Specific binding of proinsulin C-peptide to human cell membranes.
The study demonstrated specific binding of proinsulin C-peptide to human cell membranes, indicating a high-affinity interaction that may underlie its biological effects.
Connecting peptide · Proinsulin C-peptide
C-Peptide, or connecting peptide, is a proinsulin cleavage product produced by pancreatic beta cells during insulin synthesis. Researchers primarily study C-peptide to understand its role in beta-cell function and its potential effects on diabetes-related complications. Key findings indicate that C-peptide may improve blood flow and cellular function in various tissues, while also exhibiting bioactive properties that could influence insulin signaling pathways. Additionally, clinical evidence suggests that C-peptide levels serve as a valuable marker for assessing beta-cell activity in diabetes patients. Current research continues to explore the peptide's biological activities and its implications for diabetes management and complications.
C-Peptide, also known as Connecting peptide or Proinsulin C-peptide, is an endogenous peptide produced in the pancreas as a byproduct of insulin synthesis. It is cleaved from proinsulin to form insulin and C-peptide, both of which are secreted into the bloodstream. C-Peptide belongs to the peptide class of compounds and is not typically synthesized for therapeutic use. Research has shown that C-peptide plays a significant role in insulin and glucose regulation. It is used as a marker for beta-cell function in diabetes research, as it is co-secreted with insulin and reflects endogenous insulin production. Studies have indicated that C-peptide may have biological activities that influence vascular function and nerve health, suggesting potential roles in mitigating diabetes-associated complications. The mechanism of action of C-peptide involves its interaction with cell membranes, potentially through a G-protein-coupled receptor, leading to various intracellular responses such as increased calcium concentration and activation of MAP-kinase pathways. These pathways are thought to mediate its effects on blood flow and cellular function. Pharmacokinetic properties of C-peptide include a circulating half-life of approximately 30 minutes, with metabolism primarily occurring in the kidneys. It is not typically administered as a drug, so bioavailability by various routes is not applicable. Clinically, C-peptide is not used as a therapeutic agent but is an important biomarker in diabetes management and research. It is not regulated as a drug for therapeutic use, but its measurement is standard in clinical settings to assess pancreatic function.
| Formel | C129H211N35O48 |
| Molekulargewicht | 3020.3g/mol |
| CAS-Nummer | 33017-11-7 |
| PubChem CID | 16157840 |
C-Peptide is thought to interact with cell membranes via a G-protein-coupled receptor, leading to intracellular signaling cascades such as MAP-kinase activation. This interaction results in physiological effects like increased blood flow and modulation of Na+,K(+)-ATPase activity.
C-peptide interacts with cell-surface binding sites, likely through G-protein-coupled receptors, leading to intracellular signaling that includes an increase in Ca2+ concentration and activation of MAP-kinase pathways. This signaling promotes biological processes such as enhanced blood flow, improved neuronal function, and anti-apoptotic effects in diabetic complications. Although C-peptide's precise molecular mechanism remains incompletely understood, its bioactivity suggests a role in modulating insulin signaling pathways and vascular function.
Circulating half-life ~30 minutes
C-Peptide is primarily cleared by the kidneys, and its half-life reflects its role as a biomarker rather than a therapeutic agent.
Temperature
Refrigerate at 2-8C
Light
Protect from light
Form
Aqueous solution: use within specified period after reconstitution
Notes
Storage conditions are relevant for laboratory settings where C-peptide is measured.
C-Peptide is soluble in water, which is relevant for its use in laboratory assays.
🇩🇪DE
Data limited
🇺🇸US
C-Peptide is not FDA-approved as a therapeutic agent but is used as a clinical biomarker.
🇦🇺AU
Data limited
🇬🇧UK
Data limited
Legal status information is provided for general reference only and may not reflect the most current regulatory changes. Always verify with official government sources before making any decisions.
Current evidence is limited regarding the specific molecular mechanisms through which C-peptide exerts its biological effects, particularly in relation to its potential interactions with G-protein-coupled receptors and the insulin signaling pathway. Further research is needed to clarify the dual role of C-peptide in both beneficial and detrimental contexts, especially in long-term studies assessing its impact on diabetes-associated complications across diverse populations. Additionally, larger randomized controlled trials are necessary to evaluate the therapeutic potential of C-peptide supplementation in preventing complications of diabetes, as well as to explore its effects in different demographic groups, including those with varying degrees of insulin resistance and beta-cell function.
3,236
Total Citations
21
Human/RCT
3.6
Avg. Influence
2021
Latest
The study demonstrated specific binding of proinsulin C-peptide to human cell membranes, indicating a high-affinity interaction that may underlie its biological effects.
Thomas Melissa K, et al. · The Journal of clinical endocrinology and metabolism · 2021
Researchers observed that tirzepatide significantly improved beta-cell function and insulin sensitivity in humans with type 2 diabetes, with effects only partially attributable to weight loss.
Key findings
Sims Emily K, et al. · Science translational medicine · 2021
The study demonstrated that teplizumab treatment improved beta cell function, as indicated by increased C-peptide area under the curve, and delayed the diagnosis of type 1 diabetes in high-risk individuals.
Key findings
Researchers observed that optimizing the secretory expression system in Saccharomyces cerevisiae allows for efficient secretion of folded single-chain proinsulin-like molecules, enhancing insulin production potential.
The study demonstrated that C-peptide significantly increases nitric oxide production in bovine aortic endothelial cells, suggesting a mechanism for its vasodilatory effects.
Steiner Donald F · Experimental diabesity research · 2004
The review highlighted C-peptide's multifaceted roles in insulin biosynthesis and its potential physiological activities post-release.
Key findings
Researchers observed that C-peptide is biologically active and may reverse the harmful effects of high glucose in tissues affected by diabetes, indicating its therapeutic potential.
Researchers observed that C-peptide treatment improves nerve conduction and blood flow in diabetic rats, with effects mediated by nitric oxide pathways.
Researchers observed that proinsulin C-peptide activates multiple signaling pathways, enhancing glucose disposal and ameliorating diabetic complications in type 1 diabetic patients.
The study demonstrated that proinsulin C-peptide plays a crucial role in the biosynthesis and secretion of insulin and may have broader implications for other secretory systems.
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