PMID- 10727211
OWN - NLM
STAT- MEDLINE
DCOM- 20000504
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 39
IP  - 12
DP  - 2000 Mar 28
TI  - Molecular cloning and functional analysis of apoxin I, a snake venom-derived 
      apoptosis-inducing factor with L-amino acid oxidase activity.
PG  - 3197-205
AB  - We previously purified apoxin I, an apoptosis-inducing factor with L-amino acid 
      oxidase (LAO) activity, from Western diamondback rattlesnake venom. To determine 
      the primary structure of apoxin I, we cloned its cDNA. The amino acid sequence 
      showed that apoxin I has an FAD binding domain and shares homology with L-amino 
      acid oxidase (LAO) from Neurospora crassa, human monoamine oxidase B, and mouse 
      interleukin 4-induced F1G1 protein. The full-length apoxin I has an N-terminal 
      signal sequence that is processed in mature apoxin I in venom. When the apoxin I 
      gene was transfected into human 293T cells, the recombinant protein was expressed 
      in the cells, and a significant amount of apoxin I was secreted into the medium. 
      The secreted recombinant apoxin I protein showed LAO and apoptosis-inducing 
      activity, but the recombinant protein in the cells did not, suggesting that 
      maturation and secretion of the apoxin I protein is needed for its activity. 
      Treating the transfected cells with tunicamycin inhibited the secretion and LAO 
      activity of the recombinant apoxin I. In addition, deleting the amino-terminal 
      region flanking the signal sequence, the FAD-binding domain and the 
      carboxy-terminal region abolished the secretion and LAO activity of the 
      recombinant proteins. These results indicate that in order for apoxin I to become 
      active, these regions and posttranslational modification, such as 
      N-glycosylation, are required.
FAU - Torii, S
AU  - Torii S
AD  - Institute of Molecular and Cellular Biosciences, The University of Tokyo, Yayoi, 
      Bunkyo-ku, Tokyo 113-0032, Japan.
FAU - Yamane, K
AU  - Yamane K
FAU - Mashima, T
AU  - Mashima T
FAU - Haga, N
AU  - Haga N
FAU - Yamamoto, K
AU  - Yamamoto K
FAU - Fox, J W
AU  - Fox JW
FAU - Naito, M
AU  - Naito M
FAU - Tsuruo, T
AU  - Tsuruo T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Crotalid Venoms)
RN  - 0 (DNA, Complementary)
RN  - 0 (Recombinant Proteins)
RN  - EC 1.4.- (Amino Acid Oxidoreductases)
RN  - EC 1.4.3.2 (L-Amino Acid Oxidase)
SB  - IM
MH  - Amino Acid Oxidoreductases/*genetics/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Apoptosis/drug effects
MH  - Cell Line
MH  - Cloning, Molecular
MH  - Crotalid Venoms/enzymology/*genetics/*metabolism
MH  - DNA, Complementary/biosynthesis/isolation & purification
MH  - Fluorescent Antibody Technique, Direct
MH  - Glycosylation
MH  - HL-60 Cells
MH  - Humans
MH  - L-Amino Acid Oxidase
MH  - Molecular Sequence Data
MH  - Recombinant Proteins/antagonists & inhibitors/metabolism/pharmacology
MH  - Sequence Deletion
EDAT- 2000/03/22 09:00
MHDA- 2000/05/08 09:00
CRDT- 2000/03/22 09:00
PHST- 2000/03/22 09:00 [pubmed]
PHST- 2000/05/08 09:00 [medline]
PHST- 2000/03/22 09:00 [entrez]
AID - bi992416z [pii]
AID - 10.1021/bi992416z [doi]
PST - ppublish
SO  - Biochemistry. 2000 Mar 28;39(12):3197-205. doi: 10.1021/bi992416z.