scholarly journals The uptake of amino acids and the synthesis of amines by neoplastic mast cells in culture

1962 ◽  
Vol 164 (2) ◽  
pp. 210-226 ◽  
Author(s):  
Margaret Day ◽  
J. P. Green
1988 ◽  
Vol 448 (1) ◽  
pp. 46-52 ◽  
Author(s):  
Ann Kingsbury ◽  
Vittorio Gallo ◽  
Robert Balazs

2018 ◽  
Vol 27 (11) ◽  
pp. 1298-1303 ◽  
Author(s):  
Magda Babina ◽  
Zhao Wang ◽  
Metin Artuc ◽  
Sven Guhl ◽  
Torsten Zuberbier

Blood ◽  
1996 ◽  
Vol 87 (1) ◽  
pp. 273-283 ◽  
Author(s):  
T Tsujimura ◽  
M Morimoto ◽  
K Hashimoto ◽  
Y Moriyama ◽  
H Kitayama ◽  
...  

Abstract A peculiar point mutation results in constitutive activation of c-kit receptor tyrosine kinase (KIT) in three different tumor mast cell lines; ie, the HMC-1, P-815, and RBL-2H3. Because constitutive activation of KIT was also observed in the FMA3 mouse mastocytoma cell line, we investigated the molecular mechanism. Sequencing of the whole coding region of the c-kit showed that the point mutation found in HMC- 1, P-815, and RBL-2H3 cells was absent in FMA3 cells and that the c-kit cDNA of FMA3 cells carried an in-frame deletion of 21 base pairs (bp) encoding Thr-Gln-Leu-Pro-Tyr-Asp-His at codons 573 to 579 at the juxtamembrane domain. The FMA3-type c-kit cDNA with 21 bp deletion was introduced into the IC-2 cell line, which was derived from murine cultured mast cells. IC-2 cells were dependent on interleukin (IL)-3 and did not express KIT on the surface. In IC-2 cells introduced with the FMA3-type c-kit cDNA, KIT was constitutively phosphorylated on tyrosines and activated. Moreover, the FMA3-type KIT was dimerized without the stimulation by stem cell factor (SCF), a ligand for KIT. The spontaneously dimerized FMA3-type KIT without SCF binding was not internalized even after the activation. IC-2 cells expressing the FMA3- type KIT grew in suspension culture without IL-3 and SCF and became leukemic in nude athymic mice. The deletion of seven amino acids at the juxtamembrane domain appeared to be a new activating mutation of KIT that might be involved in neoplastic growth of mast cells.


1995 ◽  
Vol 309 (3) ◽  
pp. 921-926 ◽  
Author(s):  
Y Murakumo ◽  
H Ide ◽  
H Itoh ◽  
M Tomita ◽  
T Kobayashi ◽  
...  

By using the combination of reverse-transcription PCR and rapid amplification of cDNA ends methods, a cDNA encoding mast cell tryptase was successfully cloned from the small intestine of Mongolian gerbil, Meriones unguiculatus, infected with Nippostrongylus brasiliensis. The cDNA was 1219 bp long including 810 bp of an open reading frame. Based on the deduced amino acid sequences of known mast cell tryptases of other species, the gerbil mast cell tryptase (gMCT) was highly similar to mouse mast cell protease (mMCP)-7, and seems to be translated as a prepro-enzyme with 25 amino acids of signal and activation peptides and 245 amino acids of mature enzyme. The gMCT mRNA was preferentially transcribed in the intestinal mucosa and to a far lesser extent in the connective tissue such as skin and tongue. Moreover, kinetic study after infection revealed that the amount of gMCT mRNA in the small intestine correlated well with the degree of intestinal mastocytosis. Throughout the course of infection, enzyme-histochemically detectable tryptase activity was limited to mucosal mast cells. Since mucosal mast cells of other rodents, including mice and rats, do not express tryptases, this is the first report of rodent mast cell tryptase expressed in the intestinal mucosa.


2003 ◽  
Vol 74 (6) ◽  
pp. 1026-1034 ◽  
Author(s):  
Kouichi Takeuchi ◽  
Kenichi Koike ◽  
Takehiko Kamijo ◽  
Shuichi Ishida ◽  
Yozo Nakazawa ◽  
...  

1971 ◽  
Vol 69 (1) ◽  
pp. 57-64 ◽  
Author(s):  
J. Laissue ◽  
W. Marx ◽  
A. Grieder ◽  
R. Schindler
Keyword(s):  

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