Biomaterial Database

Regulation of gelatinase B (MMP-9) in leukocytes by plant lectins. 1998

B Dubois, and W J Peumans, and E J Van Damme, and J Van Damme, and G Opdenakker

Rega Institute for Medical Research, Laboratory of Molecular Immunology, University of Leuven, Belgium.

The stimulatory or inhibitory effects of plant lectins on the production of gelatinase A (MMP-2) and gelatinase B (MMP-9) by mononuclear white blood cells was investigated by substrate zymography. Leukocyte cultures from 24-h old buffy coats were spontaneously activated and produced high levels of gelatinase B. Using such cultures the suppressing activity of the Datura stramonium, Viscum album, Bauhinia purpurea, Triticum aestivum and Maackia amurensis lectins on gelatinase B induction were demonstrated. When fresh leukocyte preparations from single blood donors were used, low levels of gelatinase B were produced. The induction of gelatinase B was confirmed for concanavalin A and phytohaemagglutinin (PHA-L4). In addition, the Urtica dioica, Calystegia sepium, Convolvulus arvensis and Colchicum autumnale lectins were documented as novel and potent inducers of gelatinase B. Since high circulating gelatinase B levels are associated with specific pathologies, including shock syndromes, the acute toxicity of many lectins might be partially mediated or influenced by gelatinase induction.

UI	MeSH Term	Description	Entries
D007963	Leukocytes, Mononuclear	Mature LYMPHOCYTES and MONOCYTES transported by the blood to the body's extravascular space. They are morphologically distinguishable from mature granulocytic leukocytes by their large, non-lobed nuclei and lack of coarse, heavily stained cytoplasmic granules.	Mononuclear Leukocyte,Mononuclear Leukocytes,PBMC Peripheral Blood Mononuclear Cells,Peripheral Blood Human Mononuclear Cells,Peripheral Blood Mononuclear Cell,Peripheral Blood Mononuclear Cells,Leukocyte, Mononuclear
D008666	Metalloendopeptidases	ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.	Metallo-Endoproteinases,Metalloendopeptidase
D010944	Plants	Multicellular, eukaryotic life forms of kingdom Plantae. Plants acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations. It is a non-taxonomical term most often referring to LAND PLANTS. In broad sense it includes RHODOPHYTA and GLAUCOPHYTA along with VIRIDIPLANTAE.	Plant
D002478	Cells, Cultured	Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.	Cultured Cells,Cell, Cultured,Cultured Cell
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D017364	Collagenases	Enzymes that catalyze the degradation of collagen by acting on the peptide bonds.	Collagen Peptidase,Collagen-Degrading Enzyme,Collagenase,Collagen Degrading Enzyme,Peptidase, Collagen
D018093	Gelatinases	A class of enzymes that catalyzes the degradation of gelatin by acting on the peptide bonds. EC 3.4.24.-.	Gelatinase
D020778	Matrix Metalloproteinase 2	A secreted endopeptidase homologous with INTERSTITIAL COLLAGENASE, but which possesses an additional fibronectin-like domain.	Gelatinase A,72-kDa Gelatinase,72-kDa Type IV Collagenase,MMP-2 Metalloproteinase,MMP2 Metalloproteinase,Matrix Metalloproteinase-2,72 kDa Gelatinase,72 kDa Type IV Collagenase,Gelatinase, 72-kDa,MMP 2 Metalloproteinase,Metalloproteinase 2, Matrix,Metalloproteinase, MMP-2,Metalloproteinase, MMP2
D020780	Matrix Metalloproteinase 9	An endopeptidase that is structurally similar to MATRIX METALLOPROTEINASE 2. It degrades GELATIN types I and V; COLLAGEN TYPE IV; and COLLAGEN TYPE V.	Gelatinase B,92-kDa Gelatinase,92-kDa Type IV Collagenase,MMP-9 Metalloproteinase,MMP9 Metalloproteinase,Matrix Metalloproteinase-9,92 kDa Gelatinase,92 kDa Type IV Collagenase,MMP 9 Metalloproteinase,Metalloproteinase 9, Matrix,Metalloproteinase, MMP-9,Metalloproteinase, MMP9
D037102	Lectins	Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.	Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal