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Ankyrin:: Complex of Five Subunits, Having A Binding Site For Acetylcholine
Ankyrin:: Complex of Five Subunits, Having A Binding Site For Acetylcholine
of the red blood cell, but none of these proteins is attached directly to the
membrane. The network of proteins is instead atta- ched to another peripheral
protein called ankyrin.
Ankyrin has a molecular weight 200,000. The protein has 2 domains: One binds
to spectrin, and the other to the N-terminal region of band-3-protein that extends
into the cytoskeleton.
It is now known that the protein network can also be bound directly to
glycophorin (integral protein) or to band-3-protein.
Acetylcholine released from the presynaptic region binds with the binding site of
postsynaptic region, which triggers the opening of the channel and influx of Na +.
• Highly selective.
CLINICAL ASPECT
Defect: They result from mutations in the genes coding for proteins of the membrane
defective spectrin that is unable to bind either ankyrin or band 4, 1 protein and in so
absent.
II. Functions:TransportSystems
An essential role of biomembranes is to allow movement of all compounds
necessary for the normal function of a cell across the membrane barrier. These
compounds include a vast array of substances like sugars, amino acids, fatty
acids, steroids, cations and anions to mention a few. These compounds must
enter or leave the cells in an orderly manner for normal functioning of the cell.
A. 1. Ion Channels
Cation conductive channels are negatively charged within the channel and have
an average diameter of about 5 to 8 nm.
All ion channels are basically made up of trans- membrane subunits that come
together to form a central pore through which ions pass selectively.
All channels have gates, and are controlled by opening and closing.
Types of Gates
2. Ionophores
In certain cells, e.g. in red blood cells, and cells of the collecting ductules of the
kidney, the movement of water by simple diffusion is enhanced by movements
of water through water channels, composed of tetrameric transmembrane
proteins called aquaporins. About five distinct types of aquaporins have been
recognised.
4. Gap Junction
Certain cells develop specialised regions on their memb- ranes for intercellular
communications which are in close proximity.Function: They mediate and
regulate the passage of ions and small molecules upto 1000 to 2000 mol wt,
through a narrow hydrophilic core connecting the cytosol of adjacent cells.
CLINICAL ASPECT
Recently mutations in the gene encoding AP-2 (Aqua- porin 2) protein, have been sho
nephrogenic diabetes insipidus.
SECTION ONE