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: EC:3.1.30.2 (
endonuclease
)
18,621
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The cluster of differentiation 44 (CD44), hereafter referred to as H-
CAM
(CD44), represents a novel class of polymorphic (Mr 80,000-215,000) cell adhesion molecules that are involved in cell-cell and cell-matrix adhesion events in a variety of organ systems. We report the detection of distinct mRNAs, in both hematopoietic and nonhematopoietic human cell lines, that encode H-
CAM
(CD44) with different cytoplasmic domains. Genomic Southern blot analyses indicate that the exons encoding these two cytoplasmic domains are located on the same approximately 16 kilobase (kb) Eco RI restriction fragment. Restriction
endonuclease
and Southern blot analyses performed on polymerase chain reaction (PCR) amplification copies of these mRNAs confirm that their sequences correspond with previously reported cDNA sequences. A consensus splice donor site which is conserved in human, baboon, and mouse mRNAs that encode a molecule with an elongated cytoplasmic domain (H-
CAM
-L) is utilized to generate a distinct but low-abundance mRNA species that encodes H-
CAM
(CD44) with a truncated cytoplasmic domain of only three amino acids (H-
CAM
-S). Estimations of the relative abundance of these mRNA species in B-lymphoblastoid cells using the PCR amplification technique exhibit average H-
CAM
-L/H-
CAM
-S ratios ranging between 100 and 200. Therefore, H-
CAM
(CD44)-mediated adhesive events may be regulated through a differential capacity of H-
CAM
-L and H-
CAM
-S to interact with the cytoskeleton and to participate in intracellular signaling events.
...
PMID:Identification of mRNA that encodes an alternative form of H-CAM(CD44) in lymphoid and nonlymphoid tissues. 227 59
Cell death plays an essential role in cell homeostasis and the pathological process in cancer. Apoptosis has been identified by the internucleosomal DNA cleavage which appears to be associated with
endonuclease
activation. Proteolysis is considered to be an early event in apoptosis. We studied the effects of proteolysis on early apoptotic events, such as chromatin condensation, nuclear breakdown, DNA breakage and sensitivity to denaturation induced by anticancer drugs (camptothecin:
CAM
, 5-azacytidine: AZA) on HL-60 cells.
CAM
induced apoptosis on S phase and AZA on G1 phase. The internucleosomal DNA cleavage shown by both the presence of DNA fragments during gel electrophoresis and a large number of in situ DNA strands breaks (revealed in high intensity fluorescence FITC of cells in the TdT reaction) was prevented by the protease inhibitor, TPCK (N-tosyl-L-phenylalanine chlorometyl-ketone), as well as by an inhibitor of the apoptosis-associated
endonuclease
, ZnSO4. The protective effects were observed under conditions in which apoptosis was induced by agents with a different mechanism of action, such as the DNA damaging drug.
CAM
(topo-isomerase inhibitor), and an RNA antimetabolite, AZA. The protease inhibitor inhibits early events of apoptosis such as chromatin condensation, nuclear breakdown, DNA breakage and sensitivity to denaturation, which have different structures and a different mechanism of interaction with drugs. The results suggest that control of protease inhibitor may be a useful strategy to treat cancers.
...
PMID:[Analysis of drug-induced apoptosis in human leukemic cell line (HL-60)]. 958 41