PMID- 9124034
OWN - NLM
STAT- MEDLINE
DCOM- 19970424
LR  - 20211203
IS  - 0001-5180 (Print)
IS  - 0001-5180 (Linking)
VI  - 156
IP  - 3
DP  - 1996
TI  - Roles of kringle domain-containing serine proteases in epithelial-mesenchymal 
      transitions during embryonic development.
PG  - 162-72
AB  - Transformation of an epithelial sheet into a migrating mesenchymal cell 
      population implies the destruction of the basal lamina underlying the epithelium, 
      and the subsequent localized digestion of the extracellular matrix by the 
      migrating cells. Proteases are involved in these processes. Among them, molecules 
      containing both a serine protease domain and at least one kringle domain have 
      been identified as possible important effectors. Interestingly, related proteins 
      containing an inactive serine protease domain also seem to play a role, 
      suggesting that the function of these molecules in epithelial-mesenchymal 
      transformation is not confined to proteolytic digestion of cell attachments. 
      Instead, these molecules act through specific tyrosine kinase receptors in the 
      membrane of the responding cells. In this review, we summarize data implicating 
      this family of molecules in various epithelial-mesenchymal transitions during 
      embryonic development. Our major focus of attention are: hepatocyte growth 
      factor/scatter factor (HGF/SF), its tyrosine kinase receptor proto-oncogene 
      c-met, and the related peptide factor HGF-like/macrophage-stimulating protein 
      (HGF1/MSP), whose receptor is the Ron tyrosine kinase. c-met and Ron also have 
      another close homolog in the chick, called Sea, whose ligand remains unknown. 
      Interestingly, HGF/SF is activated by other plasminogen-related molecules which, 
      apart from a specific activator, include the protease urokinase. HGF/SF, c-met 
      and HGF/MSP are expressed in dynamic ways during early embryonic development, 
      correlating with regions undergoing epithelial/mesenchymal transformations. 
      Moreover, several assays are now starting to reveal great pleiotropism of 
      function during development, including both the loss and the acquisition of 
      epithelial morphology according to the cell type and assay used, as well as 
      angiogenesis, kidney tubule morphogenesis, cell motility, the maintenance of 
      competence for neural induction and some aspects of the later development of the 
      musculoskeletal and nervous systems.
FAU - Thery, C
AU  - Thery C
AD  - Department of Genetics and Development, College of Physicians and Surgeons of 
      Columbia University, New York, N.Y. 10032, USA.
FAU - Stern, C D
AU  - Stern CD
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - Switzerland
TA  - Acta Anat (Basel)
JT  - Acta anatomica
JID - 0370272
RN  - 0 (MAS1 protein, human)
RN  - 0 (Proto-Oncogene Mas)
RN  - 67256-21-7 (Hepatocyte Growth Factor)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
RN  - EC 3.4.21.- (Serine Endopeptidases)
SB  - IM
MH  - Animals
MH  - *Embryonic and Fetal Development/physiology
MH  - Epithelium/enzymology
MH  - Hepatocyte Growth Factor/physiology
MH  - Humans
MH  - Kringles/*physiology
MH  - Mesoderm/*enzymology
MH  - Proto-Oncogene Mas
MH  - Receptor Protein-Tyrosine Kinases/metabolism
MH  - Serine Endopeptidases/*physiology
RF  - 101
EDAT- 1996/01/01 00:00
MHDA- 1996/01/01 00:01
CRDT- 1996/01/01 00:00
PHST- 1996/01/01 00:00 [pubmed]
PHST- 1996/01/01 00:01 [medline]
PHST- 1996/01/01 00:00 [entrez]
AID - 10.1159/000147844 [doi]
PST - ppublish
SO  - Acta Anat (Basel). 1996;156(3):162-72. doi: 10.1159/000147844.