PMID- 18284540
OWN - NLM
STAT- MEDLINE
DCOM- 20080811
LR  - 20231213
IS  - 1600-0714 (Electronic)
IS  - 0904-2512 (Linking)
VI  - 37
IP  - 6
DP  - 2008 Jul
TI  - Human laminin-332 degradation by Candida proteinases.
PG  - 329-35
LID - 10.1111/j.1600-0714.2008.00638.x [doi]
AB  - BACKGROUND: Human laminin-332 (Lm-332) degradation by 12 Candida strains and 
      effects of synthetic proteinase inhibitors [Ilomastat (ILM), EDTA, chemically 
      modified tetracycline-3(CMT-3), CMT-308, synthetic peptide CTT-2, and Pefabloc] 
      were studied. MATERIALS AND METHODS: Laminin-332 was incubated with sonicated 
      cell fractions and 10 times concentrated cell-free fractions of reference and 
      clinical strains of C. albicans, C. dubliniensis, C. guilliermondii, C. glabrata, 
      C. krusei, and C. tropicalis. Proteolysis, pH effects, and inhibitors were 
      analyzed by fluorography and zymography. RESULTS: Cell fractions of all species 
      except C. guilliermondii and cell-free fractions of C. albicans, and C. 
      dubliniensis showed 20-70 kDa gelatinases at pH 5.0 and 6.0. At pH 7.6, C. 
      glabrata, C. krusei, and C. tropicalis cell fractions and C. tropicalis cell-free 
      fractions showed 55-70 kDa gelatinases. CMT-3, CMT-308, and CTT-2 inhibited 
      Candida gelatinases slightly better than Pefabloc, ILM, and EDTA. No Candida 
      fractions degraded Lm-332 at pH 7.6, but at pH 5.0, 100 kDa bands were generated 
      by cell fractions of C. dubliniensis and C. tropicalis; C. albicans and C. 
      glabrata clinical strains; and C. guilliermondii reference strain. C. krusei 
      reference strain yielded three 100-130 kDa bands. C. albicans, C. dubliniensis, 
      and C. tropicalis reference and clinical strain's cell-free fractions generated 
      100 kDa band. CONCLUSIONS: Laminin-332 degradation is pH-dependent and 
      differences exist between studied Candida strains. Lm-332 degradation can exert 
      functional disturbances on basement membrane integrity, possibly aiding Candida 
      cell invasion into tissues. Certain synthetic matrix metalloproteinase inhibitors 
      (CMTs, CTT) can inhibit Candida proteinases and may be therapeutically useful in 
      future.
FAU - Parnanen, P
AU  - Parnanen P
AD  - University of Helsinki, Institute of Dentistry, Helsinki, Finland. 
      pirjo.parnanen@helsinki.fi
FAU - Kari, K
AU  - Kari K
FAU - Virtanen, I
AU  - Virtanen I
FAU - Sorsa, T
AU  - Sorsa T
FAU - Meurman, J H
AU  - Meurman JH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080215
PL  - Denmark
TA  - J Oral Pathol Med
JT  - Journal of oral pathology & medicine : official publication of the International 
      Association of Oral Pathologists and the American Academy of Oral Pathology
JID - 8911934
RN  - 0 (CMT-308)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Fungal Proteins)
RN  - 0 (GRENYHGCTTHWGFTLC peptide)
RN  - 0 (Hydroxamic Acids)
RN  - 0 (Indoles)
RN  - 0 (Peptides, Cyclic)
RN  - 0 (Protease Inhibitors)
RN  - 0 (Sulfones)
RN  - 0 (Tetracyclines)
RN  - 0 (tetracycline CMT-3)
RN  - 34284-75-8 (4-(2-aminoethyl)benzenesulfonylfluoride)
RN  - 9G34HU7RV0 (Edetic Acid)
RN  - EC 3.4.24.- (Gelatinases)
RN  - I0403ML141 (ilomastat)
SB  - IM
MH  - Basement Membrane/microbiology
MH  - Candida/*enzymology
MH  - Cell Adhesion Molecules/antagonists & inhibitors/*metabolism
MH  - Cell Line
MH  - Edetic Acid/pharmacology
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Fungal Proteins/metabolism
MH  - Gelatinases/metabolism
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Hydroxamic Acids
MH  - Indoles/pharmacology
MH  - Keratinocytes/microbiology
MH  - Peptides, Cyclic/pharmacology
MH  - Protease Inhibitors/*pharmacology
MH  - Sulfones/pharmacology
MH  - Tetracyclines/pharmacokinetics
MH  - Kalinin
EDAT- 2008/02/21 09:00
MHDA- 2008/08/12 09:00
CRDT- 2008/02/21 09:00
PHST- 2008/02/21 09:00 [pubmed]
PHST- 2008/08/12 09:00 [medline]
PHST- 2008/02/21 09:00 [entrez]
AID - JOP638 [pii]
AID - 10.1111/j.1600-0714.2008.00638.x [doi]
PST - ppublish
SO  - J Oral Pathol Med. 2008 Jul;37(6):329-35. doi: 10.1111/j.1600-0714.2008.00638.x. 
      Epub 2008 Feb 15.