Structure, expression, and developmental function of early divergent forms of metalloproteinases in Hydra

被引:28
作者
Sarras, MP
Yan, L
Leontovich, A
Zhang, JS
机构
[1] Univ Kansas, Med Ctr, Dept Anat & Cell Biol, Kansas City, KS 66160 USA
[2] Centocor Inc, Malvern, PA 19355 USA
[3] Mayo Clin, Dept Expt Pathol, Rochester, MN 55904 USA
[4] Univ Kansas, Lawrence, KS 66047 USA
关键词
Hydra; metalloproteinases; development; astacin; matrix metalloproteinases; endothelin;
D O I
10.1038/sj.cr.7290123
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Metalloproteinases have a critical role in a broad spectrum of cellular processes ranging from the breakdown of extracellular matrix to the processing of signal transduction-related proteins. These hydrolytic functions underlie a variety of mechanisms related to developmental processes as well as disease states. Structural analysis of metalloproteinases from both invertebrate and vertebrate species indicates that these enzymes are highly conserved and arose early during metazoan evolution. In this regard, studies from various laboratories have reported that a number of classes of metalloproteinases are found in hydra, a member of Cnidaria, the second oldest of existing animal phyla. These studies demonstrate that the hydra genome contains at least three classes of metalloproteinases to include members of the 1) astacin class, 2) matrix metalloproteinase class, and 3) neprilysin class. Functional studies indicate that these metalloproteinases play diverse and important roles in hydra morphogenesis and cell differentiation as well as specialized functions in adult polyps. This article will review the structure, expression, and function of these metalloproteinases in hydra.
引用
收藏
页码:163 / 176
页数:14
相关论文
共 85 条
[61]   Hydra and Niccolo!Paganini (1782-1840) -: two peas in a pod?: The molecular basis of extracellular matrix structure in the invertebrate, Hydra [J].
Sarras, MP ;
Deutzmann, R .
BIOESSAYS, 2001, 23 (08) :716-724
[62]   CLONING AND BIOLOGICAL FUNCTION OF LAMININ IN HYDRA-VULGARIS [J].
SARRAS, MP ;
YAN, L ;
GRENS, A ;
ZHANG, XM ;
AGBAS, A ;
HUFF, JK ;
STJOHN, PL ;
ABRAHAMSON, DR .
DEVELOPMENTAL BIOLOGY, 1994, 164 (01) :312-324
[63]  
SARRAS MP, 1997, ASTACINS STRUCTURE F, P307
[64]   Matrix metalloproteinase MMP-19 (RASI 1) is expressed on the surface of activated peripheral blood mononuclear cells and is detected as an autoantigen in rheumatoid arthritis [J].
Sedlacek, R ;
Mauch, S ;
Kolb, B ;
Schätzlein, C ;
Eibel, H ;
Peter, HH ;
Schmitt, J ;
Krawinkel, U .
IMMUNOBIOLOGY, 1998, 198 (04) :408-423
[65]   Rat endothelin-converting enzyme-1 forms a dimer through Cys(412) with a similar catalytic mechanism and a distinct substrate binding mechanism compared with neutral endopeptidase-24.11 [J].
Shimada, K ;
Takahashi, M ;
Turner, AJ ;
Tanzawa, K .
BIOCHEMICAL JOURNAL, 1996, 315 :863-867
[66]   THE DROSOPHILA DORSAL-VENTRAL PATTERNING GENE TOLLOID IS RELATED TO HUMAN BONE MORPHOGENETIC PROTEIN-1 [J].
SHIMELL, MJ ;
FERGUSON, EL ;
CHILDS, SR ;
OCONNOR, MB .
CELL, 1991, 67 (03) :469-481
[67]  
Shimizu H, 2002, DEVELOPMENT, V129, P1521
[68]   Neuropilin in the midst of cell migration and retraction [J].
Soker, S .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 2001, 33 (04) :433-437
[69]  
STEINER DF, 1992, J BIOL CHEM, V267, P23435
[70]   How matrix metalloproteinases regulate cell behavior [J].
Sternlicht, MD ;
Werb, Z .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 2001, 17 :463-516