Literature summary for 3.4.21.75 extracted from

Wilbers, R.H.; Westerhof, L.B.; van Raaij, D.R.; van Adrichem, M.; Prakasa, A.D.; Lozano-Torres, J.L.; Bakker, J.; Smant, G.; Schots, A.
Co-expression of the protease furin in Nicotiana benthamiana leads to efficient processing of latent transforming growth factor-beta1 into a biologically active protein (2016), Plant Biotechnol. J., 14, 1695-1704 .

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Cloned(Commentary)

Cloned (Comment)	Organism
transient co-expression of human furin and human TGF-beta1 in the presence of the latency-associated peptide (LAP) in Nicotiana benthamiana leaves processing of the latent complex by a furin-like protease does not occur in planta. The use of a chitinase signal peptide enhances the expression and secretion of LAP-TGF-beta1, and co-expression of human furin enables the proteolytic processing of latent TGF-beta1 into a biologically active protein. Mature TGF-beta1 can be expressed without LAP, but results in necrosis (due to improper signal peptide cleavage). The Fc portion of immunoglobulin alpha 1 (Fcalpha), a natural dimer, is used as a fusion partner allowing dimerization of TGF-beta1. Furin requires multiple processing steps and correct localization within the secretory pathway to become active. Biological activity of Fcalpha-TGF-beta1 in crude plant extracts is assessed in a cell-based assay using mink lung epithelial cells carrying a TGF-beta-responsive luciferase reporter gene that is activated upon binding to the TGF-beta receptor. Proteolytic processing of LAP-TGF-beta1 in plants requires co-expression of furin	Homo sapiens

Cloned (Comment)

Organism

transient co-expression of human furin and human TGF-beta1 in the presence of the latency-associated peptide (LAP) in Nicotiana benthamiana leaves processing of the latent complex by a furin-like protease does not occur in planta. The use of a chitinase signal peptide enhances the expression and secretion of LAP-TGF-beta1, and co-expression of human furin enables the proteolytic processing of latent TGF-beta1 into a biologically active protein. Mature TGF-beta1 can be expressed without LAP, but results in necrosis (due to improper signal peptide cleavage). The Fc portion of immunoglobulin alpha 1 (Fcalpha), a natural dimer, is used as a fusion partner allowing dimerization of TGF-beta1. Furin requires multiple processing steps and correct localization within the secretory pathway to become active. Biological activity of Fcalpha-TGF-beta1 in crude plant extracts is assessed in a cell-based assay using mink lung epithelial cells carrying a TGF-beta-responsive luciferase reporter gene that is activated upon binding to the TGF-beta receptor. Proteolytic processing of LAP-TGF-beta1 in plants requires co-expression of furin

Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
pro-transforming growth factor-beta1 + H2O	Homo sapiens	-	transforming growth factor-beta1 + propeptide	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P09958	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pro-transforming growth factor-beta1 + H2O	-	Homo sapiens	transforming growth factor-beta1 + propeptide	-	?

General Information

General Information	Comment	Organism
physiological function	transforming growth factor beta (TGF-beta) is a signalling molecule that plays a key role in developmental and immunological processes in mammals. Pro-TGF-beta forms homodimers and is further processed in the trans-Golgi by a furin protease. Proteolytic cleavage by furin separates mature TGF-beta from latency-associated peptide (LAP). This dimeric complex is called the small latency complex (SLC) and keeps mature TGF-beta in an inactive form. Furin requires multiple processing steps and correct localization within the secretory pathway to become active	Homo sapiens