PMID- 15820774
OWN - NLM
STAT- MEDLINE
DCOM- 20050801
LR  - 20061115
IS  - 0009-9120 (Print)
IS  - 0009-9120 (Linking)
VI  - 38
IP  - 5
DP  - 2005 May
TI  - Evidence for the association of synaptotagmin with glutathione S-transferases: 
      implications for a novel function in human breast cancer.
PG  - 436-43
AB  - OBJECTIVE: To analyze the pattern of changes in GSTs in cancerous and adjacent 
      non-cancerous tissues obtained from breast cancer patients undergoing surgery. 
      DESIGN AND METHODS: Cytosolic GST purification, assay of GST, protein expression 
      levels, and GST-synaptotagmin association were analyzed using standard 
      biochemical techniques like GSH-affinity purification, spectrophotometry, 
      SDS-PAGE, Western blots, and matrix-assisted laser desorption and ionization-time 
      of flight (MALDI-TOF). RESULTS: GST activity in cancerous tissues (0.26 U/mg 
      protein) was significantly higher (P < 0.05) as compared to those from adjacent 
      non-cancerous tissues (0.14 U/mg protein) of breast cancer patients. Further 
      analysis of GST subunits on SDS-PAGE and Western blots using class-specific GST 
      antibodies revealed significant elevation in GST-pi levels in cancer tissues with 
      no appreciable changes in GST-alpha and GST-mu. Along with the elevation of 
      GST-pi levels, high molecular weight proteins (approximately 70 kDa) cross 
      reacting with GST antibodies were detected only in surgically resected tumor 
      biopsies but not in the non-cancerous tissues adjacent to the tumor. Based on 
      MALDI-TOF analysis, the high molecular weight band was identified as 
      synaptotagmin V bound to GST-M1 with 47% sequence coverage after processing on an 
      MS-FIT search engine. CONCLUSIONS: Our results suggest a novel putative 
      functional role for the GST-synaptotagmin complex in human breast cancers. As 
      this association of GST M1-synaptotagmin was not seen in adjacent non-cancerous 
      tissues, this can be used as a marker for breast cancers.
FAU - Sreenath, A S
AU  - Sreenath AS
AD  - Department of Animal Sciences, School of Life Sciences, University of Hyderabad, 
      Hyderabad 500046, India.
FAU - Kumar, K Ravi
AU  - Kumar KR
FAU - Reddy, G V
AU  - Reddy GV
FAU - Sreedevi, B
AU  - Sreedevi B
FAU - Praveen, D
AU  - Praveen D
FAU - Monika, S
AU  - Monika S
FAU - Sudha, S
AU  - Sudha S
FAU - Reddy, M Gopal
AU  - Reddy MG
FAU - Reddanna, P
AU  - Reddanna P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Clin Biochem
JT  - Clinical biochemistry
JID - 0133660
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (SYT5 protein, human)
RN  - 134193-27-4 (Synaptotagmins)
RN  - EC 2.5.1.18 (Glutathione Transferase)
SB  - IM
MH  - Adult
MH  - Blotting, Western
MH  - Breast/enzymology
MH  - Breast Neoplasms/enzymology/*physiopathology
MH  - Calcium-Binding Proteins/*metabolism
MH  - Carcinoma, Ductal, Breast/enzymology/physiopathology
MH  - Chromatography, Affinity
MH  - Female
MH  - Glutathione Transferase/*metabolism
MH  - Humans
MH  - Membrane Glycoproteins/*metabolism
MH  - Middle Aged
MH  - Nerve Tissue Proteins/*metabolism
MH  - Synaptotagmins
EDAT- 2005/04/12 09:00
MHDA- 2005/08/02 09:00
CRDT- 2005/04/12 09:00
PHST- 2004/09/07 00:00 [received]
PHST- 2005/01/04 00:00 [revised]
PHST- 2005/01/17 00:00 [accepted]
PHST- 2005/04/12 09:00 [pubmed]
PHST- 2005/08/02 09:00 [medline]
PHST- 2005/04/12 09:00 [entrez]
AID - S0009-9120(05)00019-6 [pii]
AID - 10.1016/j.clinbiochem.2005.01.009 [doi]
PST - ppublish
SO  - Clin Biochem. 2005 May;38(5):436-43. doi: 10.1016/j.clinbiochem.2005.01.009.