Heterologously overexpressed, affinity-purified human meprin α is functionally active and cleaves components of the basement membrane in vitro

Meprins are astacin-like metalloproteases of renal and intestinal epithelia and embryonic neuroepithelial cells. The full length cDNA of the human meprin α subunit has been overexpressed in baculovirus-infected insect cells yielding the tetrameric proprotein which could be proteolytically activated...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	FEBS letters 2000-01, Vol.465 (1), p.2-7
Hauptverfasser:	Köhler, Danny, Kruse, Markus-N., Stöcker, Walter, Sterchi, Erwin E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Astacin family Baculoviridae - genetics Baculovirus Basement Membrane - metabolism Cell Line Chromatography, Affinity DNA, Complementary - isolation & purification EGF, epidermal growth factor Enzyme Activation Enzyme Precursors - biosynthesis Enzyme Precursors - genetics Enzyme Precursors - metabolism Expression Gene Expression Insecta Laminin - metabolism Laminin cleavage MAM, meprin, A5 protein, receptor protein-tyrosine phosphatase μ MATH, meprin and TRAF homology Meprin Metalloendopeptidases - biosynthesis Metalloendopeptidases - genetics Metalloendopeptidases - metabolism PAA, polyacrylamide PABA-peptide, N-benzoyl-tyrosyl-p-aminobenzoic acid PBS, phosphate-buffered saline SF, Spodoptera frugiperda Transfection
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!