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Functional profiles of growth-related genes during embryogenesis and postnatal development of chicken and mouse skeletal muscle

Başlık çevirisi mevcut değil.

  1. Tez No: 400425
  2. Yazar: HAKAN KOCAMIŞ
  3. Danışmanlar: DR. JOHN KILLEFER
  4. Tez Türü: Doktora
  5. Konular: Veteriner Hekimliği, Veterinary Medicine
  6. Anahtar Kelimeler: Belirtilmemiş.
  7. Yıl: 2001
  8. Dil: İngilizce
  9. Üniversite: West Vırgınıa Unıversıty
  10. Enstitü: Yurtdışı Enstitü
  11. Ana Bilim Dalı: Veteriner Hekimliği Tarihi ve Deontoloji Ana Bilim Dalı
  12. Bilim Dalı: Belirtilmemiş.
  13. Sayfa Sayısı: Belirtilmemiş.

Özet

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Özet (Çeviri)

Myostatin (also known as growth differentiation factor/8), a recently identifiedmember of the TGF-ß family, has been shown to negatively regulate skeletal musclegrowth. Activins, also members of the TGF-ß family, and their binding protein,follistatin, once thought to be restricted to reproductive cycle function are in fact involvedin the development of a wide variety of embryological and adult tissues, particularlyskeletal muscles. Reverse-transcription ploymerase chain reaction (RT-PCR) wasperformed to measure the ontogeny of myostatin, activin-B, and follistatin geneexpression during chicken embryonic development. Strong myostatin expression wasfound in the early chicken embryos (E 0, E 1) and the developmental expression patternof myostatin mRNA coincided with the periods of primary and secondary muscle fiberformation. Follistatin transcripts followed a linear expression pattern from E 0 to E 20,while activin-B had a quadratic pattern.The ontogeny of myostatin gene expression was nearly identical in satellite cellsisolated from pectoralis major (PM) and biceps femoris (BF) muscles of chicken.Activin-B mRNA level in PM satellite cells was higher than in BF satellite cells at 72 hand 120 h (P < 0.01), whereas levels in BF satellite cells were higher than in PM satellitecells at 96 h and 144 h (P < 0.01). Amounts of follistatin mRNA in PM satellite cellswere higher than in BF satellite cells at 24, 96, and 120 h of culture (P < 0.01). No IGF-Igene expression was detected in either cell culture at any time point in the present study.IGF-II mRNA level plateaued in PM satellite cells by 48 h after plating (P < 0.05), andremained elevated until 144 h of culture. In ovo administration of rhIGF-I at E 3 alteredmyostatin, follistatin, activin-B, and TGF-ß2 gene expressions during chicken embryonicdevelopment with emphasis on skeletal muscle development. Myostatin mRNA frompectoralis muscles of rhIGF-I injected embryos increased on E 10 (~ 2.5 fold) andremained high through E 13, whereas mRNA from control pectoralis muscles increasedat E 9 and remained high until E 12.IGF-I, -II and IGF receptor-I mRNA and protein levels were determined in a widevariety of myostatin knockout mice tissues. IGF-I mRNA levels were not differentbetween control and knockout mice tissues, whereas levels for IGF-II were significantlyhigher in myostatin knockout mice kidney and soleus muscles than that of control mice(P < 0.01). IGF-Receptor-1 mRNA levels from control mice heart (P < 0.05) and kidney(P < 0.01) were significantly higher than that of myostatin knockout mice, while levelswere lower in control mice pectoralis muscle than that of knockout mice (P < 0.01). Thestrongly IGF-II positive cells were more common in myostatin knockout mice and wereseen in a few foci in control mice, while no consistent differences in IGF-IIimmunoreactivity were detected between the two groups of mice kidneys.

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