Сравнение
Follistatin (FST) vs. MGF (Mechano Growth Factor)
Два пептида рядом — идентичность, доказательная база, правовой статус и известные нежелательные явления.
Идентичность
Категория
Рост
Рост
Номер CAS
122956-17-2
12-Aminosäuren-C-terminales E-Domänen-Peptid (Sequenz nicht standardisiert)
Молекулярная масса
35000 g/mol
2867.2 g/mol
Период полувыведения
нет данных
0.1 h
Последовательность
Glykoprotein, ~315 Aminosäuren in der zirkulierenden Hauptform (Sequenz isoformabhängig, kein einheitliches kurzes Peptid)YQPPSTNKNTKSQRRKGSTFEERKМеханизм действия
Follistatin (FST)
Follistatin binds with high affinity to activin and to myostatin (GDF-8), as well as related TGF-β ligands such as GDF-11 and some BMPs, preventing their binding to the activin type-II receptors. Myostatin is a negative regulator of skeletal muscle mass; by sequestering myostatin, its growth-inhibiting signalling is removed (de-repression). Because follistatin additionally neutralises activin, it acts on several muscle-inhibiting pathways at once — in animal models this produced greater muscle gain than knocking out myostatin alone. Several isoforms exist (including FST-288 and FST-315) that differ in tissue binding via heparan sulfate. The FST344 variant used in gene therapy was chosen to reduce binding to off-target structures.
MGF (Mechano Growth Factor)
The IGF-1 gene produces multiple isoforms by alternative splicing. IGF-1Ec is upregulated after mechanical muscle loading; the C-terminal E-domain is cleaved from the mature IGF-1 protein and appears to have independent effects on satellite cells. The exact receptor binding of the E-domain is not established; a classical IGF-1R effect is unlikely since mature IGF-1 is responsible. In cell-culture studies, stimulation of myoblast proliferation and differentiation has been observed.
Доказательная база
Наивысшая доказательность
Исследование на людях
Модель на животных
Исследования
4
4
из них на людях
1
0
Зафиксированные эффекты
4
3
Открытые противоречия
1
1
Задокументированные нежелательные явления
1
1
Правовой статус
Полные записи
Frequently asked questions
- What is the difference between Follistatin (FST) and MGF (Mechano Growth Factor)?
- Follistatin (FST) is classified as "Рост", while MGF (Mechano Growth Factor) is classified as "Рост". Follistatin (FST): Follistatin is an endogenous glycosylated binding protein (~35 kDa, considerably larger than typical peptides) that binds and neutralises members of the TGF-β superfamily, including activin and myostatin (GDF-8). In animal models, raising follistatin de-represses muscle growth. Clinically it has been studied mainly via AAV gene therapy (FS344) in muscular dystrophies. Follistatin is not an approved drug; human efficacy and safety data are limited and stem mostly from early gene-therapy trials and preclinical research. A 'follistatin-344' product is sold on the grey market, the identity and purity of which cannot be verified without analytics. MGF (Mechano Growth Factor): Synthetic peptide corresponding to the C-terminal E-domain of the IGF-1 splice variant IGF-1Ec. Described in preclinical studies as a 'mechano-induced' skeletal muscle repair factor. No marketing approval; clinical use largely confined to the black market. This page contrasts both neutrally and source-based — with no usage or dosing recommendation.
- Which peptide is better supported by science, Follistatin (FST) or MGF (Mechano Growth Factor)?
- The highest available evidence level is "Исследование на людях" for Follistatin (FST) and "Модель на животных" for MGF (Mechano Growth Factor). A higher evidence level means more robust data, but says nothing about suitability for an individual. The full body of evidence is on each peptide's own page.
- What is the legal status of Follistatin (FST) and MGF (Mechano Growth Factor) in Germany and the United States?
- Германия: Follistatin (FST) — Не одобрено, MGF (Mechano Growth Factor) — Не одобрено. США: Follistatin (FST) — Не одобрено, MGF (Mechano Growth Factor) — Не одобрено. These are factual summaries with source and review date on the individual pages.