Detail
Článek
Článek online
FT
Medvik - BMČ
  • Je něco špatně v tomto záznamu ?

Shb is a ubiquitously expressed Src homology 2 protein

M Welsh, J Mares, T Karlsson, C Lavergne, B Breant, L Claesson-Welsh

. 1994 ; 9 (1) : 19-27.

Jazyk angličtina Země Velká Británie

Typ dokumentu práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc13036797

Grantová podpora
PL456 MZ0 CEP - Centrální evidence projektů

To identify serum-inducible genes in the insulin-producing cell line beta TC-1, a library subtraction screening procedure was performed on serum-deprived (G0) and serum-restimulated (G1) insulin-producing beta TC-1 cells. A cDNA containing a motif with strong homology to Src homology 2 (SH2) domains was found using this procedure and called Shb. The Shb cDNA contains two methionine codons in its N-terminus and thus may code for two proteins of 67 and 56 kDa, each with one SH2 domain in its C-terminus. No other structural similarity to proteins with catalytic activity could be detected, suggesting that Shb is a so called adaptor. Shb contains the proline-rich sequence PPPGPGR between the two proposed initiator methionines which resembles a sequence for binding to Src homology 3 (SH3) domains. A second proline-rich sequence was detected after the second methionine codon. The Shb cDNA hybridized to a similar or identical mRNA of 3.1 kb expressed in mouse brain, liver, kidney, heart, NIH3T3 fibroblasts and beta TC-1 cells. Western blot analysis of the same tissues using an antiserum directed against a synthetic peptide corresponding to a part of the SH2 domain of Shb, revealed reactivity with two proteins of 56 and 67 kDa. In addition, a third reactive component of 40 kDa was detected in most tissues. Transfection and transient expression of the Shb cDNA in COS-1 cells yielded increased expression of the 67, 56 and 40 kDa proteins. Transfection and stable expression of the Shb cDNA in pig aortic endothelial cells showed increased expression primarily of the 67 kDa protein. A fusion protein consisting of the SH2 domain of Shb linked to glutathione S-transferase showed increased binding to glycoproteins of cells stimulated with platelet-derived growth factor (PDGF-BB). Furthermore, the autophosphorylated PDGF beta-receptor but not the autophosphorylated epidermal growth factor (EGF) receptor bound specifically to immobilized fusion protein. It is concluded that Shb is a novel SH2-containing protein with proline-rich domains and therefore probably involved in the signal-transduction of some ligand-activated tyrosine kinase receptors.

Bibliografie atd.

Literatura

000      
00000naa a2200000 a 4500
001      
bmc13036797
003      
CZ-PrNML
005      
20131129145449.0
007      
ta
008      
131118s1994 xxka f 000 0|eng||
009      
AR
035    __
$a (PubMed)8302579
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxk
100    1_
$a Welsh, Michael $u Department of Medical Cell Biology, Uppsala University, Sweden
245    10
$a Shb is a ubiquitously expressed Src homology 2 protein / $c M Welsh, J Mares, T Karlsson, C Lavergne, B Breant, L Claesson-Welsh
504    __
$a Literatura
520    9_
$a To identify serum-inducible genes in the insulin-producing cell line beta TC-1, a library subtraction screening procedure was performed on serum-deprived (G0) and serum-restimulated (G1) insulin-producing beta TC-1 cells. A cDNA containing a motif with strong homology to Src homology 2 (SH2) domains was found using this procedure and called Shb. The Shb cDNA contains two methionine codons in its N-terminus and thus may code for two proteins of 67 and 56 kDa, each with one SH2 domain in its C-terminus. No other structural similarity to proteins with catalytic activity could be detected, suggesting that Shb is a so called adaptor. Shb contains the proline-rich sequence PPPGPGR between the two proposed initiator methionines which resembles a sequence for binding to Src homology 3 (SH3) domains. A second proline-rich sequence was detected after the second methionine codon. The Shb cDNA hybridized to a similar or identical mRNA of 3.1 kb expressed in mouse brain, liver, kidney, heart, NIH3T3 fibroblasts and beta TC-1 cells. Western blot analysis of the same tissues using an antiserum directed against a synthetic peptide corresponding to a part of the SH2 domain of Shb, revealed reactivity with two proteins of 56 and 67 kDa. In addition, a third reactive component of 40 kDa was detected in most tissues. Transfection and transient expression of the Shb cDNA in COS-1 cells yielded increased expression of the 67, 56 and 40 kDa proteins. Transfection and stable expression of the Shb cDNA in pig aortic endothelial cells showed increased expression primarily of the 67 kDa protein. A fusion protein consisting of the SH2 domain of Shb linked to glutathione S-transferase showed increased binding to glycoproteins of cells stimulated with platelet-derived growth factor (PDGF-BB). Furthermore, the autophosphorylated PDGF beta-receptor but not the autophosphorylated epidermal growth factor (EGF) receptor bound specifically to immobilized fusion protein. It is concluded that Shb is a novel SH2-containing protein with proline-rich domains and therefore probably involved in the signal-transduction of some ligand-activated tyrosine kinase receptors.
590    __
$a bohemika - dle Pubmed
650    12
$a adaptorové proteiny signální transdukční $7 D048868
650    02
$a sekvence aminokyselin $7 D000595
650    02
$a zvířata $7 D000818
650    02
$a sekvence nukleotidů $7 D001483
650    02
$a buněčné linie $7 D002460
650    02
$a komplementární DNA $x chemie $7 D018076
650    02
$a regulace genové exprese $7 D005786
650    12
$a geny src $7 D016391
650    02
$a lidé $7 D006801
650    02
$a Langerhansovy ostrůvky $x metabolismus $7 D007515
650    02
$a myši $7 D051379
650    02
$a molekulární sekvence - údaje $7 D008969
650    02
$a tyrosinkinasy $x fyziologie $7 D011505
650    12
$a protoonkogenní proteiny $x analýza $x fyziologie $7 D011518
650    02
$a sekvenční homologie aminokyselin $7 D017386
650    02
$a signální transdukce $7 D015398
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Mareš, Jaroslav, $d 1951- $7 jo20010082326 $u Institute of Biology and Medical Genetics, Charles University, Prague, Czech Republic
700    1_
$a Karlsson, Torbjörn $u Department of Medical Cell Biology, Uppsala University, Sweden
700    1_
$a Lavergne, Corinne $u INSERM, U55, Hôpital St-Antoine, Paris, France
700    1_
$a Bréant, Bernadette $u INSERM, U55, Hôpital St-Antoine, Paris, France
700    1_
$a Claesson-Welsh, Lena $u Ludwig Institute for Cancer Research, Uppsala University, Sweden
773    0_
$t Oncogene $x 0950-9232 $g Roč. 9, č. 1 (1994), s. 19-27 $p Oncogene $w MED00003600
773    0_
$p Oncogene $g 9(1):19-27, 1994 Jan $x 0950-9232
910    __
$a ABA008 $b B 1746 $y 4 $z 0
990    __
$a 20131118144651 $b ABA008
991    __
$a 20131129150125 $b ABA008
999    __
$a ok $b bmc $g 1001066 $s 835285
BAS    __
$a 3
BMC    __
$a 1994 $b 9 $c 1 $d 19-27 $x MED00003600 $i 0950-9232 $m Oncogene $n Oncogene
GRA    __
$a PL456 $p MZ0
LZP    __
$a 2013-11/gvbo

Najít záznam

Citační ukazatele

Pouze přihlášení uživatelé

Možnosti archivace