PMID- 23131589
OWN - NLM
STAT- MEDLINE
DCOM- 20130829
LR  - 20161125
IS  - 1638-6183 (Electronic)
IS  - 0300-9084 (Linking)
VI  - 95
IP  - 4
DP  - 2013 Apr
TI  - Expression and distribution of aggrecanases in human larynx: 
      ADAMTS-5/aggrecanase-2 is the main aggrecanase in laryngeal carcinoma.
PG  - 725-34
LID - S0300-9084(12)00438-5 [pii]
LID - 10.1016/j.biochi.2012.10.022 [doi]
AB  - Members of the ADAMTS family of proteases degrade proteoglycans and thereby have 
      the potential to alter tissue architecture and regulate cellular functions. 
      Aggrecanases are the main enzymes responsible for aggrecan degradation, due to 
      their specific cleavage pattern. In this study, the expression status, the 
      macromolecular organization and localization of ADAMTS-1, ADAMTS-4/aggrecanase-1 
      and ADAMTS-5/aggrecanase-2 in human normal larynx and laryngeal squamous cell 
      carcinoma (LSCC) were investigated. On mRNA level, the results showed that 
      ADAMTS-4 was the highest expressed enzyme in normal larynx, whereas ADAMTS-5 was 
      the main aggrecanase in LSCC presenting a stage-related increase up to stage III 
      (8-fold higher expression compared to normal), and thereafter decreased in stage 
      IV. Accordingly, immunohistochemical analysis showed that ADAMTS-5, but not 
      ADAMTS-4, was highly expressed by carcinoma cells. Sequential extraction revealed 
      an altered distribution and organization of multiple molecular forms (latent, 
      activated and fragmented forms) of the enzymes within the cancerous and their 
      corresponding macroscopically normal laryngeal tissues, compared to the normal 
      ones. Importantly, these analyses indicated that critical macromolecular changes 
      occurred from the earliest LSCC stages not only in malignant parts of the tissue 
      but also in areas that were not in proximity to carcinoma cells and appeared 
      otherwise normal. Overall, the results of the present study show that 
      ADAMTS-5/aggrecanase-2 is the main aggrecanase present in laryngeal carcinoma 
      suggesting a critical role for the enzyme in aggrecan degradation and laryngeal 
      tissue destruction during tumor progression.
CI  - Copyright (c) 2012 Elsevier Masson SAS. All rights reserved.
FAU - Filou, S
AU  - Filou S
AD  - Laboratory of Biochemistry, Department of Chemistry, University of Patras, 26500 
      Patras, Greece.
FAU - Stylianou, M
AU  - Stylianou M
FAU - Triantaphyllidou, I E
AU  - Triantaphyllidou IE
FAU - Papadas, T
AU  - Papadas T
FAU - Mastronikolis, N S
AU  - Mastronikolis NS
FAU - Goumas, P D
AU  - Goumas PD
FAU - Papachristou, D J
AU  - Papachristou DJ
FAU - Ravazoula, P
AU  - Ravazoula P
FAU - Skandalis, S S
AU  - Skandalis SS
FAU - Vynios, D H
AU  - Vynios DH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20121103
PL  - France
TA  - Biochimie
JT  - Biochimie
JID - 1264604
RN  - 0 (RNA, Messenger)
RN  - EC 3.4.24.- (ADAM Proteins)
RN  - EC 3.4.24.- (ADAMTS1 Protein)
RN  - EC 3.4.24.- (ADAMTS1 protein, human)
RN  - EC 3.4.24.- (ADAMTS5 Protein)
RN  - EC 3.4.24.- (ADAMTS5 protein, human)
RN  - EC 3.4.24.14 (Procollagen N-Endopeptidase)
RN  - EC 3.4.24.82 (ADAMTS4 Protein)
RN  - EC 3.4.24.82 (ADAMTS4 protein, human)
SB  - IM
MH  - ADAM Proteins/*genetics/*metabolism
MH  - ADAMTS1 Protein
MH  - ADAMTS4 Protein
MH  - ADAMTS5 Protein
MH  - Aged
MH  - Carcinoma, Squamous Cell/enzymology/genetics/metabolism
MH  - Female
MH  - *Gene Expression Regulation, Neoplastic
MH  - Humans
MH  - Laryngeal Neoplasms/*enzymology/*genetics/metabolism
MH  - Larynx/enzymology/*metabolism
MH  - Male
MH  - Procollagen N-Endopeptidase/genetics/metabolism
MH  - Protein Transport
MH  - RNA, Messenger/genetics/metabolism
EDAT- 2012/11/08 06:00
MHDA- 2013/08/30 06:00
CRDT- 2012/11/08 06:00
PHST- 2012/06/05 00:00 [received]
PHST- 2012/10/27 00:00 [accepted]
PHST- 2012/11/08 06:00 [entrez]
PHST- 2012/11/08 06:00 [pubmed]
PHST- 2013/08/30 06:00 [medline]
AID - S0300-9084(12)00438-5 [pii]
AID - 10.1016/j.biochi.2012.10.022 [doi]
PST - ppublish
SO  - Biochimie. 2013 Apr;95(4):725-34. doi: 10.1016/j.biochi.2012.10.022. Epub 2012 
      Nov 3.