contents
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Phosphoglycerides
50-90
Phosphatidylcholine
40-60
Phosphatidylethanolamine
20-30
Phsphatidylserine
5-15
Cardiolipin
0-20
Phosphatidylinositol
5-10
Sphingomyelin
5-20
Cholesterol
0-10
Aquaporin
The structure of
aquaporin, a waterchannel protein
[Adapted from A. Chang et
al., 1997, Nature 387:627.]
Contents
Genome
Total genetic information stored in the
chromosomes
Human genome: 3x109 nucleotide pairs
24 different DNA molecules in the nucleus
of human cells
Utilization of different coats in vesicular traffic. Different coat proteins select different cargo and shape
the transport vesicles that mediate the various steps in the biosynthetic- secretory and endocytic pathways.
When the same coats function in different places in the cell, they can incorporate different coat protein
subunits that modify their properties (not shown). Many differentiated cells have additional pathways beside
those shown in this figure, including a sorting pathway from the trans Golgi network to the apical surface in
polarized cells and a specialized recycling pathway for proteins of synaptic vesicles in the synapses of
neurons
Clathrin-coated
pits and vesicles.
This rapid-freeze,
deep-etch electron
micrograph shows
numerous clathrincoated pits and
vesicles on the inner
surface of the
plasma membrane
of cultured
fibroblasts. The cells
were rapidly frozen
in liquid helium,
fractured, and deepetched to expose the
cytoplasmic surface
of the plasma
membrane. (From J.
Heuser, J. Cell Biol.
84:560 583, 1980.
Three pathways to degradation in lysosomes. (A) Each pathway leads to the intracellular
digestion of materials derived from a different source. (B) An electron micrograph of an
autophagosome containing a mitochondrion and a peroxisome. (B, courtesy of Daniel S. Friend,
from D.W. Fawcett, A Textbook of Histology, 12th edn. New York: Chapman and Hall, 1994.)
Contents
Mitochondria and
cellular energy
Peroxisome
Contents
To be engulfed by phagocytes
No spllilage, no inflammation
Contents
The cytoskeleton
Figure 11.45. Microtubule motor proteins Kinesin and dynein move in opposite directions along microtubules, toward the plus and minus ends, respectively. Kinesin consists of two heavy chains, wound around each
other in a coiled-coil structure, and two light chains. The globular head domains of the heavy chains bind microtubules and are the motor domains of the molecule. Dynein consists of two or three heavy chains (two are
shown here) in association with multiple light and intermediate chains. The globular head domains of the heavy chains are the motor domains.
Transport of vesicles along microtubules Kinesin and other plus end-directed members of the
kinesin family transport vesicles and organelles in the direction of microtubule plus ends, which
extend toward the cell periphery. In contrast, dynein and minus end-directed members of the
kinesin family carry their cargo in the direction of microtubule minus ends, which are anchored in
the center of the cell.
The surface of an ependymal cell contains basal bodies (arrows) connected to the microtubules of
cilia, seen here in longitudinal section. Several microvilli are also present. 37,000
Movement of microtubules in cilia and flagella The bases of dynein arms are attached to A
tubules, and the motor head groups interact with the B tubules of adjacent doublets. Movement
of the dynein head groups in the minus end direction (toward the base of the cilium) then causes
the A tubule of one doublet to slide toward the base of the adjacent B tubule. Because both
microtubule doublets are connected by nexin links, this sliding movement forces them to bend.
Contents
Cell junction,
cell-cell
adhesion and
extracellular
matrix
Adhesion molecules in junctions involved in cell-cell adhesion. Adherens junctions and desmosomes
are specialized cell-cell junctions that consist of clustered-cadherin dimers. Cadherin is connected to either
the circumferential belt of actin filaments or bundles of keratin filaments in the cytoskeleton through the
catenin adapter proteins.
Structure of gap junctions. (a) In this model, a gap junction is a cluster of channels between two plasma
membranes that are separated by a gap of about 2 3 nm. (b) Both membranes contain connexon
hemichannels, cylinders of six dumbbell-shaped connexin subunits. (c) Each connexin subunit has four
transmembrane a helices. Two connexons join in the gap between the cells to form a gap-junction channel,
1.5 2.0 nm in diameter, that connects the cytoplasm of the two cells.
Contents
Molecular
mechanism in
signal
transduction:
basic cell
signalling
pathways
Three classes of
cell-surface
receptors
Contents
Contents