Evidence for the presence of α1 B-glycoprotein in mammalian sera: immunoblotting studies

Stratil, A.; Kaláb, Petr; Pokorný, R.

doi:10.1016/0305-0491(88)90208-8

Cited by 5 publications

(3 citation statements)

References 11 publications

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“…Besides in humans, A1BG has also been detected in more than 40 other mammalian species and is thought to be present in plasma of all mammals (40). CRISP-3, however, has only been detected in three mammalian species (human, horse, and mouse) and in plasma so far only in humans.…”

Section: Discussionmentioning

confidence: 99%

Cysteine-Rich Secretory Protein 3 Is a Ligand of α₁B-Glycoprotein in Human Plasma

et al. 2004

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Human cysteine-rich secretory protein 3 (CRISP-3; also known as SGP28) belongs to a family of closely related proteins found in mammals and reptiles. Some mammalian CRISPs are known to be involved in the process of reproduction, whereas some of the CRISPs from reptiles are neurotoxin-like substances found in lizard saliva or snake venom. Human CRISP-3 is present in exocrine secretions and in secretory granules of neutrophilic granulocytes and is believed to play a role in innate immunity. On the basis of the relatively high content of CRISP-3 in human plasma and the small size of the protein (28 kDa), we hypothesized that CRISP-3 in plasma was bound to another component. This was supported by size-exclusion chromatography and immunoprecipitation of plasma proteins. The binding partner was identified by mass spectrometry as alpha(1)B-glycoprotein (A1BG), which is a known plasma protein of unknown function and a member of the immunoglobulin superfamily. We demonstrate that CRISP-3 is a specific and high-affinity ligand of A1BG with a dissociation constant in the nanomolar range as evidenced by surface plasmon resonance. The A1BG-CRISP-3 complex is noncovalent with a 1:1 stoichiometry and is held together by strong electrostatic forces. Similar complexes have been described between toxins from snake venom and A1BG-like plasma proteins from opossum species. In these cases, complex formation inhibits the toxic effect of snake venom metalloproteinases or myotoxins and protects the animal from envenomation. We suggest that the A1BG-CRISP-3 complex displays a similar function in protecting the circulation from a potentially harmful effect of free CRISP-3.

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Section: Discussionmentioning

confidence: 99%

Cysteine-Rich Secretory Protein 3 Is a Ligand of α₁B-Glycoprotein in Human Plasma

et al. 2004

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“…The high affinity of abundant serum proteins towards all investigated NPs inhibited the detection of less abundant serum proteins by mass spectrometry and only allowed minor differences in the adsorption patterns to be identied. The main identied proteins adsorbed onto all PVA-SPION surfaces, irrespective of their surface charge or the incubation period, were BSA, which is known to acts as a "dys-opsonin", thus prolonging the circulation time of NPs in blood; 51-53 alpha-2macrogloblulin, known to inhibit proteinases; 54 serotransferrin and vitamin D-binding protein, important proteins in transport and trafficking; 55,56 alpha-fetoprotein, which has a regulatory effect associated with the regulation of growth, differentiation, regeneration, and transformation in both ontogenetic and oncogenic growth processes; 57 alpha-1B-glycoprotein, an immunoglobulin superfamily member whose biological function still remains unknown; 58,59 alpha-1-antiproteinase, which is involved in blood coagulation 54 and alpha-2-HS-gylcoprotein, which is involved in several functions, such as endocytosis, brain development and formation of bone tissue. 54 Based on these observations it could be suggested that protein adsorption can be independent of the NP surface charge.…”

Section: Np-protein Interactionsmentioning

confidence: 99%

Surface charge of polymer coated SPIONs influences the serum protein adsorption, colloidal stability and subsequent cell interaction in vitro

et al. 2013

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It is known that the nanoparticle-cell interaction strongly depends on the physicochemical properties of the investigated particles. In addition, medium density and viscosity influence the colloidal behaviour of nanoparticles. Here, we show how nanoparticle-protein interactions are related to the particular physicochemical characteristics of the particles, such as their colloidal stability, and how this significantly influences the subsequent nanoparticle-cell interaction in vitro. Therefore, different surface charged superparamagnetic iron oxide nanoparticles were synthesized and characterized. Similar adsorbed protein profiles were identified following incubation in supplemented cell culture media, although cellular uptake varied significantly between the different particles. However, positively charged nanoparticles displayed a significantly lower colloidal stability than neutral and negatively charged particles while showing higher non-sedimentation driven cell-internalization in vitro without any significant cytotoxic effects. The results of this study strongly indicate therefore that an understanding of the aggregation state of NPs in biological fluids is crucial in regards to their biological interaction(s).

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“…In view of the homology between oprin and human alB-G and the fact that alB-G has been reported in many other mammalian sera (Stratil et al, 1988; Patterson et al, 1991), the name opossum alB-glycoprotein is more appropriate. In this paper, the terms oprin and opossum alBglycoprotein are used interchangeably.…”

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confidence: 99%

Isolation from opossum serum of a metalloproteinase inhibitor homologous to human .alpha.1B-glycoprotein

Catanese¹,

Kress²

1992

Biochemistry

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Fractionation of opossum (Didelphis virginiana) serum with (NH4)2SO4, followed by chromatography on DEAE-Sepharose, phenyl-Sepharose, and Mono Q HR 5/5, has resulted in the isolation in homogeneous condition of a metalloproteinase inhibitor designated oprin (opossum proteinase inhibitor). Oprin is a single-chain glycoprotein (26% carbohydrate) with an estimated Mr = 52,000, pI = 3.5, and E(1%/1 cm) = 11. Oprin inhibited snake venom metalloproteinases, but showed no activity on venom serine proteinases or on bacterial metalloproteinases. Incubation of Crotalus atrox alpha-proteinase (EC 3.4.24.1) with oprin, and analysis of the reaction products by chromatography on Mono Q HR 5/5 and by electrophoresis under nondenaturing conditions, indicated formation of an inactive enzyme/inhibitor complex. The complex dissociated during SDS/polyacrylamide gel electrophoresis. An opossum liver cDNA library was immunoscreened, and clones containing cDNA encoding for part of the open reading frame for oprin were isolated. The cDNA inserts contained nucleotide sequences corresponding to two internal amino acid sequences of oprin which had been separately determined by protein sequence analysis. Protein database screening using a 211 amino acid sequence deduced from one of the cDNA inserts showed no significant homology to known proteinase inhibitors. There was, however, a 36% identity with human alpha 1B-glycoprotein, a plasma protein of unknown function related to the immunoglobulin supergene family. In addition, the amino-terminal sequence of oprin showed 46% identity with human alpha 1B-glycoprotein in a 26 amino acid residue overlap.(ABSTRACT TRUNCATED AT 250 WORDS)

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Evidence for the presence of α1 B-glycoprotein in mammalian sera: immunoblotting studies

Cited by 5 publications

References 11 publications

Cysteine-Rich Secretory Protein 3 Is a Ligand of α₁B-Glycoprotein in Human Plasma

Cysteine-Rich Secretory Protein 3 Is a Ligand of α₁B-Glycoprotein in Human Plasma

Surface charge of polymer coated SPIONs influences the serum protein adsorption, colloidal stability and subsequent cell interaction in vitro

Isolation from opossum serum of a metalloproteinase inhibitor homologous to human .alpha.1B-glycoprotein

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Evidence for the presence of α1 B-glycoprotein in mammalian sera: immunoblotting studies

Cited by 5 publications

References 11 publications

Cysteine-Rich Secretory Protein 3 Is a Ligand of α1B-Glycoprotein in Human Plasma

Cysteine-Rich Secretory Protein 3 Is a Ligand of α1B-Glycoprotein in Human Plasma

Surface charge of polymer coated SPIONs influences the serum protein adsorption, colloidal stability and subsequent cell interaction in vitro

Isolation from opossum serum of a metalloproteinase inhibitor homologous to human .alpha.1B-glycoprotein

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Cysteine-Rich Secretory Protein 3 Is a Ligand of α₁B-Glycoprotein in Human Plasma

Cysteine-Rich Secretory Protein 3 Is a Ligand of α₁B-Glycoprotein in Human Plasma