Studies On the Coxsackie and Adenovirus Receptor
Functional Studies On the Coxsackie and Adenovirus Receptor (CAR) in Skeletal Muscle Cells
Lieferzeit: Print on Demand - Lieferbar innerhalb von 3-5 Werktagen I
ISBN-13:
9783639151831
Seiten:
88
Autor:
Yunlin Tai
Format:
220x176x33 mm
Sprache:
Englisch
Beschreibung:
CAR has recently been identified as a high affinity
receptor for both Coxsackievirus and certain
adenovirus (AV) serotypes. Virus bound by CAR is
passed to integrins which bind an RGD (Arg-Gly-Asp)
sequence in the viral penton base protein and act as
secondary receptors responsible for virus
internalization.
Recent studies have shown that, in integrin-
expressing cells, CAR can directly mediate AV uptake
without penton base RGD-av integrin interactions. I
confirmed that EC+ transmembrane (TM) domains of CAR
are sufficient for AV uptake in integrin-expressing
cells.
CAR is the primary AV receptor and integrins are
secondary AV receptors. To investigated the
possibility that these proteins associate in a
functional complex in the cell membrane, I forced
CAR expression in a line of human myoblasts and
obtained coprecipitation of CAR and B3 integrin
suggesting these proteins may associate.
I also found that mouse brain extract reproducibly
modifies the immunoreactivity of the CAR C-terminal
fusion protein and increase its tendency to
dimerize. Mouse brain extracts also modified the
isoelectric pH of the CAR C-terminal fusion protein.
receptor for both Coxsackievirus and certain
adenovirus (AV) serotypes. Virus bound by CAR is
passed to integrins which bind an RGD (Arg-Gly-Asp)
sequence in the viral penton base protein and act as
secondary receptors responsible for virus
internalization.
Recent studies have shown that, in integrin-
expressing cells, CAR can directly mediate AV uptake
without penton base RGD-av integrin interactions. I
confirmed that EC+ transmembrane (TM) domains of CAR
are sufficient for AV uptake in integrin-expressing
cells.
CAR is the primary AV receptor and integrins are
secondary AV receptors. To investigated the
possibility that these proteins associate in a
functional complex in the cell membrane, I forced
CAR expression in a line of human myoblasts and
obtained coprecipitation of CAR and B3 integrin
suggesting these proteins may associate.
I also found that mouse brain extract reproducibly
modifies the immunoreactivity of the CAR C-terminal
fusion protein and increase its tendency to
dimerize. Mouse brain extracts also modified the
isoelectric pH of the CAR C-terminal fusion protein.