PMID- 1683874
OWN - NLM
STAT- MEDLINE
DCOM- 19920115
LR  - 20131121
IS  - 0021-9541 (Print)
IS  - 0021-9541 (Linking)
VI  - 149
IP  - 3
DP  - 1991 Dec
TI  - Localization of cellular transglutaminase on the extracellular matrix after 
      wounding: characteristics of the matrix bound enzyme.
PG  - 375-82
AB  - Extending our previous observation that tissue transglutaminase (TGase) binds to 
      extracellular matrix (ECM) fibronectin, we report here that endogenous tissue 
      TGase is localized on the adjacent ECM after puncture wounding embryonic human 
      lung fibroblasts (WI-38). The bound TGase persisted at the wound site for many 
      hours, demonstrated by immunofluorescence and by catalytic activity using an 
      overlay assay. The binding characteristics of TGase with ECM were studied further 
      by the addition of exogenous TGase to cell monolayers and monitoring by 
      immunofluorescence or overlay catalytic activity assays. Binding occurred equally 
      well at 4 degrees C or 37 degrees C. Prior incubation of exogenous TGase with 
      guanosine 5'-triphosphate (GTP), guanosine 5'-diphosphate (GDP), or adenosine 
      triphosphate (ATP) had little effect on the amount bound to matrix, but prior 
      treatment with calcium, magnesium, strontium, or manganese ions enhanced binding 
      2- to 3-fold. The Ca(++)-dependent change was a concentration-dependent effect on 
      soluble exogenous TGase, rather than an effect on ECM. Immunofluorescent 
      techniques showed that binding of exogenous TGase to ECM was prevented by prior 
      mixing with fibronectin or collagen, but not with several other ECM components, 
      including laminin, elastin, chondroitin sulfate, heparan sulfate, and hyaluronic 
      acid. ECM-bound TGase was released by 2 M potassium thiocyanate (KSCN) treatment 
      but was not released by treatment with a variety of amino acids, salts, reducing 
      agents, glycerol, or other chaotropic agents.
FAU - Upchurch, H F
AU  - Upchurch HF
AD  - Samuel Roberts Noble Foundation, Inc., Ardmore, Oklahoma 73402.
FAU - Conway, E
AU  - Conway E
FAU - Patterson, M K Jr
AU  - Patterson MK Jr
FAU - Maxwell, M D
AU  - Maxwell MD
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Cell Physiol
JT  - Journal of cellular physiology
JID - 0050222
RN  - 146-91-8 (Guanosine Diphosphate)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 2.3.2.13 (Transglutaminases)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Adenosine Triphosphate/pharmacology
MH  - Binding Sites
MH  - Calcium/pharmacology
MH  - Cell Line
MH  - Extracellular Matrix/enzymology/*physiology/ultrastructure
MH  - Guanosine Diphosphate/pharmacology
MH  - Guanosine Triphosphate/pharmacology
MH  - Humans
MH  - Kinetics
MH  - Protein Binding
MH  - Transglutaminases/*metabolism
MH  - Wounds and Injuries
EDAT- 1991/12/11 19:15
MHDA- 2001/03/28 10:01
CRDT- 1991/12/11 19:15
PHST- 1991/12/11 19:15 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1991/12/11 19:15 [entrez]
AID - 10.1002/jcp.1041490304 [doi]
PST - ppublish
SO  - J Cell Physiol. 1991 Dec;149(3):375-82. doi: 10.1002/jcp.1041490304.