Drug Database
IN

insulin (insulin, HGT / Insuman Implantable / Insuman Comb)

✓ Approved

Sanofi S.A · INSR · Recombinant Proteins

What is insulin?

insulin is a recombinant proteins developed by Sanofi S.A. It is approved for therapeutic indications via injectable (others) or intramuscular (im) injection or subcutaneous injection or surgical implantation or intraperitoneal injection.

Drug Profile

Brand Namesinsulin, HGT, Insuman Implantable, Insuman Comb
CompanySanofi S.A
Drug ClassRecombinant Proteins, Polypeptide
Molecular TargetINSR
RouteInjectable (Others), Intramuscular (IM) Injection, Subcutaneous Injection, Surgical Implantation, Intraperitoneal Injection
StatusApproved
Sources: ClinicalTrials.gov, Sanofi S.A

Mechanism of Action

Molecular Targets

insulin acts on 1 molecular target:

INSRinsulin receptor (CD220, HHF5)
Want deeper analysis?Noah AI can explain complex mechanisms and compare to similar drugs.

Therapeutic Indications

insulin is developed for 2 unique indications across 1 therapeutic area.

Therapeutic AreaConditionPhase
Metabolism and nutrition disordersType 1 diabetes mellitus✓ Approved
Metabolism and nutrition disordersType 2 diabetes mellitus✓ Approved

Related Research Articles

PubMedMicrobial cell factories2026-10-15

RNA thermometers as temperature-dependent tools for enhanced recombinant protein production in precision fermentation.

Peternell Christina C, Noll Philipp P, Henkel Marius M

Precision fermentation is a key technology for the future sustainable production of food proteins, bulk ingredients, and high-value recombinant products. However, process efficiency is often limited by the coupling of biomass formation and recombinant protein synthesis, leading to substantial carbon losses into non-recyclable biomass. Particularly for cost-sensitive bulk products such as food proteins, economically viable production requires highly efficient and dynamically controllable bioprocesses. RNA thermometers (RNATs) offer a promising inducer-free strategy for temperature-dependent control of recombinant protein production and dynamic bioprocess regulation, with the potential to improve carbon efficiency and product yields. In this study, a fluorescent reporter protein (EmGFP) under the control of a fourU (4U) RNA thermometer was evaluated in E. coli BL21 across a temperature range of 25-40 °C. Temperature-dependent regulation enabled maximal recombinant protein production at 35 °C, resulting in a 2.6-fold higher specific productivity compared to the derepressed control. The strongest RNAT-mediated regulatory effect was observed at 35.5 °C, highlighting the relevance of precise temperature control for recombinant protein production. Evaluation of altered carbon partitioning revealed a substantially increased carbon allocation toward product formation, while carbon partitioning into biomass and CO2 remained largely unchanged. Furthermore, the product-per-acetate yield increased more than threefold at induction temperature, indicating controllable carbon partitioning and reveals potential for decoupling approaches of biomass formation from recombinant protein production. This study demonstrates the successful implementation of an RNAT-controlled recombinant expression system enabling temperature-dependent regulation of protein production in E. coli. Quantitative analysis revealed controllable carbon partitioning toward recombinant protein synthesis and defined target temperatures for future process induction and switching. In contrast to conventional inducer-based systems, RNAT-mediated regulation enables dynamic control without chemical additives, supporting more resource-efficient bioprocess operation. However, fully exploiting RNAT-based process control will require advanced model-based strategies integrating temperature and feeding regimes, particularly for cost-sensitive precision fermentation processes such as food protein production. Overall, RNATs represent promising molecular control elements for future high-efficiency precision fermentation processes.

PMID 42875774
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PubMedThe Journal of pharmacy technology : jPT : official publication of the Association of Pharmacy Technicians2026-10-15

Evaluation of Chromium Picolinate Supplementation and Insulin Requirements in Critically Ill Adults With Type 2 Diabetes Mellitus.

Tomika Alvin A, Finnell Corey C, Yann Reesie R, Bui Phuoc Tyler PT

Chromium picolinate has been studied as an adjunct to improve glycemic indices in ambulatory type 2 diabetes mellitus, but its role in critically ill patients is unknown. To evaluate whether chromium picolinate supplementation was associated with reduced insulin requirements without worsening glycemic control in critically ill adults with type 2 diabetes mellitus. We conducted a single-center retrospective pre-post cohort study of adult intensive care unit patients with type 2 diabetes mellitus or hemoglobin A1c ≥6.5% who received insulin and at least 4 consecutive chromium picolinate doses between July 2022 and January 2023. Patients served as their own controls during 24-hour pre- and post-chromium periods. The primary outcome was change in total daily insulin dose. Secondary outcomes included proportion of measured glucose values within 140 to 180 mg/dL, acute kidney injury, hypoglycemia, and exploratory Sequential Organ Failure Assessment-2 change. Among 91 screened patients, 45 met the inclusion criteria. Median total daily insulin dose decreased from 76.3 U/d (interquartile range [IQR], 40.1-96.9) before chromium to 40.0 U/d (IQR, 20.5-65.6) after chromium; the Hodges-Lehmann paired difference was -23.0 U/d (95% CI, -33.25 to -14.25; P < .0001). Proportion of measured glucose values within target did not differ significantly. No post-intervention hypoglycemia was observed, and 2 patients met the study-defined acute kidney injury criterion. Interpretation is limited by the retrospective design and absence of a concurrent control group. Chromium picolinate supplementation was associated with lower insulin requirements without worsening glycemic control. These hypothesis-generating findings require confirmation in prospective controlled studies.

PMID 42876873
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PubMedFrontiers in endocrinology2026-10-15

Diabetes in Cushing's disease: age, hypercortisolism, central adiposity, and β-cell stress as determinants of glycaemia.

Witek Przemysław P, Kwiatkowski Jakub J, Witek Joanna J, Szamotulska Katarzyna K et al.

Diabetes is a frequent complication of Cushing's disease, but metabolic differences between normal glucose tolerance, prediabetes, and diabetes remain incompletely characterised. We aimed to characterise glucose metabolism across these groups, assess abnormalities in patients with normal glucose tolerance, and identify clinical, hormonal, and body-composition factors associated with glycaemia. Cross-sectional analysis of a prospective cohort with matched healthy controls. The study included 50 patients with Cushing's disease and 52 age- and sex-matched healthy controls who underwent detailed metabolic phenotyping, including multi-timepoint oral glucose tolerance testing with assessment of insulin sensitivity and β-cell compensatory function, and body composition analysis by dual-energy X-ray absorptiometry. Forward stepwise linear regression was performed separately in each group to identify variables independently associated with HbA1c. Glucose metabolism disturbances affected 68% of patients with Cushing's disease, including prediabetes in 42% and diabetes in 26%, with most diabetes cases previously undiagnosed. Even patients with normal glucose tolerance showed lower insulin sensitivity and enhanced β-cell secretory activity compared with healthy controls. Prediabetes was characterised mainly by lower insulin sensitivity with preserved β-cell compensation, whereas diabetes was associated with a reduced insulin-to-glucose AUC ratio without significantly lower insulin sensitivity than in prediabetes. In Cushing's disease, age, morning cortisol, waist-to-hip ratio, and proinsulin were independently associated with HbA1c, explaining 59.5% of its variance; in controls, only age and BMI were associated with HbA1c. BMI was not significantly correlated with HbA1c in Cushing's disease, whereas trunk fat percentage was positively associated with HbA1c. In Cushing's disease, reduced insulin sensitivity with preserved β-cell compensation is detectable even in patients with normal glucose tolerance, whereas overt diabetes is characterised by impaired β-cell compensation without significantly lower insulin sensitivity than in prediabetes. Age, morning cortisol, waist-to-hip ratio, and proinsulin are independently associated with HbA1c. Central fat distribution may be more closely related to glycaemia than BMI.

PMID 42876832
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PubMedImmunological reviews2026-10-15

Oxidative Stress, Post-Translational Modifications, and Type 1 Diabetes Pathogenesis.

Winstead Colleen J CJ, Hodel Miki M, Tse Hubert M HM

Type 1 diabetes (T1D) is an organ-specific autoimmune disease that destroys insulin-producing beta-cells. Insulin is a vital hormone for regulating glycemia that often undergoes post-translational modifications during processing from pre-proinsulin to biologically active insulin. While necessary for proper glucose homeostasis, insulin is also an autoantigen recognized by autoreactive T cells in T1D. Cellular stress pathways including endoplasmic reticulum stress and oxidative stress mediated by an increase in reactive oxygen species (ROS) synthesis and/or a concomitant decrease in antioxidant function can further drive post-translational modifications of various autoantigens in T1D including insulin. Innate immune-derived ROS generation is an essential frontline defense against microbial infections, but ROS can also function as signaling intermediates to properly stimulate T cell responses. Oxidative stress-induced post-translational modifications are thought to trigger autoreactive T cells in T1D by generating novel neoepitopes, eliciting epitope spreading, or enhancing autoantigen interactions with antigen-presenting cells. With the current technology, detecting post-translationally modified proteins is challenging. In this review, we will explore the role of ROS and other post-translational modifications involved in T1D. We will also discuss islet transplantation strategies being used for patients with T1D including novel cell sources for beta-cell replacement and management of oxidative stress after transplantation.

PMID 42876362
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PubMedPakistan journal of biological sciences : PJBS2026-10-15

Molecular Engineering of the Thioredoxin (trxA) Gene in Chryseobacterium proteolyticum Enhanced its Keratinase Bioconversion of Chicken Feathers.

Mpaka Lindelwa L, Nnolim Nonso E NE, Nwodo Uchechukwu U UU

<b>Background and Objective:</b> Keratinases are gaining traction in green technology and the bio-economy due to their ability to convert keratinous biomass into valuable products, such as animal feed. However, improving their output remains challenging. This study investigated genetic engineering approaches to increase keratinase production. <b>Materials and Methods:</b> The genome of the keratinolytic bacterium, <i>C. proteolyticum,</i> was sequenced using the Ion GeneStudio<sup>™</sup> S5 Prime System, covering 2,484,843 reads, and sequence reads generated were assembled using SPAdes 3.13.0. The quality of the reads was assessed with QUAST V4.1, and the obtained sequences were annotated with Prokka 1.14.6, which revealed that trxA is associated with keratinolytic activity. The nucleotide sequence obtained was uploaded to the NCBI database and was assigned the accession number JBJLWK000000000. The <i>trxA</i> gene was amplified with primers from NCBI Primer-BLAST, cloned into a p-GEM<sup>®</sup>-T Easy vector, and transformed into <i>E. coli</i> JM109, and expressed using IPTG and SDS-PAGE analysis. The effects of pH and temperature on enzyme production were studied, and the recombinant strain's thermostability and tolerance to commercial laundry detergents were assessed. <b>Results:</b> The gene was successfully cloned and expressed, with SDS-PAGE showing a clear band at 11 kDa, matching trxA's molecular weight. The pGEM-trxA construct demonstrated high keratinase activity across various pH and temperature conditions. Additionally, the recombinant strain showed excellent thermostability and detergent tolerance. <b>Conclusion:</b> These findings highlight the potential of recombinant technology to boost keratinase yields and support the sustainable recycling of keratinous waste.

PMID 42876176
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PubMedThe International journal of artificial organs2026-10-15

In vitro replication of relationship between α1-microglobulin reduction rate and albumin leakage in post-dilution hemodiafiltration.

Li Maozhen M, Inoue Hiroyuki H, Yamaguchi Satoru S, Sunohara Takashi T et al.

Efficient removal of middle-to-large molecules, such as α1-microglobulin (α1-MG, 33 kDa), is essential for mitigating long-term complications in patients undergoing hemodiafiltration (HDF). However, objective evaluation of diafilter performance requires standardized laboratory systems that can reproduce clinical transport characteristics while monitoring albumin leakage. This study established an in vitro experimental system utilizing recombinant α1-MG to evaluate post-dilution on-line HDF. Two configurations were compared: Circuit#1, featuring an auxiliary pump at the blood outlet, and Circuit#2, where the pump was removed to optimize flow regulation. Results demonstrated that Circuit#1 significantly deviated from clinical benchmarks due to internal pressure accumulation. Conversely, Circuit#2 successfully mirrored clinical trends, showing a strong positive correlation between α1-MG removal and albumin leakage. Observed clearances in Circuit#2 were slightly higher than clinical averages, likely due to the smaller molecular weight of the recombinant solute (31 vs. 33 kDa), reduced circulation volume, and the absence of α1 in vitro-MG-IgA dimer binding complexes. This validated model provides a robust and reliable platform for the standardized assessment and development of next-generation blood purification devices.

PMID 42876027
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