PMID- 11097207
OWN - NLM
STAT- MEDLINE
DCOM- 20010301
LR  - 20191104
IS  - 1044-6672 (Print)
IS  - 1026-7905 (Linking)
VI  - 7
IP  - 2-4
DP  - 2000
TI  - In vitro and in vivo expression of interstitial collagenase/MMP-1 by human mast 
      cells.
PG  - 131-42
AB  - Degradation of the extracellular matrix occurs under physiological and 
      pathological conditions, thought to be principally mediated by a family of 
      neutral proteolytic enzymes termed the matrix metalloproteinases (MMPs). The 
      present study was initiated to determine whether mast cells have the ability to 
      produce these proteases in diseased and normal human tissue. Immunohistochemistry 
      and in situ hybridization was performed to localize interstitial collagenase 
      protein and mRNA transcripts in diseased human tissue. The human mast cell line 
      HMC-1 was cultured under serum free conditions, stimulated with phorbol mystrate 
      acetate (PMA) and supernatants analyzed by Western blotting and zymography to 
      determine the profile of secreted MMPs. The dog mast cell line BR, known to 
      secrete gelatinolytic enzymes, was used in parallel studies. Total RNA was 
      extracted and analyzed by RT-PCR for the expression of tissue inhibitors of MMP 
      (TIMPs). Collagenase-1 protein and mRNA were expressed by tryptase and chymase 
      positive human mast cells in all tissue analyzed. This proteinase was also 
      detected in the cytoplasm and conditioned media of HMC-1 cells. PMA induced 
      gelatinolytic activity in both mast cell lines examined. TIMP-1 immunoreactivity 
      was detected and TIMP-1, and -2 (but not TIMP-3) mRNA transcripts were amplified 
      from HMC-1 cells. This is the first demonstration of the expression of 
      collagenase-1 by human mast cells in both inflamed and normal tissues, and by a 
      human mast cell line. MMPs secreted by these cells could contribute to the 
      extensive matrix lysis characteristic of diseases such as rheumatoid arthritis 
      and inflammatory ocular disorders. Alternatively collagenase-1 production by mast 
      cells may play a critical role in cell invasion and migration into sites of 
      inflammation.
FAU - Di Girolamo, N
AU  - Di Girolamo N
AD  - Inflammation Research Unit, School of Pathology, The University of New South 
      Wales, Sydney, Australia. N.Digirolamo@unsw.edu.au
FAU - Wakefield, D
AU  - Wakefield D
LA  - eng
PT  - Journal Article
PL  - England
TA  - Dev Immunol
JT  - Developmental immunology
JID - 9200624
RN  - 0 (RNA, Messenger)
RN  - 0 (Tissue Inhibitor of Metalloproteinase-1)
RN  - 0 (Tissue Inhibitor of Metalloproteinase-3)
RN  - 127497-59-0 (Tissue Inhibitor of Metalloproteinase-2)
RN  - EC 3.4.24.- (Collagenases)
RN  - EC 3.4.24.- (collagenase 1)
RN  - NI40JAQ945 (Tetradecanoylphorbol Acetate)
SB  - IM
MH  - Cell Communication
MH  - Cells, Cultured
MH  - Collagenases/*biosynthesis/genetics
MH  - Humans
MH  - Mast Cells/*enzymology
MH  - RNA, Messenger/analysis
MH  - Tetradecanoylphorbol Acetate/pharmacology
MH  - Tissue Inhibitor of Metalloproteinase-1/genetics
MH  - Tissue Inhibitor of Metalloproteinase-2/genetics
MH  - Tissue Inhibitor of Metalloproteinase-3/genetics
PMC - PMC2276052
EDAT- 2000/11/30 11:00
MHDA- 2001/03/07 10:01
PMCR- 2000/01/01
CRDT- 2000/11/30 11:00
PHST- 2000/11/30 11:00 [pubmed]
PHST- 2001/03/07 10:01 [medline]
PHST- 2000/11/30 11:00 [entrez]
PHST- 2000/01/01 00:00 [pmc-release]
AID - S1740252200827080 [pii]
AID - 10.1155/2000/82708 [doi]
PST - ppublish
SO  - Dev Immunol. 2000;7(2-4):131-42. doi: 10.1155/2000/82708.