Examination of insulin injection sites: an unexpected finding of localized amyloidosis

Swift, Benjamin; Hawkins, P. N.; Richards, C. J.; Gregory, Rob

doi:10.1046/j.1464-5491.2002.07581.x

Cited by 97 publications

(59 citation statements)

References 3 publications

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“…So far ~35 different proteins are known to be associated with the onset of many neurodegenerative diseases (Greenwald and Riek 2010;Chiti and Dobson 2006). The process of protein aggregation is also a matter of much concern for the storage of protein therapeutic agents (Swift 2002). One of the straightforward approaches to target amyloid-linked diseases and its associated medical complication is to find potential inhibitors against the onset of amyloid aggregation of proteins.…”

Section: Introductionmentioning

confidence: 99%

Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin

et al. 2015

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Here, we have strategically synthesized stable gold (AuNPs(Tyr), AuNPs(Trp)) and silver (AgNPs(Tyr)) nanoparticles which are surface functionalized with either tyrosine or tryptophan residues and have examined their potential to inhibit amyloid aggregation of insulin. Inhibition of both spontaneous and seed-induced aggregation of insulin was observed in the presence of AuNPs(Tyr), AgNPs(Tyr), and AuNPs(Trp) nanoparticles. These nanoparticles also triggered the disassembly of insulin amyloid fibrils. Surface functionalization of amino acids appears to be important for the inhibition effect since isolated tryptophan and tyrosine molecules did not prevent insulin aggregation. Bioinformatics analysis predicts involvement of tyrosine in H-bonding interactions mediated by its C=O, -NH2, and aromatic moiety. These results offer significant opportunities for developing nanoparticle-based therapeutics against diseases related to protein aggregation.

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Section: Introductionmentioning

confidence: 99%

Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin

et al. 2015

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“…It has been shown that local amyloid deposition very infrequently takes place at the site of repeated insulin injection in patients with insulin requiring diabetes (4,5). The amyloid at the injected site was identified as amyloid insulin type (A-Ins) (1,2).…”

Section: Amyloidosis Is a Systemic Or Local Disease In Which Amyloid mentioning

confidence: 99%

“…To date, there are only 3 case reports in the English language literature on localized amyloidosis caused by repeated insulin injection in diabetic patients (4,6). The nature of amyloid in the insulin injection site is considered to be insulin itself (4,5) or insulin-related substance (6) i n a n d u s e o f i n s u l i n i n t h e p a t i e n t . (Fig.…”

Section: Amyloidosis Is a Systemic Or Local Disease In Which Amyloid mentioning

confidence: 99%

Localized Amyloidosis at the Site of Repeated Insulin Injection in a Diabetic Patient

et al. 2010

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“…3 However, other types of skin alterations (e.g., nodular changes) have also been reported with unclear impact on insulin absorption. 4,5 Patients prefer to inject in such skin areas, as they are anesthetic, i.e., injection induces no pain.…”

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confidence: 99%

Insulin Absorption from Lipodystrophic Areas: A (Neglected) Source of Trouble for Insulin Therapy?

Heinemann

2010

J Diabetes Sci Technol

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Abbreviations: (CSII) continuous subcutaneous insulin infusion, (SC) subcutaneousKeywords: diabetes-related complications, insulin absorption, insulin action, insulin pharmacokinetics, insulin therapy, lipodystrophy AbstractThe experienced clinical diabetologist first checks the skin at the area where the patient usually injects his insulin when he sees widely fluctuating blood glucose levels in the diary of the patient. He knows that insulin absorption from skin with lipodystrophic changes is irregular. However, our scientific knowledge about why this is the case is very limited. Most probably, the number of blood vessels near the insulin depot in the subcutaneous tissue varies depending on the nature of the lipodystrophic changes, or the structural changes in this tissue hamper the diffusion of insulin. Not only is our knowledge about the number of patients who exhibit such changes very limited, but also our understanding why such changes show up in certain patients and not in others is minimal. More practically important, we also have few quantitative studies investigating the impact of this diabetes-related complication on insulin absorption/insulin action; however, it is not difficult to run such studies in practice. Nevertheless, it is impressive to see how often metabolic control improves considerably once the patients apply the insulin into other skin areas.

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Examination of insulin injection sites: an unexpected finding of localized amyloidosis

Cited by 97 publications

References 3 publications

Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin

Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin

Localized Amyloidosis at the Site of Repeated Insulin Injection in a Diabetic Patient

Insulin Absorption from Lipodystrophic Areas: A (Neglected) Source of Trouble for Insulin Therapy?

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