Abstract
Connective tissue cells synthesize and secrete a group of matrix metalloproteinases (MMPs), all of which are capable of degrading the extracellular-matrix components. One of them, MMP-3 (stromelysin) has been shown to degrade purified basement-membrane components, collagen IV and laminin [Okada, Y., Nagase, H. & Harris, E.D., Jr. (1986) J. Biol. Chem. 261, 14245-14255]. Here we report that MMP-3 degrades collagen IV and laminin in intact basement membranes from bovine glomeruli (GBM) and bovine anterior-lens capsules (LBM). Degradation products were analysed by SDS/polyacrylamide-gel electrophoresis to determine the number and sizes of polypeptide fragments. Immunoblotting techniques were used to identify the origins of the fragments, i.e. collagen IV or laminin. The fragments of collagen IV were further mapped using specific antibodies that recognize the N-terminal (7 S) domain, the C-terminal (NC-1) domain, or the major triple-helical region between the terminal domains. Degradation of collagen IV was extensive; many fragments were found, from both GBM and LBM, in the M(r) range 25,000-380,000. A large fragment of laminin (M(r) > 380,000) was found in the GBM digests without reduction, but it dissociated into 220,000-M(r) chains upon reduction. The results suggest that MMP-3 plays an important role in the catabolism of basement membranes.
| Original language | English |
|---|---|
| Pages (from-to) | 413-419 |
| Number of pages | 7 |
| Journal | Biochemical Journal |
| Volume | 256 |
| Issue number | 2 |
| State | Published - Dec 1 1988 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Degradation of basement membranes by human matrix metalloproteinase 3 (stromelysin). / Bejarano, P. A.; Noelken, M. E.; Suzuki, K.; Hudson, B. G.; Nagase, H.
In: Biochemical Journal, Vol. 256, No. 2, 01.12.1988, p. 413-419.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Degradation of basement membranes by human matrix metalloproteinase 3 (stromelysin)
AU - Bejarano, P. A.
AU - Noelken, M. E.
AU - Suzuki, K.
AU - Hudson, B. G.
AU - Nagase, H.
PY - 1988/12/1
Y1 - 1988/12/1
N2 - Connective tissue cells synthesize and secrete a group of matrix metalloproteinases (MMPs), all of which are capable of degrading the extracellular-matrix components. One of them, MMP-3 (stromelysin) has been shown to degrade purified basement-membrane components, collagen IV and laminin [Okada, Y., Nagase, H. & Harris, E.D., Jr. (1986) J. Biol. Chem. 261, 14245-14255]. Here we report that MMP-3 degrades collagen IV and laminin in intact basement membranes from bovine glomeruli (GBM) and bovine anterior-lens capsules (LBM). Degradation products were analysed by SDS/polyacrylamide-gel electrophoresis to determine the number and sizes of polypeptide fragments. Immunoblotting techniques were used to identify the origins of the fragments, i.e. collagen IV or laminin. The fragments of collagen IV were further mapped using specific antibodies that recognize the N-terminal (7 S) domain, the C-terminal (NC-1) domain, or the major triple-helical region between the terminal domains. Degradation of collagen IV was extensive; many fragments were found, from both GBM and LBM, in the M(r) range 25,000-380,000. A large fragment of laminin (M(r) > 380,000) was found in the GBM digests without reduction, but it dissociated into 220,000-M(r) chains upon reduction. The results suggest that MMP-3 plays an important role in the catabolism of basement membranes.
AB - Connective tissue cells synthesize and secrete a group of matrix metalloproteinases (MMPs), all of which are capable of degrading the extracellular-matrix components. One of them, MMP-3 (stromelysin) has been shown to degrade purified basement-membrane components, collagen IV and laminin [Okada, Y., Nagase, H. & Harris, E.D., Jr. (1986) J. Biol. Chem. 261, 14245-14255]. Here we report that MMP-3 degrades collagen IV and laminin in intact basement membranes from bovine glomeruli (GBM) and bovine anterior-lens capsules (LBM). Degradation products were analysed by SDS/polyacrylamide-gel electrophoresis to determine the number and sizes of polypeptide fragments. Immunoblotting techniques were used to identify the origins of the fragments, i.e. collagen IV or laminin. The fragments of collagen IV were further mapped using specific antibodies that recognize the N-terminal (7 S) domain, the C-terminal (NC-1) domain, or the major triple-helical region between the terminal domains. Degradation of collagen IV was extensive; many fragments were found, from both GBM and LBM, in the M(r) range 25,000-380,000. A large fragment of laminin (M(r) > 380,000) was found in the GBM digests without reduction, but it dissociated into 220,000-M(r) chains upon reduction. The results suggest that MMP-3 plays an important role in the catabolism of basement membranes.
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M3 - Article
C2 - 3223920
AN - SCOPUS:0024270297
VL - 256
SP - 413
EP - 419
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 2
ER -