Linked Life Data

21383996

Source:http://linkedlifedata.com/resource/pubmed/id/21383996

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2011-3-25
pubmed:abstractText
In the beginning of the 20th century, enzymes with proteolytic activity were classified as peptidases, Erepsin, and proteases. Among these, pepsin, trypsin, and autolytic enzymes were of the protease class. Spleen-derived proteases were poorly characterized until Sven Gustaf Hedin performed several digestion experiments with bovine spleen. He incubated minced bovine spleen under acidic or neutral conditions and characterized two active proteases; the results were published in 1903. The first protease was named ?-protease and was active under neutral conditions. The second was named ?-protease and was active under acidic conditions. We replicated Hedin's experiments according to his methods and found, by using activity-based probes to visualize proteases, that the historical ?-protease is the present-day serine protease cathepsin G (CatG), which is known to be important in several immune processes, including antigen processing, chemotaxis, and activation of surface receptors. The ?-protease, however, comprised different proteases including CatX, B, S, and D. We suggest that Hedin described CatG activity in bovine spleen over 100 years ago.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1734-154X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-44
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Was the serine protease cathepsin G discovered by S. G. Hedin in 1903 in bovine spleen?
pubmed:affiliation
Division of Endocrinology and Diabetes, Department of Internal Medicine I, University Medical Center Ulm, Ulm, Germany.
pubmed:publicationType
Journal Article, Historical Article, Research Support, Non-U.S. Gov't