Literature summary for 3.4.21.79 extracted from

Shevtsov, M.; Stangl, S.; Nikolaev, B.; Yakovleva, L.; Marchenko, Y.; Tagaeva, R.; Sievert, W.; Pitkin, E.; Mazur, A.; Tolstoy, P.; Galibin, O.; Ryzhov, V.; Steiger, K.; Smirnov, O.; Khachatryan, W.; Chester, K.; Multhoff, G.
Granzyme B functionalized nanoparticles targeting membrane Hsp70-positive tumors for multimodal cancer theranostics (2019), Small, 15, e1900205 .

Search for more literature for 3.4.21.79

Application

Application	Comment	Organism
pharmacology	functionalized superparamagnetic iron oxide nanoparticles (SPIONs) have emerged as potential clinical tools for cancer theranostics. GrB-functionalized SPIONs act as a contrast enhancement agent for magnetic resonance imaging and induce specific tumor cell apoptosis. Combinatorial regimens employing stereotactic radiotherapy and/or magnetic targeting are found to further enhance the therapeutic efficacy of GrB-SPIONs in different tumor mouse models. GrB-SPIONs accumulate in the tumor and increase MR contrast enhancement. The therapeutic potential of a systemic administration of GrB-SPIONs is evaluated in o.t. xenograft H1339 lung cancer model with and without brain metastases and U87 glioma mouse models, overview	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged inactive enzyme in HEK-293 cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	synthesis of the GrB-superparamagnetic nanocarriers (SPIONs): preparation of superparamagnetic iron oxide nanoparticles from salt solutions FeSO4 and FeCl3 by coprecipitation, dextran is added to the nanosuspension for prevention of sedimentation. The dextran coating of the synthesized nanoparticles is cross-linked with epichlorohydrin and aminated. Activated by carbodiimide aminated-dextran is coupled to the carboxyl groups of proteins. The hydrodynamic size and electrophoretic properties of the nanoparticles are estimated. Functionalized superparamagnetic iron oxide nanoparticles (SPIONs) have emerged as potential clinical tools for cancer theranostics. GrB-functionalized SPIONs act as a contrast enhancement agent for magnetic resonance imaging and induce specific tumor cell apoptosis. Combinatorial regimens employing stereotactic radiotherapy and/or magnetic targeting are found to further enhance the therapeutic efficacy of GrB-SPIONs in different tumor mouse models. Magnetic targeting of the nanoparticles in vivo with a magnet placed on top of orthotopic U87 glioblastoma in NMRU nu/nu mice and C6 glioma in Wistar rats drastically enhances the accumulation of nanoparticles to the location of the magnet	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Homo sapiens	5829	-
extracellular	-	Homo sapiens	-	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P10144	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged inactive enzyme from HEK-293 cells by nickel affinity chromatography, enzyme activation by enterokinase, and further purification by heparin affinity chromatography	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	following binding to Hsp70, GrB is rapidly internalized into tumor cells	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
GrB	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	the serine protease granzyme B (GrB) is produced as an effector molecule and is activated by T and natural killer cells, it specifically targets membrane-bound 70 kDa heat shock protein (mHsp70) on tumor cells, i.e. human tumor cell lines LN229 (glioblastoma), U87 (glioblastoma), HeLa (cervix carcinoma), and H1339 (SCLC), and animal cell lines C6 (rat glioma) and GL261 (glioma). The serine protease granzyme B (GrB) derived from lysates of activated NK cells specifically binds to a sequence of Hsp70 (TKDNNLLGRFELSG, aa450-463) that mediates oligomerization of Hsp70 and is exposed on the cell surface of mHsp70 positive tumor cells. Following binding to mHsp70, GrB is specifically taken up into the cytosol and thereby induces apoptosis in a perforin-independent manner	Homo sapiens

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Release 2023.1 (January 2023)