Dataset Information

Proteolytic processing of CD99

ABSTRACT: The adhesion molecule CD99 is essential for transendothelial migration (TEM) of leukocytes. Here we demonstrate by biochemical and cellular assays that CD99 undergoes ectodomain shedding by the metalloprotease meprin β and subsequent intramembrane proteolysis by γ-secretase. The cleavage site in CD99 was identified by mass spectrometry within an acidic region highly conserved through different vertebrate species.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Andreas Tholey

LAB HEAD: Andreas Tholey

PROVIDER: PXD005428 | Pride | 2017-01-02

REPOSITORIES: Pride

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Publications

Ectodomain shedding of CD99 within highly conserved regions is mediated by the metalloprotease meprin β and promotes transendothelial cell migration.

Bedau Tillmann T Peters Florian F Prox Johannes J Arnold Philipp P Schmidt Frederike F Finkernagel Malin M Köllmann Sandra S Wichert Rielana R Otte Anna A Ohler Anke A Stirnberg Marit M Lucius Ralph R Koudelka Tomas T Tholey Andreas A Biasin Valentina V Pietrzik Claus U CU Kwapiszewska Grazyna G Becker-Pauly Christoph C

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 20161221 3

The adhesion molecule CD99 is essential for the transendothelial migration of leukocytes. In this study, we used biochemical and cellular assays to show that CD99 undergoes ectodomain shedding by the metalloprotease meprin β and subsequent intramembrane proteolysis by γ-secretase. The cleavage site in CD99 was identified by mass spectrometry within an acidic region highly conserved through different vertebrate species. This finding fits perfectly to the unique cleavage specificity of meprin β wi ...[more]

PMID: 28003343

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			Action	DRS
	CD_99_1_6uL.msf	Msf
	CD_99_1_6uL.pep.xml.xml	Pepxml
	CD_99_1_6uL.raw	Raw
	CD_99_2_6uL.msf	Msf
	CD_99_2_6uL.pep.xml.xml	Pepxml