Avidin is a heparin-binding protein. Affinity, specificity and structural analysis

Kett, Warren C.; Osmond, Ronald I. W.; Moe, Lily; Skett, Spencer E; Kinnear, Beverley F.; Coombe, Deirdre R.

doi:10.1016/s0304-4165(02)00539-1

Cited by 48 publications

(30 citation statements)

References 28 publications

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“…Avidin molecules have a strong affinity for highly negatively charged molecules in MC secretory granules, e.g., heparin (26). We therefore investigated whether incorporation of fluorochrome-labeled avidin could interfere with MC degranulation, the release of granule-associated mediators, or the induction of classical MC-dependent allergic inflammation at sites of IgE-dependent passive cutaneous anaphylaxis (PCA).…”

Section: Resultsmentioning

confidence: 99%

Imaging protective mast cells in living mice during severe contact hypersensitivity

Reber¹,

Sibilano²,

Starkl³

et al. 2017

JCI Insight

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Section: Resultsmentioning

confidence: 99%

Imaging protective mast cells in living mice during severe contact hypersensitivity

Reber¹,

Sibilano²,

Starkl³

et al. 2017

JCI Insight

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“…Unlike previously published heparinization methods that involve multiple steps, the use of biotin and prefabricated heparin complexes reduce the handling time and the risk of damage to the islets. The present heparinization protocol is based on the fact that avidin expresses binding sites for both biotin and heparin (22), thus bolstering the multiattachment binding effect achieved by using a conjugate composed of multiple heparin molecules.…”

Section: Discussionmentioning

confidence: 99%

Islet Surface Heparinization Prevents the Instant Blood-Mediated Inflammatory Reaction in Islet Transplantation

et al. 2007

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OBJECTIVE—In clinical islet transplantation, the instant blood-mediated inflammatory reaction (IBMIR) is a major factor contributing to the poor initial engraftment of the islets. This reaction is triggered by tissue factor and monocyte chemoattractant protein (MCP)-1, expressed by the transplanted pancreatic islets when the islets come in contact with blood in the portal vein. All currently identified systemic inhibitors of the IBMIR are associated with a significantly increased risk of bleeding or other side effects. To avoid systemic treatment, the aim of the present study was to render the islet graft blood biocompatible by applying a continuous heparin coating to the islet surface. RESEARCH DESIGN AND METHODS—A biotin/avidin technique was used to conjugate preformed heparin complexes to the surface of pancreatic islets. This endothelial-like coating was achieved by conjugating barely 40 IU heparin per full-size clinical islet transplant. RESULTS—Both in an in vitro loop model and in an allogeneic porcine model of clinical islet transplantation, this heparin coating provided protection against the IBMIR. Culturing heparinized islets for 24 h did not affect insulin release after glucose challenge, and heparin-coated islets cured diabetic mice in a manner similar to untreated islets. CONCLUSIONS—This novel pretreatment procedure prevents intraportal thrombosis and efficiently inhibits the IBMIR without increasing the bleeding risk and, unlike other pretreatment procedures (e.g., gene therapy), without inducing acute or chronic toxicity in the islets.

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“…Recent studies demonstrate that avidin and some avidin-related genes are induced during inflammation [4]. Moreover, the evidence that avidin binds specifically heparin [5] and possibly its natural counterparts, heparan sulfate proteoglycans that are activated and secreted as part of normal defenses to injury, stress or inflammation, reinforces the hypothesis that avidin plays a critical role in the innate immune response.…”

mentioning

confidence: 86%

Expression and purification of a recombinant avidin with a lowered isoelectric point in Pichia pastoris

Zocchi

Jobé

Neuhaus

et al. 2003

Protein Expression and Purification

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A recombinant glycosylated avidin (recGAvi) with an acidic isoelectric point was expressed and secreted by the methylotrophic yeast Pichia pastoris. The coding sequence for recGAvi was de novo synthesized based on the codon usage of P. pastoris. RecGAvi is secreted at approximately 330 mg/L of culture supernatant. RecGAvi monomer displays a molecular weight of 16.5 kDa, as assessed by ESI mass spectrometry. N-terminal amino acid sequencing indicates the presence of three additional amino acids (E-A-E), which contribute to further lowering the isoelectric point to 5.4. The data presented here demonstrate that the P. pastoris system is suitable for the production of recGAvi and that the recombinant avidin displays biotin-binding properties similar to those of the hen-egg white protein.

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Avidin is a heparin-binding protein. Affinity, specificity and structural analysis

Cited by 48 publications

References 28 publications

Imaging protective mast cells in living mice during severe contact hypersensitivity

Imaging protective mast cells in living mice during severe contact hypersensitivity

Islet Surface Heparinization Prevents the Instant Blood-Mediated Inflammatory Reaction in Islet Transplantation

Expression and purification of a recombinant avidin with a lowered isoelectric point in Pichia pastoris

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