دماي بالا يكي از فاكتورهاي اصلي محيطي مؤثر بر كاهش سود اقتصادي واحدهاي پرورش طيور است، زيرا رشد و توليد پرنده را مختل ميكند. پروتئينهاي شوك گرمايي (HSPs) نقش كليدي در مكانيسم دفاعي سلولي عليه گرماي محيط دارند. هدف از انجام مطالعه حاضر، بررسي ميزان بيان ژنهاي HSPA2 و HSPB1 در كبد مرغان بومي خراسان تحت تنش گرمايي حاد بود. براي اين هدف، تعداد 16 قطعه جوجه در سن 42 روزگي به دو گروه شاهد (دماي C 25 و رطوبت %50) و تيماري (دماي 40 و C 42 و رطوبت %50 به مدت 24 ساعت) تقسيم شده و پس از كشتار از كبد آنها نمونهبرداري به عمل آمد. سپس ميزان بيان ژنهاي HSPA2 و HSPB1 با روش RT-qPCR مورد ارزيابي قرار گرفت. بيان ژن HSPA2 نسبت به گروه شاهد افزايش معنيداري داشت (05/0
چكيده لاتين :
Heat stress is one of the main environmental factors causing economic losses to the poultry
industry, as it reduces growth and production performance of chickens. The heat shock proteins
(HSPs) involved in the key cellular defense mechanisms during exposure in hot environmental
conditions. Elevated level of expression of HSPs helps to overcome the stress caused by high
temperatures. The aim of this study was to evaluate the expression level of HSPA2 and HSPB1
transcripts in the liver of Khorasan native chickens under acute heat stress. Sixteen 42days old
chickens were divided into two groups of control (25 C and 50% humidity) and heat treated (40
and 42 C, 50% humidity for 24h), and then the liver was sampled after killing. The
transcription level of HSPA2 and HSPB1 was evaluated using RT-qPCR method. The HSPA2
expression was significantly induced (P0.05). However, the expression of HSPB1 did not show
any change. The analysis of protein-protein interaction revealed that HSPA2 and HSPB1 had no
interaction, however, four pathways in gene ontology including Protein processing in
endoplasmic reticulum, Progesterone-mediated oocyte maturation, MAPK signaling pathway
and VEGF signaling pathway had the highest significancy. The results indicated that Khorasan
native chickens have suitable genetic reaction to acute heat stress and HSPA2 has the ability to
express under high ambient temperature to protect the structure of cellular proteins.