title: Functions for proteinases in the ovulatory process.
abstract: The ovary is a unique and dynamic organ in respect to rapid and extensive degrees of tissue development and remodeling that are periodically repeated in the female reproductive activity. Ovulation is a directed and sequential process accompanied by broad-spectrum proteolysis and culminates in the follicular rupture to release the matured oocyte. This review will focus on the potential roles of six representative proteinases that are involved in various aspects of ovulatory processes: matrix metalloproteinases (MMPs), plasminogen activator (PA)/plasmin, a disintegrin and metalloproteinase domain with thrombospondin motif (ADAMTS), cathepsin-L, pregnancy-associated plasma protein-A (PAPP-A), and bone morphogenetic protein 1/mammalian Tolloid (BMP-1/mTld). Based on the studies of expression and function, these selected proteinases provide and share diverse functions ranging from cleaving components of the extracellular matrix (ECM) to modulating non-ECM molecules, such as various growth factors and their binding proteins. Consistently, the genetic deletion of each individual gene in mice shows their functional overlap in the reproductive activity.
authors.affiliation: Department of Molecular Cell Biology, Medical Research Institute, Tokyo Medical and Dental University, Tokyo 101-0062, Japan; Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
authors.forename: Junji
authors.initials: J
authors.lastname: Ohnishi
authors.forename: Eriko
authors.initials: E
authors.lastname: Ohnishi
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Shibuya
authors.forename: Takayuki
authors.initials: T
authors.lastname: Takahashi
mesh_terms: D051722:ADAM Proteins; D000071097:ADAMTS1 Protein; D000818:Animals; D055395:Bone Morphogenetic Protein 1; D019485:Bone Morphogenetic Proteins / Q000172:deficiency / Q000502:physiology; D056668:Cathepsin L; D002403:Cathepsins / Q000172:deficiency / Q000502:physiology; D003546:Cysteine Endopeptidases / Q000172:deficiency / Q000502:physiology; D019483:Disintegrins / Q000172:deficiency / Q000502:physiology; D005260:Female; D005341:Fibrinolysin / Q000172:deficiency / Q000502:physiology; D006801:Humans; D020782:Matrix Metalloproteinases / Q000172:deficiency / Q000502:physiology; D008666:Metalloendopeptidases / Q000172:deficiency / Q000502:physiology; D045726:Metalloproteases / Q000502:physiology; D051379:Mice; D010053:Ovary / Q000201:enzymology*; D010060:Ovulation / Q000502:physiology*; D010447:Peptide Hydrolases / Q000502:physiology*; D010641:Phenotype; D010960:Plasminogen Activators / Q000172:deficiency / Q000502:physiology; D011266:Pregnancy-Associated Plasma Protein-A / Q000172:deficiency / Q000502:physiology; D055394:Tolloid-Like Metalloproteinases
chemical_list: D019485:Bone Morphogenetic Proteins; D019483:Disintegrins; D002403:Cathepsins; D045726:Metalloproteases; D010447:Peptide Hydrolases; D055394:Tolloid-Like Metalloproteinases; D010960:Plasminogen Activators; D005341:Fibrinolysin; D003546:Cysteine Endopeptidases; C534281:CTSL protein, human; D056668:Cathepsin L; C534278:Ctsl protein, mouse; D051722:ADAM Proteins; D000071097:ADAMTS1 Protein; C103859:ADAMTS1 protein, human; D020782:Matrix Metalloproteinases; D008666:Metalloendopeptidases; D011266:Pregnancy-Associated Plasma Protein-A; C484478:TLL1 protein, human; C484477:Tll1 protein, mouse; C525705:BMP1 protein, human; C525707:Bmp1 protein, mouse; D055395:Bone Morphogenetic Protein 1