碩士 / 國立臺灣大學 / 動物學系 / 85 / Our laboratory purified a 23 kDa secreted metalloprotease
from carp headkidney, an organ consists of nervous, endocrine,
immune, and hematopoietic tissues. The cDNA encoding this
protease was isolated and it turned out to be a new member of
the astacin family of metalloproteases. This thesis presents the
biochemical action of nephrosin in the extracellular matrix of
headkidney.
Since the cells in hematopoietic tissues are active in migratory
events, in which remodeling of extracellular matrix ( ECM )
usually involves. First, It was examined if nephrosin degraded
the common components of ECM. Among the proteins tested,
including type IV collagen, fibronectin, and laminin, only
bovine fibronectin was degraded by nephrosin. Then carp
fibronectin was purified and it was also degraded by nephrosin,
raising the possibility that fibronectin is a natural substrate
of nephrosin. The mature form of nephrosin is composed
of a single proteolytic domain, different from other members of
the astacin family, which contain protein-interaction domains C-
terminal to their proteolytic domains. Since nephrosin is a
heparin binding protein, the hypothesis that nephrosin binds to
extracellular matrix via the glycosaminoglycan chain(s) of the
proteoglycan(s) was tested. It was found that buffers containing
chondroitin sulfate B, dextran sulfate, heparin, heparan
sulfate, de-N-sulfated heparin,and high concentrations of NaCl
all facilitated the extraction of nephrosin from headkidney ECM-
like materials. Therefore, all the results indicate that
secreted nephrosin is targetedto ECM by binding to
proteoglycans.
| Identifer | oai:union.ndltd.org:TW/085NTU00312015 |
| Date | January 1997 |
| Creators | Chan, Ching-Yi, 詹靜怡 |
| Contributors | Chang Geen-Dong, Huang Fore-Lien, 張震東, 黃火鍊 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 53 |
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