Fst 344 Buy
Follistatin (FST), which was first found in the follicles of cattle and pigs, has been shown to be an essential regulator for muscle development. Mice that were genetically engineered to overexpress Fst specifically in muscle had at least twice the amount of skeletal muscle mass as controls; these findings are similar to earlier results obtained in myostatin-knockout mice. However, the role of follistatin in skeletal muscle development has yet to be clarified in livestock. Here, we describe transgenic Duroc pigs that exogenously express Fst specifically in muscle tissue. The transgenic pigs exhibited an increased proportion of skeletal muscle and a reduced proportion of body fat that were similar to those reported in myostatin-null cattle. The lean percentage of lean meat was significantly higher in the F1 generation of TG pigs (72.95 1.0 %) than in WT pigs (69.18 0.97 %) (N = 16, P
fst 344 buy
We thank Qiuyan Li for technical assistance. This work was supported by funding from the National Basic Research Program of China (2015CB943103), National Transgenic Breeding Program (2014ZX08006 and 2013ZX08006-002) and National Scientific Foundation of China (81370840).
Rui Fang conceived and designed the experiments; Fei Chang, Meng Wang, Xin Zhao, Rui Fang and Wen Chang performed the experimental work; Zaihu Zhang managed the breeding and feeding of transgenic pigs; Rui Fang, Fei Chang, Meng Wang, Ning Li and Qingyong Meng wrote the manuscript.
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Follistatin (FST) is a secreted glycoprotein that was first identified as a follicle-stimulating hormone inhibiting substance in ovarian follicular fluid (1, 2). Human Follistatin cDNA encodes a 344 amino acid (aa) protein with a 29 aa signal sequence, an N-terminal atypical TGF binding domain, three Follistatin domains that contain EGF-like and kazal-like motifs, and a highly acidic C-terminal tail. The first Follistatin domain (FS1) contains a heparin binding site, while FS1 and FS2 are most critical for activin binding and neutralization (3, 4). In addition to activin, Follistatin regulates bioavailability of many non-TGF-beta members of the TGF-beta superfamily, such as BMP6, BMP7 and myostatin (5). It also regulates hematopoietic stem cell adhesion to fibronectin via FS2, and binds angiogenin via FS2 and FS3 (6, 7). Some Follistatin binding partners will also bind Follistatin-like proteins such as FSL-3 (3, 5, 6). Of three Follistatin isoforms, the full-length mature Follistatin (FST315) is the most abundant and the sole form in plasma, but has lower binding affinity for both activins and heparins than alternative isoforms (5, 8, 9). The acidic tail is missing in the splice variant FST288 which shows the highest affinity for activins, while a partial tail exists in the proteolytically produced FST303, which shows intermediate activin affinity (5, 8, 9). FST315 shares 98% aa identity with mouse, rat, equine and ovine FST, 99% with porcine and 97% with bovine FST. Genetic deletion of Follistatin in mice, or expression of only the FST288 form, is perinatally lethal due to defects of lung, skin and musculoskeletal system (10). Expression of only the FST315 isoform allows survival, with defects in vascularization and female fertility (10).
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Follistatin also known as activin-binding protein is a protein that in humans is encoded by the FST gene.[5][6] Follistatin is an autocrine glycoprotein that is expressed in nearly all tissues of higher animals.[6]
An earlier name for the same protein was FSH-suppressing protein (FSP). At the time of its initial isolation from follicular fluid, it was found to inhibit the anterior pituitary's secretion of follicle-stimulating hormone (FSH).
Currently there are three reported isoforms, FS-288, FS-300, and FS-315. Two, FS-288 and FS-315, are known to be created by alternative splicing of the primary mRNA transcript. FS-300 (porcine follistatin) is thought to be the product of posttranslational modification via truncation of the C-terminal domain from the primary amino-acid chain.
The activin-binding protein follistatin is produced by folliculostellate (FS) cells of the anterior pituitary. FS cells make numerous contacts with the classical endocrine cells of the anterior pituitary including gonadotrophs.
In the tissues activin has a strong role in cellular proliferation, thereby making follistatin the safeguard against uncontrolled cellular proliferation and also allowing it to function as an instrument of cellular differentiation. Both of these roles are vital in tissue rebuilding and repair, and may account for follistatin's high presence in the skin.
In the blood, activin and follistatin are both known to be involved in the inflammatory response following tissue injury or pathogenic incursion. The source of follistatin in circulating blood plasma has yet to be determined, but due to its autocrine nature speculation suggests the endothelial cells lining all blood vessels, or the macrophages and monocytes also circulating within the whole blood, may be sources.
Follistatin is involved in the development of the embryo. It has inhibitory action on bone morphogenic proteins (BMPs); BMPs induce the ectoderm to become epidermal ectoderm. Inhibition of BMPs allows neuroectoderm to arise from ectoderm, a process which eventually forms the neural plate. Other inhibitors involved in this process are noggin and chordin.
Follistatin and BMPs are also known to play a role in folliculogenesis within the ovary. The main role of follistatin in the oestrus/menstrus ovary, so far, appears to be progression of the follicle from early antral to antral/dominant, and importantly the promotion of cellular differentiation of the estrogen producing granulosa cells (GC) of the dominant follicle into the progesterone producing large lutein cells (LLC) of the corpus luteum.
Follistatin is being studied for its role in regulation of muscle growth in mice, as an antagonist to myostatin (also known as GDF-8, a TGF superfamily member) which inhibits excessive muscle growth. Lee & McPherron demonstrated that inhibition of GDF-8, either by genetic elimination (knockout mice) or by increasing the amount of follistatin, resulted in greatly increased muscle mass.[7][8] In 2009, research with macaque monkeys demonstrated that regulating follistatin via gene therapy also resulted in muscle growth and increases in strength. This research paves the way for human clinical trials, which are hoped to begin in the summer of 2010 on Inclusion body myositis.[9]
A study has also shown that increased levels of follistatin, by leading to increased muscle mass of certain core muscular groups, can increase life expectancy in cases of spinal muscular atrophy (SMA) in animal models.[10] There is increased risk of type 2 diabetes with increased level of circulating follistatin.[11][unreliable medical source]
Follistatin-344 and Breast Cancer A clinical study in breast cancer patients used immune-histochemistry and Reverse Transcription Polymerase Chain Reaction (RT-PCR). The study reported under-expression of Follistatin-344 in the majority of participants, while over-expression was only found in a small number of patients[3]. The over-expression of Follistatin was associated with a better prognosis, as per the studies for ABC monomer. It appeared to prevent metastasis of the tumor, but did increase its growth. Contrastingly, under-expression of Follistatin-344 appeared to lead to higher incidences of metastasis. A study done on a mouse model of HER-2 positive breast cancer suggested that Follistatin-344 may prevent activin-induced migration of epithelial cells in breast tissue. This potential of Follistatin may prevent metastasis without increasing the growth of the tumor mass. A study done on cases involving benign proliferative diseases of the breast indicated over-expression of Follistatin. This result supports the anti-metastatic potential of Follistatin.
Dr. Usman (BSc, MBBS, MaRCP) completed his studies in medicine at the Royal College of Physicians, London. He is an avid researcher with more than 30 publications in internationally recognized peer-reviewed journals. Dr. Usman has worked as a researcher and a medical consultant for reputable pharmaceutical companies such as Johnson & Johnson and Sanofi.
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The activin-binding protein Follistatin is an autocrine glyco-protein produced by folliculostellate (FS) cells of the anterior pituitary and it is part of the inhibin-activin-follistatin axis. Follistatin is expressed in nearly all tissues of higher animals, and its main function is the binding and bioneutralization of members of the TGF-β superfamily, incl. GDF-8 (Growth Differentiation factor 8; called also often Myostatin), and with a particular effect on activin, a paracrine hormone. Isoform Follistatin-344 is able preferentially suppress the effects of Myostatin and is its potent inhibitor. 041b061a72