BibTex RIS Kaynak Göster

Localizations of α-SMA, S-100 Protein and Their Subunits in the Lacrimal Glands of the Rats

Yıl 2016, Cilt: 42 Sayı: 2, 161 - 170, 04.07.2016
https://doi.org/10.16988/iuvfd.2016.94909

Öz

This study is intended to reveal immunohistochemical localizations of α-SMA and calcium binding wbS-100, S-100α and S-100β proteins in intraorbital and extraorbital lacrimal gland of adult male rats. After extraorbital and intraorbital sections of the lacrimal gland were extracted from the rats under anesthesia, Streptavidin-biotin-peroxidase immunohistochemical technique to determine wbS-100, S-100α, S-100β and α-SMA proteins were applied to the 4-μm sections taken from the tissue samples blocked following the routine histological procedure. Immunoreaction of wbS-100, S-100α and S-100β was determined both in cytoplasm and nucleus of the acinus epithelium, duct epithelium, myoepithelial and endothelial cells of extraorbital lacrimal gland. While S-100α immunoreaction in all structural components of the intraorbital gland was most densely observed in the nucleus, S-100β immunoreaction was negative in myoepithelial cells. Moreover, it is detected that wbS-100 immunreaction was positive in the lateral membranes of acinus epithelial cells of extraorbital gland and wbS100 and S-100β immunoreaction was positive in the lateral membranes of acinus and duct epithelial cells of intraorbital gland. α-SMA immunoreaction was detected in the myoepithelial cells and the smooth muscle cells in the wall of blood vessels of both glands. In conclusion, the differences detected between wbS-100, S-100α and S-100β proteins in all structural components of intraorbital and extraorbital lacrimal glands in terms of immunohistochemical staining density suggest that there is a functional difference between both lacrimal glands with respect to the secretory activity.

Kaynakça

  • Bao, L., Odell, A.F., Stephen, S.L., Wheatcroft, S.B., Walker, J.H., Ponnambalam, S., 2012. The S100A6 calciumbinding protein regulates endothelial cell-cycle progression and senescence. FEBS Journal 279, 45764588.
  • Botelho, H.M., Fritz, G., Gomes, C.M., 2012. Analysis of S100 oligomers and amyloids. Methods in Molecular Biolology 849, 373-386.
  • Brown, N.M., Lamartiniere, C.A., 2000. Genistein regulation of transforming growth factor-a, epidermal growth factor (EGF), and EGF Receptor expression in the rat uterus and vagina. Cell Growth and Differentiation 11, 255260.
  • Case, R.M., Ansah, T.A., Dho, S., Miziniak, A., Wilson, L., 1988. Calcium homeostasis in exocrine secretory cells. In: Gerdary CH, Gilles R, Bolis L (Eds), Calcium and calcium binding proteins. Molecular and funstional aspects. Springer, Berlin Heidelberg New York, pp. 211-219.
  • Cocchia, D., 1981. Immunocytochemical localization of S-100 protein in the brain of adult rat. An ultrastructural study. Cell and Tissue Research 214, 529-540.
  • Cruzana, B.C., Hondo, E., Kitamura, N., Nakagawa, M., Yamada, J., 2000. Differential localization of immunreactive α- and β-subunits of S-100 protein in feline testis. Anatomia Histologia Embryologia 29, 8386.
  • Cruzana, B.C., Budipitojo, T., Ocampo, G.D., Sasaki, M., Kitamura, N., Yamada, J., 2003. Immunohistochemical distribution of S-100 protein and subunits (S100-α and S100-β) in the swamp-type water buffalo (Bubalus bubalis) testis. Andrologia 35, 142-145
  • Dannies, P.S., Lewine, L., 1971. Structural properties of bovine brain S-100 protein. Journal of Biological Chemistry 246, 6276-6283.
  • Donato, R., 1991. Perspectives in S-100 biology. Cell Calcium 12, 713-726.
  • Donato, R., 1999. Functional roles of S-100 proteins, calciumbinding proteins of the EF-hand type. Biochimica et Biophysica Acta 1450, 191-231.
  • Donato, R., Michetti, F., Miani, N., 1975. Soluble and membrane-bound S-100 protein in cerebral cortex synaptosomes. Properties of the S-100 receptor. Brain Research 98, 561-573.
  • Donato, R., Prestagiovanni, B., Zelano, G., 1986. Identity between cytoplasmic and membrane-bound S-100 proteins purified from bovine and rat brain. Journal of Neurochemistry 46, 1333-1337.
  • Foell, D., Frosch, M., Sorg, C., Roth, J., 2004. Phagocyte-specific calcium-binding S100 proteins as clinical laboratory markers of inflammation. Clinica Chimica Acta 334, 3751.
  • Gugliotta, P., Sapino, A., Macri, L., Skalli, O., Gabbiani, G., Bussolatti, G., 1988. Specific Demonstration of miyoepithelial cells by anti-alpha smooth muscle actin antibody. Journal of Histochemistry and Cytochemistry 36, 659-663.
  • Haimoto, H., Hosoda, S., Kato, K., 1987. Differential distribution of immunoreactive S-100α and S-100β proteins in normal non-nervous human tissues. Laboratory Investigation, 57, 489-498.
  • Hara, K., Ito, M., Takeuchi, J., Iijima, S., Endo, T., Hidaka, H., 1983. Distribution of S-100b protein in normal salivary glands and salivary gland tumors. Virchows Archiv A 401, 237-249.
  • Hirano, T., Gluckman, J.L., de Vries, E.J., 1990. The expression of a vascular smooth muscle actin in salivary gland tumors. Archives of Otolaryngology- Head and Neck Surgery 116, 692-696.
  • Hirayama, K., Kagawa, Y., Tsuzuki, K., Kotani, T., Azuma, Y., Yoshino, T., Taniyama, H., 2000. A pleomorphic adenoma of the lacrimal gland in a dog. Veterinary Pathology 37, 353-356.
  • Isobe, T., Okuyama, T., 1981. The amino acid sequence of the subunit in bovine brain S-100a protein. European Journal of Biochemistry 166, 79-86
  • Isobe, T., Ishioka, N., Okuyama, T., 1981. Structural relation of two S-100 proteins in bovine brain; subunit composition of S-100a protein. European Journal of Biochemistry 115, 469-474.
  • Iwamoto, T., Jacobiec, F.A., 1985. Lacrimal glands. In: Duane, T.D., Jaeger, E.A., (Eds.), Biomedical Foundation of Ophthalmology. Vol 1. Revised ed. Philadelphia, Harper & Row, 30, 1.
  • Kawashima, M., Kawaikata, T., Inaba, T., Okada, N., Ito, M., Shimmura, S., Watanabe, M., Shinmura, K., Tsubota, K., 2012. Dietary lactoferrin alleviates age-related lacrimal gland dysfunction in mice. PLoS One 7, e33148.
  • Kivelä, T., 1992. Antigenic profile of the human lacrimal gland. Journal of Histochemistry and Cytochemistry 40, 629642.
  • Komarek, V., Gembardt, C., Krinke, A., Mahrous, T.A., Schaetti, P., 2000. Synopsis of The Organ Anatomy. In: Krinke, G.J., Handbook of The Experimental Animals. The Laboratory Rat. London, Academic Press, pp. 283-319.
  • Lauboeck, S., Egerbacher, M., 1997. Distribution of S-100 protein and its subunits in bovine exocrine glands. Histochemistry and Cell Biolology 108, 83-91.
  • Lee, S.K., Kim, E.C., Chi, J.G., Hashimura, K., Mori, M., 1993. Immunohistochemical detection of S-100, S-100α, S100β proteins, glial fibrillary acidic protein, and neuron specific enolase in the prenatal and adult human salivary glands. Pathology, Research and Practice 189, 1036-1043.
  • Leoncini, P., Cintorino, M., Vindigni, C., Leoncini, L., Armellini, D., Bugnoli, M., Skalli, O., Gabbiani, G., 1988. Distribution of cytoskeletal and contractile proteins in normal and tumor bearing salivary and lacrimal gland. Virchows Archive A: Pathological Anatomy and Histopathology 412, 329-337.
  • Liman, N., 2011. Duyu Sistemi. Özer, A. (Ed.), Veteriner Özel Histoloji, Birinci Baskı. Nobel Tıp Kitabevi, Ankara, Türkiye, pp. 269-322.
  • Makarenkova, H.P., Dartt, D.A., 2015. Myoepithelial cells: Their origin and function in lacrimal gland morphogenesis, homeostasis, and repair. Current Molecular Biology Reports, 1, 115-123.
  • Mandinova, A., Atar, D., Schäfer, B.W., Spiess, M., Aebi, U., Heizmann, C.W., 1998. Distinct subcellular localization of calcium binding S-100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium. Journal of Cell Science, 111, 20432054.
  • Marettová, E., Legáth, J., 2008. Distribution of S-100 protein in mandibular salivary gland of the sheep. Folia Veterinaria 52, 181-184.
  • Molin, S-O, Rosengren, L., Haglid, K., Baudier, J., Hamberger, A., 1984. Differential localization of “Brain-specific” S100 and its subunits in rat salivary glands. Journal of Histochemistry and Cytochemistry 32, 805-814.
  • Moore, B.W., 1965. A soluble protein characteristic of the nervous system. Biochemical and Biophysical Research Communications 19, 739-744
  • Mori, M., Kasai, T., Yuba, R., Chomette, G., Auriol, M., Vaillant, J.M., 1990. Immunohistochemical distribution studies of S-100 protein α and β subunits in adenoid cystic carcinoma of salivary glands. Virchows Archives Journal 59, 115-123.
  • Mori, M., Yamada, K., Ohomura, H., Wataru, K., Takai, Y., Ilg, E., Schäfer, B.W., Heizmann, C.W., 1998. Immunohistochemical localization of S100A1 and S100A6 in postnatally developing salivary glands of rats. Histochemistry and Cell Biology 110, 579-587.
  • Petersen, O.H., 1992. Stimulus secretion coupling: cytoplasmic calcium signals and the control of ion channels in exocrine acinal cells. Journal of Physiology 448, 1-51.
  • Putney, J.W., Bird, G.S., 2014. Calcium signaling in lacrimal glands. Cell Calcium 55, 290-296.
  • Sandusky, G.E., Carlton, W.W., Wightman, K.A., 1985. Immunohistochemical staining for S-100 protein in the diagnosis of canine amelanotik melanoma. Veterinary Pathology 22, 577-581.
  • Stefansson, K., Wollmann, R.L., Moore, B.W., Arnason, B.G., 1982a. S-100 protein in human chondrocytes. Nature 295, 63-64.
  • Stefansson, K., Wollmann, R.L., Moore, B.W., 1982b. Distribution of S-100 protein outside the central nervous system. Brain Research 234, 309-317.
  • Stern, M.E., Gao, J., Siemasko, K.F., Beuerman, R.W., Pflugfelder, S.C., 2004. The role of the lacrimal functional unit in the pathophysiology of dry eye. Experimental Eye Research 78, 409-416.
  • Sundermeier, T., Matthews, G., Brink, P.R., Walcott, B., 2002. Calcium dependence of exocytosis in lacrimal gland acinar cells. American Journal of Physiology- Cell Physiology 282, 360-365.
  • Tosaka, Y., 1991. Immunohistochemical study of pleomoprhic adenoma of lacrimal gland. Japanase Journal Ophthalmology 35, 367-376.
  • Treves, S., Scutari, E., Robert, M., Groh, S., Ottolia, M., Prestipino, G., Ronjat, M., Zorzato, F., 1997. Interaction of S-100A1 with the Ca2+ release channel (rynnodine receptor) of skeletal muscle. Biochemistry 36, 11496-11503.
  • Walter, I., Miller, I., 1996. S-100 protein subunits in bovine oviduct epithelium: in situ distribution and changes during primary cell culture. Histochemical Journal 28, 671-680.
  • Yao, R., Lopez-Beltran, A., Maclennan, G.T., Montironi, R., Eble, J.N., Cheng, L., 2007. Expression of S100 protein family members in the pathogenesis of bladder tumors. Anticancer Research 27, 3051-3058.
  • Zimmer, D.B., Sadosky, P.W., Weber, D.J., 2003. Molecular mechanisms of S-100-target protein interactions. Microscopy Research and Technique 60, 552-559.

Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein ve Alt Ünitelerinin Lokalizasyonları

Yıl 2016, Cilt: 42 Sayı: 2, 161 - 170, 04.07.2016
https://doi.org/10.16988/iuvfd.2016.94909

Öz

Bu çalışma, erişkin erkek sıçanların intraorbital ve ekstraorbital lakrimal bezinde kalsiyum bağlayan wbS-100, S-100α ve S-100β proteinleri ile α-SMA’nın immuno-histokimyasal lokalizasyonlarını ortaya koymak amacıyla planlandı. Sıçanlardan anestezi altında lakrimal bezin ekstraorbital ve intraorbital kısımları çıkartıldıktan sonra rutin histolojik prosedürü takiben bloklanan doku örneklerinden alınan 4 μm kalınlığındaki kesitlere wbS-100, S-100α, S-100β ve α-SMA proteinlerini belirlemek için Streptavidin-biotin-peroksidaz immunohistokimyasal teknik uygulandı. Ekstraorbital lakrimal bezin asinus epiteli, akıtıcı kanal epiteli, miyoepitel ve endotel hücrelerinin hem sitoplazmasında hem de çekirdeğinde wbS-100, S-100α ve S-100β immunreaksiyonuna rastlandı. İntraorbital bezin bütün yapısal komponentlerinde S-100α immunreaksiyonu en yoğun derecede çekirdekte gözlenirken, S-100β immunreaksiyonu miyoepitel hücrelerinde negatifti. Aynı zamanda ekstraorbital bezin asinus epitel hücrelerinin lateral membranlarında wbS-100 immunreaksiyonu, intraorbital bezin asinus epiteli ve akıtıcı kanal epitel hücrelerinin lateral membranlarında ise wbS100 ve S-100β immunreaksiyonu belirlendi. Her iki bezin miyoepitel hücreleri ile kan damarlarının duvarında yer alan düz kas hücrelerinde α-SMA immunreaksiyonu saptandı. Sonuç olarak, intraorbital ve ekstraorbital lakrimal bezlerin bütün yapısal komponentlerinde wbS-100, S-100α ve S-100β proteinleri arasındaki immunohistokimyasal boyanma yoğunluğu açısından tespit edilen bu farklılıkların her iki lakrimal bez arasında salgı aktivitesi ile ilgili fonksiyonel farklılığın olduğu düşüncesini akla getirmektedir.

Kaynakça

  • Bao, L., Odell, A.F., Stephen, S.L., Wheatcroft, S.B., Walker, J.H., Ponnambalam, S., 2012. The S100A6 calciumbinding protein regulates endothelial cell-cycle progression and senescence. FEBS Journal 279, 45764588.
  • Botelho, H.M., Fritz, G., Gomes, C.M., 2012. Analysis of S100 oligomers and amyloids. Methods in Molecular Biolology 849, 373-386.
  • Brown, N.M., Lamartiniere, C.A., 2000. Genistein regulation of transforming growth factor-a, epidermal growth factor (EGF), and EGF Receptor expression in the rat uterus and vagina. Cell Growth and Differentiation 11, 255260.
  • Case, R.M., Ansah, T.A., Dho, S., Miziniak, A., Wilson, L., 1988. Calcium homeostasis in exocrine secretory cells. In: Gerdary CH, Gilles R, Bolis L (Eds), Calcium and calcium binding proteins. Molecular and funstional aspects. Springer, Berlin Heidelberg New York, pp. 211-219.
  • Cocchia, D., 1981. Immunocytochemical localization of S-100 protein in the brain of adult rat. An ultrastructural study. Cell and Tissue Research 214, 529-540.
  • Cruzana, B.C., Hondo, E., Kitamura, N., Nakagawa, M., Yamada, J., 2000. Differential localization of immunreactive α- and β-subunits of S-100 protein in feline testis. Anatomia Histologia Embryologia 29, 8386.
  • Cruzana, B.C., Budipitojo, T., Ocampo, G.D., Sasaki, M., Kitamura, N., Yamada, J., 2003. Immunohistochemical distribution of S-100 protein and subunits (S100-α and S100-β) in the swamp-type water buffalo (Bubalus bubalis) testis. Andrologia 35, 142-145
  • Dannies, P.S., Lewine, L., 1971. Structural properties of bovine brain S-100 protein. Journal of Biological Chemistry 246, 6276-6283.
  • Donato, R., 1991. Perspectives in S-100 biology. Cell Calcium 12, 713-726.
  • Donato, R., 1999. Functional roles of S-100 proteins, calciumbinding proteins of the EF-hand type. Biochimica et Biophysica Acta 1450, 191-231.
  • Donato, R., Michetti, F., Miani, N., 1975. Soluble and membrane-bound S-100 protein in cerebral cortex synaptosomes. Properties of the S-100 receptor. Brain Research 98, 561-573.
  • Donato, R., Prestagiovanni, B., Zelano, G., 1986. Identity between cytoplasmic and membrane-bound S-100 proteins purified from bovine and rat brain. Journal of Neurochemistry 46, 1333-1337.
  • Foell, D., Frosch, M., Sorg, C., Roth, J., 2004. Phagocyte-specific calcium-binding S100 proteins as clinical laboratory markers of inflammation. Clinica Chimica Acta 334, 3751.
  • Gugliotta, P., Sapino, A., Macri, L., Skalli, O., Gabbiani, G., Bussolatti, G., 1988. Specific Demonstration of miyoepithelial cells by anti-alpha smooth muscle actin antibody. Journal of Histochemistry and Cytochemistry 36, 659-663.
  • Haimoto, H., Hosoda, S., Kato, K., 1987. Differential distribution of immunoreactive S-100α and S-100β proteins in normal non-nervous human tissues. Laboratory Investigation, 57, 489-498.
  • Hara, K., Ito, M., Takeuchi, J., Iijima, S., Endo, T., Hidaka, H., 1983. Distribution of S-100b protein in normal salivary glands and salivary gland tumors. Virchows Archiv A 401, 237-249.
  • Hirano, T., Gluckman, J.L., de Vries, E.J., 1990. The expression of a vascular smooth muscle actin in salivary gland tumors. Archives of Otolaryngology- Head and Neck Surgery 116, 692-696.
  • Hirayama, K., Kagawa, Y., Tsuzuki, K., Kotani, T., Azuma, Y., Yoshino, T., Taniyama, H., 2000. A pleomorphic adenoma of the lacrimal gland in a dog. Veterinary Pathology 37, 353-356.
  • Isobe, T., Okuyama, T., 1981. The amino acid sequence of the subunit in bovine brain S-100a protein. European Journal of Biochemistry 166, 79-86
  • Isobe, T., Ishioka, N., Okuyama, T., 1981. Structural relation of two S-100 proteins in bovine brain; subunit composition of S-100a protein. European Journal of Biochemistry 115, 469-474.
  • Iwamoto, T., Jacobiec, F.A., 1985. Lacrimal glands. In: Duane, T.D., Jaeger, E.A., (Eds.), Biomedical Foundation of Ophthalmology. Vol 1. Revised ed. Philadelphia, Harper & Row, 30, 1.
  • Kawashima, M., Kawaikata, T., Inaba, T., Okada, N., Ito, M., Shimmura, S., Watanabe, M., Shinmura, K., Tsubota, K., 2012. Dietary lactoferrin alleviates age-related lacrimal gland dysfunction in mice. PLoS One 7, e33148.
  • Kivelä, T., 1992. Antigenic profile of the human lacrimal gland. Journal of Histochemistry and Cytochemistry 40, 629642.
  • Komarek, V., Gembardt, C., Krinke, A., Mahrous, T.A., Schaetti, P., 2000. Synopsis of The Organ Anatomy. In: Krinke, G.J., Handbook of The Experimental Animals. The Laboratory Rat. London, Academic Press, pp. 283-319.
  • Lauboeck, S., Egerbacher, M., 1997. Distribution of S-100 protein and its subunits in bovine exocrine glands. Histochemistry and Cell Biolology 108, 83-91.
  • Lee, S.K., Kim, E.C., Chi, J.G., Hashimura, K., Mori, M., 1993. Immunohistochemical detection of S-100, S-100α, S100β proteins, glial fibrillary acidic protein, and neuron specific enolase in the prenatal and adult human salivary glands. Pathology, Research and Practice 189, 1036-1043.
  • Leoncini, P., Cintorino, M., Vindigni, C., Leoncini, L., Armellini, D., Bugnoli, M., Skalli, O., Gabbiani, G., 1988. Distribution of cytoskeletal and contractile proteins in normal and tumor bearing salivary and lacrimal gland. Virchows Archive A: Pathological Anatomy and Histopathology 412, 329-337.
  • Liman, N., 2011. Duyu Sistemi. Özer, A. (Ed.), Veteriner Özel Histoloji, Birinci Baskı. Nobel Tıp Kitabevi, Ankara, Türkiye, pp. 269-322.
  • Makarenkova, H.P., Dartt, D.A., 2015. Myoepithelial cells: Their origin and function in lacrimal gland morphogenesis, homeostasis, and repair. Current Molecular Biology Reports, 1, 115-123.
  • Mandinova, A., Atar, D., Schäfer, B.W., Spiess, M., Aebi, U., Heizmann, C.W., 1998. Distinct subcellular localization of calcium binding S-100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium. Journal of Cell Science, 111, 20432054.
  • Marettová, E., Legáth, J., 2008. Distribution of S-100 protein in mandibular salivary gland of the sheep. Folia Veterinaria 52, 181-184.
  • Molin, S-O, Rosengren, L., Haglid, K., Baudier, J., Hamberger, A., 1984. Differential localization of “Brain-specific” S100 and its subunits in rat salivary glands. Journal of Histochemistry and Cytochemistry 32, 805-814.
  • Moore, B.W., 1965. A soluble protein characteristic of the nervous system. Biochemical and Biophysical Research Communications 19, 739-744
  • Mori, M., Kasai, T., Yuba, R., Chomette, G., Auriol, M., Vaillant, J.M., 1990. Immunohistochemical distribution studies of S-100 protein α and β subunits in adenoid cystic carcinoma of salivary glands. Virchows Archives Journal 59, 115-123.
  • Mori, M., Yamada, K., Ohomura, H., Wataru, K., Takai, Y., Ilg, E., Schäfer, B.W., Heizmann, C.W., 1998. Immunohistochemical localization of S100A1 and S100A6 in postnatally developing salivary glands of rats. Histochemistry and Cell Biology 110, 579-587.
  • Petersen, O.H., 1992. Stimulus secretion coupling: cytoplasmic calcium signals and the control of ion channels in exocrine acinal cells. Journal of Physiology 448, 1-51.
  • Putney, J.W., Bird, G.S., 2014. Calcium signaling in lacrimal glands. Cell Calcium 55, 290-296.
  • Sandusky, G.E., Carlton, W.W., Wightman, K.A., 1985. Immunohistochemical staining for S-100 protein in the diagnosis of canine amelanotik melanoma. Veterinary Pathology 22, 577-581.
  • Stefansson, K., Wollmann, R.L., Moore, B.W., Arnason, B.G., 1982a. S-100 protein in human chondrocytes. Nature 295, 63-64.
  • Stefansson, K., Wollmann, R.L., Moore, B.W., 1982b. Distribution of S-100 protein outside the central nervous system. Brain Research 234, 309-317.
  • Stern, M.E., Gao, J., Siemasko, K.F., Beuerman, R.W., Pflugfelder, S.C., 2004. The role of the lacrimal functional unit in the pathophysiology of dry eye. Experimental Eye Research 78, 409-416.
  • Sundermeier, T., Matthews, G., Brink, P.R., Walcott, B., 2002. Calcium dependence of exocytosis in lacrimal gland acinar cells. American Journal of Physiology- Cell Physiology 282, 360-365.
  • Tosaka, Y., 1991. Immunohistochemical study of pleomoprhic adenoma of lacrimal gland. Japanase Journal Ophthalmology 35, 367-376.
  • Treves, S., Scutari, E., Robert, M., Groh, S., Ottolia, M., Prestipino, G., Ronjat, M., Zorzato, F., 1997. Interaction of S-100A1 with the Ca2+ release channel (rynnodine receptor) of skeletal muscle. Biochemistry 36, 11496-11503.
  • Walter, I., Miller, I., 1996. S-100 protein subunits in bovine oviduct epithelium: in situ distribution and changes during primary cell culture. Histochemical Journal 28, 671-680.
  • Yao, R., Lopez-Beltran, A., Maclennan, G.T., Montironi, R., Eble, J.N., Cheng, L., 2007. Expression of S100 protein family members in the pathogenesis of bladder tumors. Anticancer Research 27, 3051-3058.
  • Zimmer, D.B., Sadosky, P.W., Weber, D.J., 2003. Molecular mechanisms of S-100-target protein interactions. Microscopy Research and Technique 60, 552-559.
Toplam 47 adet kaynakça vardır.

Ayrıntılar

Konular Sağlık Kurumları Yönetimi
Bölüm Araştırma Makalesi
Yazarlar

Emel Alan Bu kişi benim

Narin Liman Bu kişi benim

Yayımlanma Tarihi 4 Temmuz 2016
Yayımlandığı Sayı Yıl 2016 Cilt: 42 Sayı: 2

Kaynak Göster

APA Alan, E., & Liman, N. (2016). Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein ve Alt Ünitelerinin Lokalizasyonları. İstanbul Üniversitesi Veteriner Fakültesi Dergisi, 42(2), 161-170. https://doi.org/10.16988/iuvfd.2016.94909
AMA Alan E, Liman N. Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein ve Alt Ünitelerinin Lokalizasyonları. iuvfd. Haziran 2016;42(2):161-170. doi:10.16988/iuvfd.2016.94909
Chicago Alan, Emel, ve Narin Liman. “Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein Ve Alt Ünitelerinin Lokalizasyonları”. İstanbul Üniversitesi Veteriner Fakültesi Dergisi 42, sy. 2 (Haziran 2016): 161-70. https://doi.org/10.16988/iuvfd.2016.94909.
EndNote Alan E, Liman N (01 Haziran 2016) Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein ve Alt Ünitelerinin Lokalizasyonları. İstanbul Üniversitesi Veteriner Fakültesi Dergisi 42 2 161–170.
IEEE E. Alan ve N. Liman, “Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein ve Alt Ünitelerinin Lokalizasyonları”, iuvfd, c. 42, sy. 2, ss. 161–170, 2016, doi: 10.16988/iuvfd.2016.94909.
ISNAD Alan, Emel - Liman, Narin. “Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein Ve Alt Ünitelerinin Lokalizasyonları”. İstanbul Üniversitesi Veteriner Fakültesi Dergisi 42/2 (Haziran 2016), 161-170. https://doi.org/10.16988/iuvfd.2016.94909.
JAMA Alan E, Liman N. Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein ve Alt Ünitelerinin Lokalizasyonları. iuvfd. 2016;42:161–170.
MLA Alan, Emel ve Narin Liman. “Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein Ve Alt Ünitelerinin Lokalizasyonları”. İstanbul Üniversitesi Veteriner Fakültesi Dergisi, c. 42, sy. 2, 2016, ss. 161-70, doi:10.16988/iuvfd.2016.94909.
Vancouver Alan E, Liman N. Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein ve Alt Ünitelerinin Lokalizasyonları. iuvfd. 2016;42(2):161-70.