Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0023418 (
leukemia
)
93,477
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Mice--BDF, hybrides, males aged 3 months were injected intraperitoneally with 10(4) lymphatic leukemia cells P 388. The mice were killed by bleeding after 2.5 and 10 days after the injection. Gamma-glutamyltransferase (GGT), leucylaminopeptidase (LAP) and cobalt activated
acylase
activity were determined in the serum of the mice. The inner organs of the animals were verified histopathologically. A statistically significant increase in the activity of the examined enzymes was observed together with the development of transplantable
leukemia
. These enzymes can be helpful in early monitoring of lymphatic leukemia P 388 in mice--as markers of cancer growth.
...
PMID:Activity of some hydrolases in mice with transplantable lymphatic leukemia P 388. 288 60
The activity of cobalt-activated
acylase
was determined in the serum of mice with transplantable
leukemia
(P 388, L 1210 standard, L 1210/ara-C, L 1210/CH3-G, plasmocytoma ADJPC-5, lymphoma AKSL-4 and natural
leukemia
in mice NZB). A statistically significant increase in enzyme activity in all leukemias except lymphatic leukemia has been demonstrated. The results suggest possibility of using the enzymatic measurement as a marker of transplantable
leukemia
in mice.
...
PMID:Serum cobalt-activated acylase as a marker of transplantable leukemia in mice. 327 96
AKR mice highly susceptible to
leukemia
were fed orally for 9 months every days with a water solution of peat-liking preparation PF-290/II/2 at a dose 0.2 cm3 (70 g/cm3 water). After bleeding body and internal organs weight were measured and their ratio were calculated. Anatomo-pathological lesions, histopathological and ultrastructural examinations with the use of transmission and scanning microscope, serum cobalt-activated
acylase
(AA-Co) activity and urine arylsulphatase (ASA) activity were performed. It was found used preparation had some anti-tumors effect of mice with lymphatic leukemia. Serum cobalt-activated
acylase
and urine arylsulphatase of AKR mice for observation on disease development and dynamics of this process. In the ultrastructural picture changes of lymphatic cells after outside removal of degradated complexes of intracell membranes was observed.
...
PMID:[Morphological and biochemical studies of the effect of the peat-derived preparation PF-290/II/2 on the development of natural lymphatic leukemia in mice]. 348 32
SIRT2 is a member of the human sirtuin family of proteins and possesses NAD
+
-dependent lysine deacetylase/deacylase activity. SIRT2 has been implicated in carcinogenesis in various cancers including
leukaemia
and is considered an attractive target for cancer therapy. Here, we identified NPD11033, a selective small-molecule SIRT2 inhibitor, by a high-throughput screen using the RIKEN NPDepo chemical library. NPD11033 was largely inactive against other sirtuins and zinc-dependent deacetylases. Crystallographic analysis revealed a unique mode of action, in which NPD11033 creates a hydrophobic cavity behind the substrate-binding pocket after a conformational change of the Zn-binding small domain of SIRT2. Furthermore, it forms a hydrogen bond to the active site histidine residue. In addition, NPD11033 inhibited cell growth of human pancreatic cancer PANC-1 cells with a concomitant increase in the acetylation of eukaryotic translation initiation factor 5A, a physiological substrate of SIRT2. Importantly, NPD11033 failed to inhibit defatty-
acylase
activity of SIRT2, despite its potent inhibitory effect on its deacetylase activity. Thus, NPD11033 will serve as a useful tool for both developing novel anti-cancer agents and elucidating the role of SIRT2 in various cellular biological processes.This article is part of a discussion meeting issue 'Frontiers in epigenetic chemical biology'.
...
PMID:Identification of a novel small molecule that inhibits deacetylase but not defatty-acylase reaction catalysed by SIRT2. 2968 74