Biomedical and biotechnological applications of PEG- and PM-modified proteins

Inada, Yuji; Furukawa, Makoto; Sasaki, H.; Kodera, Yoh; Hiroto, Misao; Nishimura, Hiroyuki; Matsushima, Ayako

doi:10.1016/s0167-7799(00)88912-x

Cited by 215 publications

(105 citation statements)

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“…The purpose of these studies was to enhance the merits and improve the defects of proteins and to apply such conjugates for use in such fields as medical, pharmaceutical, engineering and agricultural sciences. Representative protein conjugates with synthetic polymers include the conjugates of proteins and polyethylene glycol (Inada et al, 1995;Veronese, 2001) and immobilized enzymes (Taylor, 1991;Liang et al, 2000). On the other hand, many studies to improve the functions of proteins by conjugation with various saccharides were also conducted: alkylation (Nieto & Palacian, 1983;Sen et al, 1981) esterification , amidation , deamidation (Matsudomi et al, 1985;Wu et al, 1976), lipophilization (Akita & Nakai, 1990a;1990b), covalent attachment of gluconic acid (Kitabatake et al, 1985), cross-linking with transglutaminase (Nio et al, 1985;Motoki et al, 1987) and so on.…”

Section: Introduction: What Is Neoglycoprotein ?mentioning

confidence: 99%

Functional Improvements in Food Proteins in Multiple Aspects by Conjugation with Saccharides: Case Studies of .BETA.-Lactoglobulin-Acidic Polysaccharides Conjugates.

Hattori

2002

FSTR

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Many studies on the conjugates of proteins and saccharides (neoglycoproteins) have been carried out over the past 20 years to improve the function of proteins. However, most have been carried out by attachment or elimination of low-molecular weight molecules for single purposes. The structure-function relationship of the conjugates has not been well understood, and little is known about the improvement of proteins by conjugation with polysaccharides. We sought to achieve functional improvements in food proteins in multiple aspects by conjugation with charged polysaccharides. We chose bovine ␤-lactoglobulin (␤-LG) as the target protein for improvement of the function and attached carboxymethyl dextrans (CMDs) of different molecular weight (10, 40, 70 and 162 kDa) covalently. After conjugation and purification, we explored the structure of the ␤-LG-CMD conjugates to prove that we could prepare conjugates while maintaining the native-like structure of protein molecule. By conjugation with CMDs, enhancement of thermal stability, improvement in the emulsifying properties and reduction of immunogenicity of ␤-LG could be achieved. Increases in the CMD content and net charge were viewed as the major factors in the improved emulsifying properties. Conjugation with high saccharide content using polysaccharides of higher molecular weight is believed to be effective in reduced immunogenicity of ␤-LG.

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Section: Introduction: What Is Neoglycoprotein ?mentioning

confidence: 99%

Functional Improvements in Food Proteins in Multiple Aspects by Conjugation with Saccharides: Case Studies of .BETA.-Lactoglobulin-Acidic Polysaccharides Conjugates.

Hattori

2002

FSTR

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“…PEG-asparaginase was found to be a useful alternative in patients with prior clinical hypersensitivity to native E. coli asparaginase. PEG-asparaginase reduces the immunogenicity of the protein, increases its stability in plasma and is suitable for use in heavily pretreated patients [60]. The recommended dose of pegaspargase is 2.5 IU/m 2 Intramuscularly (IM) or Intravenously (IV), and should be administered for every 14 days.…”

Section: Applications Of Microbial Amidases Therapeutic Applicationsmentioning

confidence: 99%

Microbial Amidases and their Industrial Applications: A Review

El-Ghonemy¹

2015

J Med Microb Diagn

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Among the pediatric cancer in developed countries, acute leukemia ¬constitutes the major part with affecting 30-45 per 1,000,000 children each year. The effect of treatment varies with differences in patients clinical, immunologic and genetic characteristics. Therefore, the search for efficient drugs to solve this problem is being continued worldwide. Although several kinds of treatments are available, enzyme therapy is equally effective. Enzymes have been used as drugs; likewise L-asparaginase and L-glutaminase had received much attention in recent years due to their anticarcinogenic potential. These enzymes constitute one of the most biotechnologically and biomedically important group of therapeutic enzymes accounting for about 40% of the total worldwide enzyme sales. Various sources are found to be good producers of the enzymes: bacteria, fungi along with some of the plant and animal species. Food and Drug Administration and World Health Organization have approved L-asparaginase for the effective treatment of acute lymphoblastic leukemia and lymphsarcoma. L-asparaginase and L-glutaminase break down L-asparagine or L-glutamine into L-aspartic acid or L-glutamic acid, respectively, and ammonia. L-asparagine depletion results in nutritional deprivation, inhibition of protein synthesis, and subsequent apoptotic cell death in lymphoblasts. On the other hand, the ability of L-asparaginase to selectively hydrolyzes L-asparagine into L-aspartateis a potential way to reduce the amount of free L-asparagine in the starting materials of food production, thus reducing the imminent risk of generating a potential carcinogenic and neurotoxic acrylamide that formed from L-asparagine and reducing sugars in carbohydrate-containing foods (such as snacks and biscuits) when they are heated above 120oC. Therefore, the present review is an attempt to compile information on the sources, antino plastic action and industrial application of microbial amidases enzymes.

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“…При использовании модифицированных ПЭГ L-аспарагиназ (ПЭГ-АСП) возрастает продолжительность их циркуляции в крови и биостабильность, вероятно, связанные с повышением устойчивости к протеолизу; снижается связывание с антителами и поглощение ретикулоэндотелиальной системой, а также способность вызывать аллергические реакции [75,76]. Всё это повышает терапевтическую эффективность и уменьшает вероятность побочных эффектов при длительном применении L-аспарагиназы.…”

Section: пегилированиеunclassified

Bacterial recombinant L-asparaginases: properties, structure and anti-proliferative activity

et al. 2015

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For more than 40 years L-asparaginases are used in combined therapy of acute lymphoblastic leukemia in children and the range of tumors sensitive to these enzymes constantly extends. This review summarizes results of studies aimed at creation of new systems for heterological expression of bacterial L-asparaginases as Erwinia carotovora (EwA), Helicobacter pylori (HpA), Yersinia pseudotuberculosis (YpA) and Rhodospirillum rubrum (RrA); special attention is paid to isolation of purified enzymes and their crystallization, modification by chitosan/polyethylene, physicochemical, kinetic and structural properties characterization, and the study of the cytotoxic or anti-proliferative activity of new recombinant L-asparaginases on cell cultures in vitro. The resultant recombinant L-asparaginases (EwA, YpA, HpA и RrA) exhibit reasonable cytotoxic action on the human leukemia cells comparable to the pharmacologically available L-asparaginase EcA and represent practical interest in respect to creation, on their basis, new effective antineoplastic remedies. Further prospects of researches on bacterial L-asparaginases are associated with development of analogs of Rhodospirillum rubrum L-asparaginase (RrA) by means of directed changes of the protein structure using genetic engineering, development of chito-PEGylation for receiving L-asparaginase preparations with improved pharmacokinetic characteristics.

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Biomedical and biotechnological applications of PEG- and PM-modified proteins

Cited by 215 publications

References 50 publications

Functional Improvements in Food Proteins in Multiple Aspects by Conjugation with Saccharides: Case Studies of .BETA.-Lactoglobulin-Acidic Polysaccharides Conjugates.

Functional Improvements in Food Proteins in Multiple Aspects by Conjugation with Saccharides: Case Studies of .BETA.-Lactoglobulin-Acidic Polysaccharides Conjugates.

Microbial Amidases and their Industrial Applications: A Review

Bacterial recombinant L-asparaginases: properties, structure and anti-proliferative activity

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