Study Set Content:
Inhibitors of receptors tyrosine kinase are finding increased
use in
in neoplastic disorders
Inhibitors of receptors tyrosine kinase are finding increased
use in neoplastic disorders in which (blank) is often involved.
excessive growth factors
signaling
Some of these inhibitors are
(blank) (eg. trastuzumab, cetuximab), which bind
to the extracellular domain of a particular receptor and interfere with
the binding of growth factors.
monoclonal antibodies
The intensity and duration of action of epidermal growth factor EGF,
platelet-derived growth factor PDGF, and other agents that act via
receptor tyrosine kinase are limited by a process called
receptor
down-regulation.
means there is a decrease in total receptor
number in the cell. This is due to endocytosis and subsequent degradation
of the receptors that is caused by long term exposure to agonists.
Receptor down-regulation
Ligand binding often induces accelerate(blank) of receptors
from the cell surface,
endocytosis
Ligand binding often induces accelerate endocytosis of receptors
from the cell surface, followed by the (blank) of those receptors
(and their bound ligands).
degradation
Ligand binding often induces accelerate endocytosis of receptors
from the cell surface, followed by the degradation of those receptors
(and their bound ligands). When this process occurs at a rate(blank)
than de novo synthesis of receptors, the total number of cell-surface
receptors is (blank) (down-regulated), and the cell’s
responsiveness to ligands is correspondingly diminished.
faster, reduced
Cytokine receptors respond to a heterogeneous group of
peptide ligands,
peptide ligands, which include
growth hormone, erythropoietin,
several kinds of interferon, and other regulators of growth and
differentiation.
These receptors use a mechanism (Figure 2-8) closely resembling
that of receptor
tyrosine kinase,
These receptors use a mechanism (Figure 2-8) closely resembling
that of receptor tyrosine kinase, except that in this case, the
protein tyrosine kinase activity is not (blank) to the receptor molecule
intrinsic,
These receptors use a mechanism (Figure 2-8) closely resembling
that of receptor tyrosine kinase, except that in this case, the
protein tyrosine kinase activity is not intrinsic to the receptor
molecule, instead of a separate protein tyrosine kinase, from
the
Janus-kinase (JAK) family,
These receptors use a mechanism (Figure 2-8) closely resembling
that of receptor tyrosine kinase, except that in this case, the
protein tyrosine kinase activity is not intrinsic to the receptor
molecule, instead of a separate protein tyrosine kinase, from
the Janus-kinase (JAK) family, binds (blank)to the
receptor.
non-covalently
Cytokine
receptors, like receptor tyrosine
kinases, have extracellular and
intracellular domains and form
dimers
However, after
activation by an appropriate
ligand, separate mobile protein
tyrosine kinase molecules (JAK)
are activated, resulting in
phosphorylation of signal
transducers and activation of
transcription
(STAT) molecules.
STAT dimers then travel to the
nucleus, where they regulate
transcription
Many of the most useful in clinical medicine act by (blank)the actions of endogenous ligands that regulate the
flow of ions through plasma membrane channels.
mimicking or
blocking
The natural ligands are
acetylcholine, serotine, GABA, and
glutamate.
The natural ligands are acetylcholine, serotine, GABA, and
glutamate. All of these agents are
synaptic transmitters.
