Farklı Yaşlardaki Koyunların Dil Dokusunda Bazı Isı Şok Proteinlerinin Dağılımı

Öz

Isı şok proteinleri çok sayıda hücresel ve fizyolojik süreci düzenleyen ve modüle eden moleküler şaperonlardır. Bu çalışma, koyunların gelişimi boyunca dil dokularında HSP27 ve HSP90' nın immünekspresyonunu belirlemek için tasarlandı. 6-12 aylık (G1, n:6), 1-2 yaşındaki (G2, n:6) ve 3-5 yaşındaki (G3, n:6) koyunlardan dil dokuları toplandı. Doku örnekleri rutin histolojik işlemlere tabi tutulduktan sonra immünohistokimyasal boyama yapıldı. Periferik sinirlerde, seröz Von Ebner bezlerinde ve müköz bezlerinde HSP27 ve HSP90 immünoreaktivitesi gözlenmedi. Kanal epitelinde HSP27 immünreaktivitesi görülmezken, HSP90 immünreaktivitesi tespit edildi. Epitel katmanda, iskelet kası hücreleri, damar endoteli ve damar düz kas hücrelerinde HSP27 ve HSP90 immünoreaktivitesi görüldü. Epitel katman, iskelet kası hücreleri, kanal epiteli ve kan damarlarındaki HSP90 immünreaktivitesinde koyunların gelişimi boyunca istatistiksel olarak anlamlı bir farklılık saptanmadı (p>0.05). Kan damarları ve epitel katmandaki HSP27 immünreaktivitesi gruplar arasında istatistiksel olarak değişmezken (p>0.05), iskelet kası hücrelerindeki HSP27 immünreaktivitesi G3’e kıyasla G1’ de istatiksel olarak daha yüksekti (p<0.05). Bu çalışmanın bulguları HSP27 ve HSP90' nın koyunların gelişimi boyunca dil dokularının epitel katmanından, kan damarları ve iskelet kası hücrelerinden eksprese olduğunu göstermiştir. Bu çalışma, HSP27 ve HSP90' nın koyunların dil gelişimi için gerekli olduğunu ve hücresel olaylarda kritik roller oynadığını göstermektedir.

Anahtar Kelimeler

• Dil
• HSP27
• HSP90
• ısı şok proteini
• immunohistokimya
• koyun

Distribution of Some Heat Shock Proteins in the Tongue Tissues of Sheep of Different Ages

Öz

Heat shock proteins are molecular chaperones that regulate and modulate a multitude of cellular and physiological processes. This study was designed to determine the immunoexpression of HSP27 and HSP90 in tongue tissues throughout the development of sheep. Tongue tissues were collected from sheep aged 6-12 months (G1, n:6), 1-2 years (G2, n:6), and 3-5 years (G3, n:6). Immunohistochemical staining was performed after the tissue samples were subjected to routine histological procedures. Immunoreactivity for HSP27 and HSP90 was not observed in peripheral nerves, serous Von Ebner’s glands, and mucous glands. While HSP27 immunoreactivity was not observed in the ductal epithelium, HSP90 immunoreactivity was detected. HSP27 and HSP90 immunoreactivity was seen in the epithelial layer, skeletal muscle cells, vascular endothelium, and vascular smooth muscle cells. There were no statistically significant differences in HSP90 immunoreactivity in the ductal epithelium, epithelial layer, blood vessels, and skeletal muscle cells throughout the development of the sheep (p>0.05). While HSP27 immunoreactivity in blood vessels and the epithelial layer was not statistically changed between groups (p>0.05), HSP27 immunoreactivity in skeletal muscle cells was statistically higher in G1 compared to G3 (p<0.05). The results of this study demonstrated that HSP27 and HSP90 were expressed in the luminal epithelium, blood vessels, and skeletal muscle cells of the tongue tissues throughout the development of the sheep. This study shows that HSP27 and HSP90 are essential for sheep tongue development and play critical roles in cellular events.

Anahtar Kelimeler

• Heat shock protein
• HSP27
• HSP90
• immunohistochemistry
• sheep
• tongue

Kaynakça

1. Erdoğan S, Sağsöz H (2018). Papillary architecture and functional characterization of mucosubstances in the sheep tongue. Anat Rec., 301(8): 1320-1335.
2. Iwasaki S (2002). Evolution of the structure and function of the vertebrate tongue. J Anat., 201(1): 1-13.
3. Goździewska-Harłajczuk K, Klećkowska-Nawrot J, Barszcz K et al. (2018). Biological aspects of the tongue morphology of Wild-captive WWCPS rats: a histological, histochemical and ultrastructural study. Anat Sci Int., 93(4): 514-532.
4. Tadjalli M, Pazhoomand R (2004). Tongue papillae in lambs: a scanning electron microscopic study. Small Rumin Res., 54: 157-164.
5. Tanyolaç A (1999). Özel Histoloji. Yorum Basın Yayın Sanayi Ltd. Şti. Ankara.
6. Tsan MF, Gao B (2004). Heat shock protein and innate immunity. Cell Mol Immunol., 1(4): 274-279.
7. Neuer A, Spandorfer SD, Giraldo P, Dieterle S, Rosenwaks Z, Witkin SS (2000). The role of heat shock proteins in reproduction. Hum Reprod Update., 6(2): 149-159.
8. Seoane J, Ramírez JR, Romero MA, Varela-Centelles P, Garcia-Pola MJ (2004). Expression of heat shock protein (HSP70) in oral lichen planus and non-dysplastic oral leucoplakia. Clin Otolaryngol Allied Sci., 29(2): 191-196.

9. Lu RC, Tan MS, Wang H, Xie AM, Yu JT, Tan L (2014). Heat shock protein 70 in Alzheimer’s disease. BioMed Res Int., 2014(435203): 1-8.
10. Wang X, Chen M, Zhou J, Zhang X (2014). HSP27, 70 and 90, anti-apoptotic proteins, in clinical cancer therapy. Int J Oncol., 45(1): 18-30.
11. Mohtasham N, Babakoohi S, Montaser-Kouhsari L et al. (2011). The expression of heat shock proteins 27 and 105 in squamous cell carcinoma of the tongue and relationship with clinicopathological ındex. Med Oral Patol Oral Cir Bucal., 16(6): e730-5.
12. Ferns G, Shams S, Shafi S (2006). Heat shock protein 27: Its potential role in vascular disease. Int J Exp Pathol., 87(4): 253-274.
13. Birbo B, Madu EE, Madu CO, Jain A, Lu Y (2021). Role of HSP90 in cancer. Int J Mol Sci., 22(19): 10317.
14. Tukaj S, Kleszczyński K, Vafia K et al. (2013). Aberrant expression and secretion of heat shock protein 90 in patients with bullous pemphigoid. PLoS One., 30;8(7): e70496.
15. Bayram B, Liman N, Alan E, Sağsöz H (2024). Angiogenic and anti-angiogenic factors during the post-hatching growth of the quail (Coturnix coturnix japonica) spleen. Anat Rec., 307(11): 3606-3622.
16. Tekkeşin MS, Mutlu S, Aksakallı N, Olgaç V (2011). Expression of heat shock proteins 27, 60 and 70 in oral carcinogenesis: an immunohistochemical study. Türk Onkoloji Dergisi., 26(3): 115-120.
17. Wilson N, McArdle A, Guerin D et al. (2000). Hyperthermia to normal human skin in vivo upregulates heat shock proteins 27, 60, 72i and 90. J Cutan Pathol., 27: 176-182.
18. Zheng CX, Wang ZQ, Lin WB, Chu ZH, Chen LH, Ji ZQ (2011). Expression of heat shock protein 27 in the esophageal tissue of rats with reflux esophagitis. Chin Med J., 124(15): 2347-2353.
19. Laplante AF, Moulin V, Auger FA et al. (1998). Expression of heat shock proteins in mouse skin during wound healing. J Histochem Cytochem., 46(11): 1291-1301.
20. Gandour-Edwards R, McClaren M, Isseroff RR (1994). Immunolocalization of low-molecular-weight stress protein HSP27 in normal skin and common cutaneous lesions. Am J Dermatopathol., 16: 504-509.
21. Romanucci M, Bongiovanni L, Marruchella G et al. (2005). Heat shock proteins expression in canine ıntracutaneous cornifying epithelioma and squamous cell carcinoma. Vet Dermatol., 16(2): 108-116.
22. Yang X, Cui Y, Yue J et al. (2017). The histological characteristics, age-related thickness change of skin, and expression of the hsps in the skin during hair cycle in yak (Bos grunniens). PLoS One., 12(5): e0176451.
23. Gernold M, Knauf U, Gaestel M, Stahl J, Kloetzel PM (1993). Development and tissue-specific distribution of mouse small heat shock protein HSP25. Dev Genet., 14(2): 103-111.
24. Brown DD, Christine KS, Showell C, Conlon FL (2007). Small heat shock protein HSP27 is required for proper heart tube formation. Genesis., 45(11): 667-78.
25. Wilkinson JM, Pollard I (1993). Immunohistochemical localisation of the 25 kda heat shock protein in unstressed rats: possible functional ımplications. Anat Rec., 237(4): 453-457.
26. Inaguma Y, Goto S, Shinohara H, Hasegawa K, Ohshima K, Kato K (1993). Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha b crystallin, in rat hindlimb muscles. J Biochem., 114(3): 378-384.
27. Ishihara A, Fujino H, Nagatomo F, Takeda I, Ohira Y (2008). Gene expression levels of heat shock proteins in the soleus and plantaris muscles of rats after hindlimb suspension or spaceflight. J Physiol Sci., 58(6): 413-417.
28. Golenhofen N, Perng MD, Quinlan RA, Drenckhahn D (2004). Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle. Histochem Cell Biol., 122(5): 415-425.
29. Sun H, Zhu T, Ding F, Hu N, Gu X (2009). Proteomic studies of rat tibialis anterior muscle during postnatal growth and development. Mol Cell Biochem., 332(1-2): 161-171.
30. Srikakulam R, Winkelmann DA (2004). Chaperone-mediated folding and assembly of myosin in striated muscle. J Cell Sci., 117(Pt 4): 641-652.
31. Ojima K, Ichimura E, Suzuki T, Oe M, Muroya S, Nishimura T (2018). HSP90 modulates the myosin replacement rate in myofibrils. Am J Physiol Cell Physiol., 315(1): C104-C114.
32. Smith DA, Carland CR, Guo Y, Bernstein SI (2014). Getting folded: chaperone proteins in muscle development, maintenance and disease. Anat Rec., 297: 1637-1649.
33. Bornman L, Polla BS, Gericke GS (1996). Heat-shock protein 90 and ubiquitin: developmental regulation during myogenesis. Muscle Nerve., 19(5): 574-580.
34. Basset C, Cappello F, Rappa F et al. (2020). Heat shock proteins in embryonic and adult submandibular salivary glands in healthy and tumorigenic tissues. The FASEB Journal., 34(S1): 1-1.
35. Vanmuylder N, Werry-Huet A, Rooze M, Louryan S (2002). Heat shock protein HSP86 expression during mouse embryo development, especially in the germ-line. Anat Embryol., 205(4): 301-306.
36. Takahashi-Horiuchi Y, Sugiyama K, Sakashita H, Amano O (2008). Expression of heat shock protein 27 with the transition from proliferation to differentiation of acinar precursor cell in regenerating submandibular gland of rats. Tohoku J Exp Med., 214(3): 221-230.
37. Liman N (2017). Heat shock proteins (hsp)-60, -70, -90, and 105 display variable spatial and temporal ımmunolocalization patterns in the ınvoluting rat uterus. Anim Reprod., 14(4): 1072-1086.
38. Bao E, Sultan KR, Nowak B, Hartung J (2008). Localization of heat shock proteins and histopathological changes in the kidneys of transported pigs. Livestock Science., 118(3): 231-237.