Galectin 3‐binding protein is a potential contaminant of recombinantly produced factor IX

Blostein, Mark; Cuerquis, Jessica; Galipeau, Jacques

doi:10.1111/j.1365-2516.2007.01525.x

Cited by 4 publications

(4 citation statements)

References 20 publications

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“…Gelectins and their binding proteins have primarily been described in cell-cell and cell-matrix interactions and play roles in autoimmunity, inflammation and tumor progression or metastasis [44]. G3BP promotes integrin-mediated cell adhesion and functions in cancer progression of human tumor cells.…”

Section: Resultsmentioning

confidence: 99%

Protein Profiling of Human Nonpigmented Ciliary Epithelium Cell Secretome: The Differentiation Factors Characterization for Retinal Ganglion Cell line

Yang

Krishnamoorthy

Jong

et al. 2011

BioMed Research International

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The purpose of this paper was to characterize proteins secreted from the human nonpigmented ciliary epithelial (HNPE) cells, which have differentiated a rat retinal ganglion cell line, RGC-5. Undifferentiated RGC-5 cells have been shown to express several marker proteins characteristic of retinal ganglion cells. However, RGC-5 cells do not respond to N-methyl-D aspartate (NMDA), or glutamate. HNPE cells have been shown to secrete numbers of neuropeptides or neuroproteins also found in the aqueous humor, many of which have the ability to influence the activity of neuronal cells. This paper details the profile of HNPE cell-secreted proteins by proteomic approaches. The experimental results revealed the identification of 132 unique proteins from the HNPE cell-conditioned SF-medium. The biological functions of a portion of these identified proteins are involved in cell differentiation. We hypothesized that a differentiation system of HNPE cell-conditioned SF-medium with RGC-5 cells can induce a differentiated phenotype in RGC-5 cells, with functional characteristics that more closely resemble primary cultures of rat retinal ganglion cells. These proteins may replace harsh chemicals, which are currently used to induce cell differentiation.

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Section: Resultsmentioning

confidence: 99%

Protein Profiling of Human Nonpigmented Ciliary Epithelium Cell Secretome: The Differentiation Factors Characterization for Retinal Ganglion Cell line

Yang

Krishnamoorthy

Jong

et al. 2011

BioMed Research International

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“…Proteomic technologies are widely used as an efficient tool for process development and characterization of recombinant therapeutic proteins, such as monoclonal antibodies, clotting factors and other physiologically active proteins [27, 28]. However, there have been only a few applications of proteomics for in-process and quality control of therapeutic proteins from human plasma [11–13, 17, 18, 29].…”

Section: Discussionmentioning

confidence: 99%

“…The most important post-translational modification is gamma-carboxylation (Gla). This reaction is catalyzed in the liver by gamma-glutamyl transferase, and is critical in production of this recombinant clotting factor [28]. While the PTMs of r F IX are well characterized, the structure and PTMs of pd F IX and other pd vitamin K dependent clotting factors and inhibitors are still poorly described in the literature [31, 32].…”

Section: Discussionmentioning

confidence: 99%

Use of proteomics for validation of the isolation process of clotting factor IX from human plasma

Clifton

Huang

Gašo-Sokač

et al. 2010

Journal of Proteomics

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The use of proteomic techniques in the monitoring of different production steps of plasma-derived clotting factor IX (pd F IX) was demonstrated. The first step, solid-phase extraction with a weak anion-exchange resin, fractionates the bulk of human serum albumin (HSA), immunoglobulin G, and other non-binding proteins from F IX. The proteins that strongly bind to the anion-exchange resin are eluted by higher salt concentrations. In the second step, anion-exchange chromatography, residual HSA, some proteases and other contaminating proteins are separated. In the last chromatographic step, affinity chromatography with immobilized heparin, the majority of the residual impurities are removed. However, some contaminating proteins still remain in the eluate from the affinity column. The next step in the production process, virus filtration, is also an efficient step for the removal of residual impurities, mainly high molecular weight proteins, such as vitronectin and inter-alpha inhibitor proteins. In each production step, the active component, pd F IX and contaminating proteins are monitored by biochemical and immunochemical methods and by LC-MS/MS and their removal documentedOur methodology is very helpful for further process optimization, rapid identification of target proteins with relatively low abundance, and for the design of subsequent steps for their removal or purification.

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“…214 The appearance of Mac-2 BP/90K as contaminant in preparations of recombinant coagulation factor IX was therefore judged to be cause of 'unforeseen consequences'. 215 Its pro-inflammatory signalling function is not only active in osteoarthritis pathogenesis, 102 but, for example, also locally in unstable plaque regions of carotid endarterectomy 216 or rheumatoid synovium. 217 The molecular and topological nature of the active galectin-counterreceptor lattice for outside-in signalling remains to be defined.…”

Section: Lectin Diversity: the Example Of Galectinsmentioning

confidence: 99%

Sensing Glycans as Biochemical Messages by Tissue Lectins: The Sugar Code at Work in Vascular Biology

Kaltner

Gabius

2019

Thromb Haemost

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Although a plethora of players has already been revealed to be engaged in the haemostatic system, a fundamental consideration of the molecular nature of information coding can give further explorations of the mechanisms of blood clotting, platelet functionality and vascular trafficking direction. By any measures, looking at ranges of occurrence and of potential for structural versatility, at strategic positioning to influence protein and cell sociology as well as at dynamics of processing and restructuring for phenotypic variability, using sugars as an alphabet of life for generating the glycan part of glycoconjugates is a success story. The handiwork by the complex system for glycan biosynthesis renders biochemical messages of exceptionally high coding capacity available. They are read and translated into cellular effects by receptors termed lectins. The different levels of regulation on both sides, that is, glycan and lectin, establish an intriguingly fine-tuned capacity for functional pairing. The emerging insights into the highly branched routes of glycosylation, into lectin structures up to complete characterization in solution and the shape of lectin networks, first obtained for the three selectins, now extended to considering many other C-type lectins, galectins and siglecs, as well as into intra- and inter-family cross-talk and cooperations are sure to push boundaries in our understanding of the molecular basis of haemostasis.

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Galectin 3‐binding protein is a potential contaminant of recombinantly produced factor IX

Cited by 4 publications

References 20 publications

Protein Profiling of Human Nonpigmented Ciliary Epithelium Cell Secretome: The Differentiation Factors Characterization for Retinal Ganglion Cell line

Protein Profiling of Human Nonpigmented Ciliary Epithelium Cell Secretome: The Differentiation Factors Characterization for Retinal Ganglion Cell line

Use of proteomics for validation of the isolation process of clotting factor IX from human plasma

Sensing Glycans as Biochemical Messages by Tissue Lectins: The Sugar Code at Work in Vascular Biology

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