A practical reference on 细胞因子: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
Reviewed 2026-03-04. Anything still debated is marked as such rather than presented as settled.
Early work on thymic extracts in the 1960s described a heat-stable acidic fraction containing many polypeptides. Separation of that mixture yielded individual components, and thymosin alpha-1 was named as one of them on the basis of assays for T-cell activity. The first preparations came from calf thymus, while subsequent research and clinical material has been chemically synthesized. Nomenclature in older papers is inconsistent, and the same peptide sometimes appears under different designations, which complicates literature searches.
Most published studies on thymosin alpha-1 report changes in immune measurements rather than clinical outcomes, and findings differ across designs and populations. Whether the peptide signals through one defined receptor or through several less specific interactions remains an open question. Its reported circulation half-life of a few hours complicates comparison of dosing schedules across trials. Mechanistic claims are frequently drawn from isolated cell cultures, and how far those results extend to whole organisms is unresolved.
Thymosin alpha-1 is a synthetic peptide of 28 amino acids whose sequence matches the amino-terminal region of prothymosin alpha. The chain is acetylated at its first residue and contains one disulfide bridge between two cysteine residues, which folds the molecule into a compact loop. Its molecular formula, C129H215N33O55, corresponds to a monoisotopic mass of roughly 3,106 daltons. Material used in laboratories is made by solid-phase synthesis rather than isolated from animal tissue.
The peptide occurs naturally in thymic tissue and has been detected in serum and other biological fluids. Reported concentrations are low, and reliable measurement generally requires immunoassay or mass spectrometry with an enrichment step. It is released from a larger precursor, prothymosin alpha, by proteolytic cleavage, although the enzymes involved are not fully characterized. Whether circulating levels reflect thymic output specifically remains an open question.
Thymosin alpha 1 is a 28-amino-acid peptide first isolated from thymosin fraction 5, a bovine thymic extract. Its sequence begins with an acetylated serine residue and carries a high proportion of acidic residues, so the molecule has a net negative charge near neutral pH. Despite the shared name, it is unrelated in sequence to the thymosin beta family. Synthetic material prepared by solid-phase peptide synthesis is identical in sequence to the natural peptide.
| Property | Value | Notes |
|---|---|---|
| Class | Synthetic peptide | 28 residues; not a small-molecule compound |
| Molecular mass | About 3,106 Da | Monoisotopic mass of the unmodified chain |
| N-terminal group | Acetylated serine | Present in both native and synthetic forms |
| Secondary structure | Disulfide-constrained loop | One bridge between two cysteine residues |
| Typical source | Solid-phase synthesis | Early isolates came from bovine thymus extracts |
Biologically, the peptide is studied mainly in the context of immune cell development and regulation. It is produced in the thymus and in several other tissues, and it appears to influence the maturation and activity of T cells and other immune populations. Laboratory work describes effects on cytokine production, on the balance between T cell subsets, and on the function of dendritic cells. Much of this evidence comes from cell culture and animal models, so the extent to which the same pathways operate in humans remains an open question.
Clinical interest has centered on chronic viral hepatitis, on immune restoration in various conditions, and on use as an adjuvant intended to improve responses to vaccines. Trials have reported mixed results, and regulatory status differs sharply between countries; in some places it is a prescription product, while elsewhere it is sold without an approved therapeutic indication. Because published studies vary widely in design, population, and endpoints, comparisons across them are difficult and no single conclusion covers the whole literature.
Several factors accelerate degradation: alkaline pH, elevated temperature, exposure to oxidants, and the presence of residual moisture. Deamidation of asparagine residues and oxidation of methionine are the most commonly reported degradation routes. Because the peptide lacks disulfide bonds, it does not undergo the thiol-related aggregation seen in some other biologics, but physical aggregation can still occur at high concentration. Stability data are product-specific, and extrapolating shelf life between formulations is not reliable.
Lyophilized thymosin alpha-1 is generally stored at or below minus twenty degrees Celsius, protected from moisture and light. Short-term handling at ambient temperature is possible for dry powder, but reconstituted solutions degrade faster and are usually kept at two to eight degrees Celsius with a defined expiry of days rather than weeks. Repeated freeze-thaw cycles should be avoided because they promote aggregation and loss of potency. Exact limits depend on the formulation and should follow the supplier's documentation.
Stability depends on temperature, pH, and the number of freeze-thaw events the sample has experienced. Freeze-dried material is commonly held at -20 °C or colder, while reconstituted liquid is kept cold and used within a short window. Extreme pH and prolonged light exposure can promote deamidation, oxidation, or aggregation, particularly at asparagine and methionine positions. Adsorption to container walls can lower the measured concentration of a dilute solution even when the peptide molecules themselves remain intact.
Identity and purity are usually assessed by reversed-phase high-performance liquid chromatography, which separates the target peptide from truncated or chemically modified byproducts. Mass spectrometry confirms the expected molecular mass and can indicate acetylation state or sequence errors. Amino acid analysis and peptide mapping supply complementary sequence-level information, while endotoxin testing is relevant for preparations intended for cell or animal work. Purity figures reported by suppliers refer to the method used and are not directly comparable across laboratories unless conditions are stated.
胸腺素α1对免疫系统的影响涉及多种细胞类型。研究表明，它可促进未成熟T细胞向成熟T细胞分化，并增强T细胞对抗原刺激的增殖反应。树突状细胞在Tα1存在下表达更高水平的共刺激分子，从而更有效地呈递抗原。此外，自然杀伤细胞的活性也观察到上升。这些效应并非直接杀伤病原体，而是调节宿主免疫应答的强度与方向。
在信号层面，Tα1可能通过Toll样受体等模式识别受体发挥作用。部分实验显示，它能激活髓样分化因子88依赖的通路，进而促进核因子κB进入细胞核。这导致白细胞介素2、干扰素γ和白细胞介素12等细胞因子的转录增加。这些细胞因子偏向辅助性T细胞1型应答，有助于细胞免疫。然而，具体受体和结合位点尚未完全确定，不同实验模型的结果存在差异。
=== Therapy === Intravenous magnesium is recommended by the ACC/AHA/ESC 2006 Guidelines for Management of Patients With Ventricular Arrhythmias and the Prevention of Sudden Cardiac Death for patients with ventricular arrhythmia associated with torsades de pointes who present with long QT syndrome; and for the treatment of patients with digoxin-induced arrhythmias. Intravenous magnesium sulfate is used for the management of pre-eclampsia and eclampsia. Hypomagnesemia, including that caused by alcoholism, is reversible by oral or parenteral magnesium administration depending on the degree of deficiency. There is limited evidence that magnesium supplementation may play a role in the prevention and treatment of migraine.
=== United States === 177Lu-DOTATATE (international nonproprietary name: lutetium (177Lu) oxodotreotide) was approved by the FDA in early 2018, for treatment of gastroenteropancreatic neuroendocrine tumors (GEP-NETs).
A variety of esters of nandrolone have been marketed and used medically. The most commonly used esters are nandrolone decanoate and to a lesser extent nandrolone phenylpropionate. Examples of other nandrolone esters that have been marketed and used medically include nandrolone cyclohexylpropionate, nandrolone cypionate, nandrolone hexyloxyphenylpropionate, nandrolone laurate, nandrolone sulfate, and nandrolone undecanoate.
Internalizing RGD (iRGD) peptides are a class of 9-amino acid cyclic peptides containing an RGD sequence, which undergo internalization as discussed below. The prototypic iRGD peptide, shown in the image on the right (sequence: CRGDKGPDC; CAS 1392278-76-0), was originally identified in an in vivo screening of phage display libraries in tumor-bearing mice. The peptide was able to home to tumor tissues, but in contrast to standard RGD (arginylglycylaspartic acid) peptides, spread much more extensively into extravascular tumor tissue. It was later identified that this extravasation and transport through extravascular tumor tissue is due to the bifunctional action of the molecule: after the initial RGD-mediated tumor homing, another pharmacologic motif is able to manipulate tumor microenvironment, making it temporarily accessible to circulating drugs. This second step is mediated through specific secondary binding to neuropilin-1 receptor, and subsequent activation of a trans-tissue pathway, dubbed the C-end Rule, or CendR pathway.
heat-shock protein (HSP) Any of a highly conserved family of proteins found in virtually all living organisms and expressed in response to a diverse variety of environmental stressors, including extreme heat or cold, ultraviolet radiation, and oxidative damage. These proteins primarily serve as molecular chaperones, stabilizing other proteins in order to ensure proper folding or to help refold those that have been damaged by the stress. Transcription of many HSP genes is dramatically upregulated as part of the heat shock response pathway.
Sources: en.wikipedia.org
The earliest known reference to morphine can be traced back to Theophrastus in the 3rd century BC, however, possible references to morphine may go as far back as 2100 BC as Sumerian clay tablets which records lists of medical prescriptions including opium-based cures. An opium-based elixir has been ascribed to alchemists of Byzantine times, but the specific formula was lost during the Ottoman conquest of Constantinople (Istanbul). Around 1522, Paracelsus made reference to an opium-based elixir that he called laudanum from the Latin word laudāre, meaning "to praise". He described it as a potent painkiller but recommended that it be used sparingly. The recipe given differs substantially from that of modern-day laudanum. Morphine was discovered as the first active alkaloid extracted from the opium poppy plant in December 1804 in Paderborn by German pharmacist Friedrich Sertürner. Sertürner noticed the compound induced drowsiness in rats and stray dogs and he reported his findings in 1805. In 1817, Sertürner reported experiments in which he administered morphine to himself, three young boys, three dogs, and a mouse; all four people almost died. Sertürner originally named the substance morphium after the Greek god of dreams, Morpheus, as it has a tendency to cause sleep. Sertürner's morphium was six times stronger than opium. He hypothesized that, because lower doses of the drug were needed, it would be less addictive.
Early in the 20th century, Dentistry shifted from treatment based therapy to prevention and as such, dentures that were in line with good health became more favourable. Having a clear occupation for dentures alone became a requirement.
== Legal status == Due to the relative ease of synthetic modification of oripavine to produce other narcotics (by either direct or indirect routes via thebaine), the World Health Organization's Expert Committee on Drug Dependence recommended in 2003 that oripavine be controlled under Schedule I of the 1961 Single Convention on Narcotic Drugs. On March 14, 2007, the United Nations Commission on Narcotic Drugs formally decided to accept these recommendations, and placed oripavine in the Schedule I. Until recently, oripavine was a Schedule II drug in the United States by default as a thebaine derivative, although it was not explicitly listed. However, as a member state under the 1961 Single Convention on Narcotic Drugs, the US was obliged to specifically control the substance under the Controlled Substances Act following its international control by the UN Commission on Narcotic Drugs. On September 24, 2007, the Drug Enforcement Administration formally added oripavine to Schedule II. Under the Controlled Substances Act 1970, oripavine has an ACSCN of 9330 and a 2013 manufacturing quota of 22,750 kg (50,160 lb).
== Medical uses == Selenium disulfide is sold as an antifungal agent in shampoos (such as Selsun Blue) for the treatment of dandruff and seborrheic dermatitis associated in the scalp with fungi of genus Malassezia. It is also used on the body to treat tinea versicolor (pityriasis versicolor), a type of fungal skin infection caused by a different species of Malassezia. A 2015 systematic review of topical treatments for seborrheic dermatitis of the scalp identified only a single randomized controlled trial evaluating selenium disulfide for the condition. It was a three-arm trial of 246 people with moderate to severe dandruff and compared treatment with 2% ketoconazole shampoo (n=97), 2.5% selenium disulfide shampoo (n=100), and placebo (shampoo base with no antiseborrheic agent) (n=49) for 29 days. The study found a 73% reduction in dandruff score with ketoconazole, a 67% reduction with selenium disulfide, and a 45% reduction with placebo. Based on the study, the systematic review concluded that selenium disulfide may be effective in the treatment of dandruff but that the available evidence is limited and overall evidence quality is low. It also found that while selenium disulfide has infrequent side effects, it seems to have more side effects than ketoconazole shampoo. Consequently, the review concluded that selenium disulfide should not be considered as a first-line therapy but instead should be used as an alternative treatment after other therapies like ketoconazole shampoo have proven not effective.
Sources: en.wikipedia.org
Its sequence corresponds to the amino-terminal portion of prothymosin alpha, a larger protein present in many cell types. The isolated 28-residue peptide is a fragment of that protein rather than a separately encoded molecule, and laboratory material is produced by synthesis.
The single bridge between two cysteine residues holds the chain in a folded loop that influences its shape and its behavior in solution. Loss of the bridge through reduction or oxidation shifts chromatographic retention and is tracked during stability work.
It is a defined 28-residue sequence derived from a larger precursor, whereas many other thymic preparations are mixtures of several polypeptides. Its acetylated amino terminus and single disulfide bridge distinguish it chemically from unrelated thymic extracts.
It is a 28-amino-acid peptide originally purified from a bovine thymic extract and later produced synthetically. It is studied mainly for its effects on immune cell function.