PMID: 8444167Feb 15, 1993Paper

An N-terminal peptide from link protein is rapidly degraded by chondrocytes, monocytes and B cells

European Journal of Biochemistry
H Martin, M F Dean

Abstract

A peptide cleaved from the link-protein component of human and pig proteoglycan aggregates by trypsin and stromelysin was taken up and degraded further by human monocytes, B cells, chondrocytes and by mouse peritoneal macrophages. Monocytes were able to process the peptide twice as rapidly as peritoneal macrophages and some 16 times more rapidly than articular chondrocytes. The B cell line Priess, which unlike the monocytes and macrophages could not take up or degrade whole proteoglycan aggregates, was able to degrade the peptide at a rapid rate. Synthetic, unglycosylated peptides consisting of the first 16 and 13 N-terminal amino acids of human link protein, corresponding to its stromelysin-cleavage and trypsin-cleavage products, were also taken up and degraded in a similar manner to the natural products and, in addition, were able to block uptake of the 125I-labelled natural peptides. The isoelectric points of the re-secreted breakdown fragment from both the synthetic and natural peptides were identical and each peptide was processed by the cells to produce a single radiolabelled fragment. Each of these fragments was eluted with the same retention time during HPLC, indicating that the natural peptides were derived from the N-...Continue Reading

References

Jan 1, 1979·The Biochemical Journal·T E Hardingham
Apr 12, 1990·Nature·A AitkenA Toker
Jun 1, 1988·Journal of Leukocyte Biology·M F DeanP Stahl
Jan 1, 1989·International Immunology·J B RothbardJ R Lamb
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Citations

Jul 6, 2000·The Biochemical Journal·M F Dean, P Sansom
May 7, 2003·The Journal of Biological Chemistry·Mátyás CzipriTibor T Glant
Oct 17, 2019·Cold Spring Harbor Perspectives in Medicine·Mitchell Fane, Ashani T Weeraratna
Dec 15, 2019·Nature Reviews. Cancer·Mitchell Fane, Ashani T Weeraratna
Aug 11, 2021·Tissue Engineering. Part B, Reviews·Boushra AjeebMichael S Detamore

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