Core–shell protein clusters comprising haemoglobin and recombinant feline serum albumin as an artificial O<sub>2</sub>carrier for cats

Yokomaku, Kyoko; Akiyama, Motofusa; Morita, Yoshitsugu; Kihira, Kiyohito; Komatsu, Teruyuki

doi:10.1039/c8tb00211h

Cited by 12 publications

(6 citation statements)

References 46 publications

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“…In addition to HSA and BSA, three-dimensional structures of leporine (LSA), equine (ESA) [ 9 ], caprine (CapSA) and ovine (OSA) [ 63 ] serum albumins, as well as structures of recombinant canine (rCanSA) [ 64 ] and feline albumins (rFSA) [ 65 ], have been obtained so far. It is worth mentioning the main differences found when comparing these albumins.…”

Section: Transporting Function and Structural Characteristics Of Albumins Of Different Speciesmentioning

confidence: 99%

“…The environment around the Cys34 in rCanSA and rFSA is more polar and flexible compared to HSA, which explains why the free sulfhydryl group ratio of Cys34 is lower in cat and dog albumins compared to HSA [ 64 , 65 ]. Interestingly, warfarin and phenylbutazone (ligands of Sudlow site I) cannot bind to canine albumin, though superposition of rCanSA and HSA shows that the architectures of their Sudlow sites are identical and the side chains of Tyr150, Lys199, and Arg222 are located at the same positions [ 64 ].…”

Section: Transporting Function and Structural Characteristics Of Albumins Of Different Speciesmentioning

confidence: 99%

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Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Belinskaia

Voronina

Шмурак

et al. 2021

IJMS

141

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Being one of the main proteins in the human body and many animal species, albumin plays a decisive role in the transport of various ions—electrically neutral and charged molecules—and in maintaining the colloidal osmotic pressure of the blood. Albumin is able to bind to almost all known drugs, as well as many nutraceuticals and toxic substances, largely determining their pharmaco- and toxicokinetics. Albumin of humans and respective representatives in cattle and rodents have their own structural features that determine species differences in functional properties. However, albumin is not only passive, but also an active participant of pharmacokinetic and toxicokinetic processes, possessing a number of enzymatic activities. Numerous experiments have shown esterase or pseudoesterase activity of albumin towards a number of endogeneous and exogeneous esters. Due to the free thiol group of Cys34, albumin can serve as a trap for reactive oxygen and nitrogen species, thus participating in redox processes. Glycated albumin makes a significant contribution to the pathogenesis of diabetes and other diseases. The interaction of albumin with blood cells, blood vessels and tissue cells outside the vascular bed is of great importance. Interactions with endothelial glycocalyx and vascular endothelial cells largely determine the integrative role of albumin. This review considers the esterase, antioxidant, transporting and signaling properties of albumin, as well as its structural and functional modifications and their significance in the pathogenesis of certain diseases.

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Section: Transporting Function and Structural Characteristics Of Albumins Of Different Speciesmentioning

confidence: 99%

Section: Transporting Function and Structural Characteristics Of Albumins Of Different Speciesmentioning

confidence: 99%

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Belinskaia

Voronina

Шмурак

et al. 2021

IJMS

141

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“… 33 , 41 , 44 To date, there are eight SAs whose structures have been determined: bovine (BSA, Bos d 6), canine (CSA, Can f 3), equine (ESA, Equ c 3), feline (FSA, Fel d 2), HSA, goat (GSA), ovine (OSA),and rabbit (RSA). 35 , 41 , 45 , 46 , 47 , 48 …”

Section: Serum Albuminsmentioning

confidence: 99%

“…Therefore, it is not surprising that SAs, due to their high sequence identities, show significant levels of cross‐reactivity 33,41,44 . To date, there are eight SAs whose structures have been determined: bovine (BSA, Bos d 6), canine (CSA, Can f 3), equine (ESA, Equ c 3), feline (FSA, Fel d 2), HSA, goat (GSA), ovine (OSA),and rabbit (RSA) 35,41,45–48 …”

Section: Serum Albuminsmentioning

confidence: 99%

Allergens and their associated small molecule ligands—their dual role in sensitization

Chruszcz

Chew

Hoffmann‐Sommergruber

et al. 2021

Allergy

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“…Previously, it was assumed that the albumin molecule had the shape of an elongated or flattened ellipsoid (“cigar” or “pill”), but X-ray analysis showed that the protein has the shape of a heart. In addition to HSA, three-dimensional structures of BSA [ 61 ], albumin of horse and rabbit [ 61 ], sheep and goat [ 62 ], dogs [ 63 ] and cats [ 64 ] have been obtained so far.…”

Section: Structural Characteristics Of Albumin and Their Interspecmentioning

confidence: 99%

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

et al. 2020

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As a carrier of many biologically active compounds, blood is exposed to oxidants to a greater extent than the intracellular environment. Serum albumin plays a key role in antioxidant defence under both normal and oxidative stress conditions. This review evaluates data published in the literature and from our own research on the mechanisms of the enzymatic and non-enzymatic activities of albumin that determine its participation in redox modulation of plasma and intercellular fluid. For the first time, the results of numerous clinical, biochemical, spectroscopic and computational experiments devoted to the study of allosteric modulation of the functional properties of the protein associated with its participation in antioxidant defence are analysed. It has been concluded that it is fundamentally possible to regulate the antioxidant properties of albumin with various ligands, and the binding and/or enzymatic features of the protein by changing its redox status. The perspectives for using the antioxidant properties of albumin in practice are discussed.

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Core–shell protein clusters comprising haemoglobin and recombinant feline serum albumin as an artificial O₂carrier for cats

Abstract: Dual-protein clusters comprising haemoglobin and recombinant feline serum albumins as a red blood cell substitute for exclusive use in cats.

Cited by 12 publications

References 46 publications

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Allergens and their associated small molecule ligands—their dual role in sensitization

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

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Core–shell protein clusters comprising haemoglobin and recombinant feline serum albumin as an artificial O2carrier for cats

Abstract: Dual-protein clusters comprising haemoglobin and recombinant feline serum albumins as a red blood cell substitute for exclusive use in cats.

Cited by 12 publications

References 46 publications

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties

Allergens and their associated small molecule ligands—their dual role in sensitization

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

Contact Info

Product

Resources

About

Core–shell protein clusters comprising haemoglobin and recombinant feline serum albumin as an artificial O₂carrier for cats