Occurrence and distribution of matrix metalloproteinase-2-immunoreactivity in human embryonic tissues.
Tissue development and structure is controlled by dynamic and interactive relationships between cells and the extra-cellular matrix (ECM) which they secrete. We have investigated the occurrence and distribution of metalloproteinase-2 (MMP-2), an enzyme involved in the catabolism of ECM components, in human embryonic tissues by immunocytochemistry. Cells displaying MMP-2 immunoreactivity showed a widespread distribution in human embryonic tissues and organs. Cytoplasmic staining was detected in cells deriving from all three embryonic layers. Although further studies are needed to clarify the possible substrates of MMP-2 in developing tissues, these morphological data lend support to the hypothesis that ECM remodelling and degradation may represent a physiological counterpart of ECM deposition that occur during development.
Casasco
A
A
Institute of Histology and Embryology, University of Pavia, Italy.
Casasco
M
M
Reguzzoni
M
M
Calligaro
A
A
Tateo
S
S
Stetler-Stevenson
W G
WG
Liotta
L A
LA
D004848:Epithelium / Q000201:enzymology; D005109:Extracellular Matrix / Q000201:enzymology*; D005260:Female; D005333:Fetus / Q000201:enzymology* / Q000276:immunology; D018093:Gelatinases / Q000378:metabolism*; D006801:Humans; D007124:Immunoenzyme Techniques; D007150:Immunohistochemistry; D020778:Matrix Metalloproteinase 2; D008666:Metalloendopeptidases / Q000378:metabolism*; D009132:Muscles / Q000196:embryology / Q000201:enzymology; D009474:Neurons / Q000201:enzymology; D010006:Osteoblasts / Q000201:enzymology; D011247:Pregnancy
D018093:Gelatinases; D008666:Metalloendopeptidases; D020778:Matrix Metalloproteinase 2