Linked Life Data

3003112

Source:http://linkedlifedata.com/resource/pubmed/id/3003112

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1986-3-21
pubmed:abstractText
A type IV collagenolytic metalloproteinase secreted by human monocytes/macrophages has been isolated and characterized. Monocytes isolated from peripheral blood and cultured in vitro exhibited a high type IV collagenolytic activity during the first and second day, but such activity declined markedly over subsequent days. Type IV collagenolytic activity was also transiently elaborated by macrophages isolated from (a) bronchioalveolar lavage of patients with pulmonary sarcoidosis, (b) primary human colostrum, and (c) peritoneal lavage of a patient with peritonitis. In contrast, macrophages isolated from the bronchioalveolar lavage of normal individuals, or from noninflammatory peritoneal fluids, failed to exhibit type IV collagenolytic activity. A type IV collagenolytic neutral proteinase was purified from macrophages isolated from inflammatory peritoneal fluid. The proteinase has a mass of 67 kDa on gel electrophoresis and is not altered in its migration under reducing conditions. It produces a characteristic 1/4-3/4 cleavage of type IV collagen, and its activity is abolished by treatment with EDTA but not phenylmethanesulfonyl fluoride. The isoelectric pH of the proteinase is 5.2 as judged by two-dimensional gel electrophoresis. The amino acid composition of the proteinase was notable for a high content of serine, glutamic acid, glycine, and alanine and no detectable hydroxyproline, cysteine, or methionine residues. The carbohydrate content of the proteinase was 11.2%, and galactose was the most abundant monosaccharide (8.7%) released following acid hydrolysis, followed by glucose (1.3%), mannose (1.2%), and trace amounts of fucose and galactosamine. Such a type IV collagenolytic protease may play an important role during the traversal of the vascular basement membrane by extravasating monocytes. The biochemical characteristics and biologic function of the macrophage proteinase may be similar or identical to the type IV collagenolytic proteinase identified in metastatic tumor cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2369-75
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:3003112-Adult, pubmed-meshheading:3003112-Amino Acids, pubmed-meshheading:3003112-Carbohydrates, pubmed-meshheading:3003112-Cells, Cultured, pubmed-meshheading:3003112-Chromatography, Gel, pubmed-meshheading:3003112-Chromatography, High Pressure Liquid, pubmed-meshheading:3003112-Collagen, pubmed-meshheading:3003112-Colostrum, pubmed-meshheading:3003112-Edetic Acid, pubmed-meshheading:3003112-Endopeptidases, pubmed-meshheading:3003112-Female, pubmed-meshheading:3003112-Gene Expression Regulation, pubmed-meshheading:3003112-Glycoproteins, pubmed-meshheading:3003112-Humans, pubmed-meshheading:3003112-Inflammation, pubmed-meshheading:3003112-Macrophages, pubmed-meshheading:3003112-Male, pubmed-meshheading:3003112-Metalloendopeptidases, pubmed-meshheading:3003112-Microbial Collagenase, pubmed-meshheading:3003112-Middle Aged, pubmed-meshheading:3003112-Monocytes, pubmed-meshheading:3003112-Neoplasm Proteins, pubmed-meshheading:3003112-Peritoneal Cavity, pubmed-meshheading:3003112-Peritonitis, pubmed-meshheading:3003112-Phenylmethylsulfonyl Fluoride, pubmed-meshheading:3003112-Pregnancy, pubmed-meshheading:3003112-Protease Inhibitors, pubmed-meshheading:3003112-Pulmonary Alveoli
pubmed:year
1986
pubmed:articleTitle
Transient expression of type IV collagenolytic metalloproteinase by human mononuclear phagocytes.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't