PMID- 1334144
OWN - NLM
STAT- MEDLINE
DCOM- 19930111
LR  - 20190902
IS  - 0022-3484 (Print)
IS  - 0022-3484 (Linking)
VI  - 27
IP  - 6
DP  - 1992 Nov
TI  - Correlation between tumor necrosis factor-alpha (TNF-alpha)-induced cytoskeletal 
      changes and human collagenase gene induction.
PG  - 562-8
AB  - Tumor necrosis factor-alpha (TNF-alpha) has been shown not only to induce the 
      biosynthesis and secretion of collagenase but also to change the organization of 
      cytoskeletal components. In the present study we explore the correlation between 
      the biosynthesis of collagenase (by mRNA hybridization, indirect 
      immunofluorescence and collagenolytic activity), and cytoskeletal reorganization 
      (by rhodamine-phalloidin staining of F-actin) induced in fibroblasts by 
      recombinant TNF (rTNF). In the concentration range of 1-100 ng/ml, rTNF increased 
      extracellular collagenase activity 8-fold and collagenase mRNA 4-fold. In 
      addition, whereas the collagenase mRNA was detected as early as 24 h 
      posttreatment, the appearance of extracellular collagenase activity required 48 
      h. Using phalloidin to follow the organization of the cytoskeleton we observed 
      that rTNF disrupted the parallel array of stress fibers normally observed in the 
      perinuclear region. In contrast to the time required to affect collagenase 
      synthesis, the effect of rTNF on stress fiber organization occurred as early as 6 
      h post-treatment. Finally, while the number of cells exhibiting this change 
      increased with increasing concentrations of rTNF, a maximum of about 30% of the 
      cells showed this effect. Interestingly, double staining studies demonstrated 
      that both stress fiber changes and procollagenase production occurred in the same 
      cells. This finding, together with the observation that the cytoskeletal 
      disorganization preceded collagenase gene induction by at least 18 h is 
      consistent with the conclusion that the organizational status of the 
      microfilaments may have a role as a regulator of procollagenase gene expression.
FAU - Gronowicz, G
AU  - Gronowicz G
AD  - Department of Orthopedic Surgery, University of Connecticut School of Dental 
      Medicine, Farmington.
FAU - Hadjimichael, J
AU  - Hadjimichael J
FAU - Richards, D
AU  - Richards D
FAU - Cerami, A
AU  - Cerami A
FAU - Rossomando, E F
AU  - Rossomando EF
LA  - eng
GR  - AR38636/AR/NIAMS NIH HHS/United States
GR  - DE00157/DE/NIDCR NIH HHS/United States
GR  - DE08440/DE/NIDCR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Periodontal Res
JT  - Journal of periodontal research
JID - 0055107
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Enzyme Precursors)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - EC 3.4.24.- (Collagenases)
RN  - EC 3.4.24.- (procollagenase)
RN  - EC 3.4.24.3 (Microbial Collagenase)
SB  - IM
MH  - Actin Cytoskeleton/*drug effects/physiology
MH  - Collagenases/biosynthesis/*genetics
MH  - Cytoskeletal Proteins/biosynthesis/*drug effects/metabolism
MH  - Enzyme Induction/*drug effects
MH  - Enzyme Precursors/biosynthesis
MH  - Fibroblasts/cytology/drug effects/enzymology
MH  - Fluorescent Antibody Technique
MH  - Gingiva/cytology/drug effects/enzymology
MH  - Humans
MH  - Immunoblotting
MH  - Microbial Collagenase/biosynthesis
MH  - RNA, Messenger/analysis
MH  - Recombinant Proteins/pharmacology
MH  - Time Factors
MH  - Tumor Necrosis Factor-alpha/*pharmacology
EDAT- 1992/11/01 00:00
MHDA- 1992/11/01 00:01
CRDT- 1992/11/01 00:00
PHST- 1992/11/01 00:00 [pubmed]
PHST- 1992/11/01 00:01 [medline]
PHST- 1992/11/01 00:00 [entrez]
AID - 10.1111/j.1600-0765.1992.tb01737.x [doi]
PST - ppublish
SO  - J Periodontal Res. 1992 Nov;27(6):562-8. doi: 10.1111/j.1600-0765.1992.tb01737.x.