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

Year 2016, Volume: 42 Issue: 2, 161 - 170, 04.07.2016
https://doi.org/10.16988/iuvfd.2016.94909

Abstract

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.

References

  • 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

Year 2016, Volume: 42 Issue: 2, 161 - 170, 04.07.2016
https://doi.org/10.16988/iuvfd.2016.94909

Abstract

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.

References

  • 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.
There are 47 citations in total.

Details

Subjects Health Care Administration
Journal Section Research Article
Authors

Emel Alan This is me

Narin Liman This is me

Publication Date July 4, 2016
Published in Issue Year 2016 Volume: 42 Issue: 2

Cite

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. June 2016;42(2):161-170. doi:10.16988/iuvfd.2016.94909
Chicago Alan, Emel, and Narin Liman. “Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein Ve Alt Ünitelerinin Lokalizasyonları”. İstanbul Üniversitesi Veteriner Fakültesi Dergisi 42, no. 2 (June 2016): 161-70. https://doi.org/10.16988/iuvfd.2016.94909.
EndNote Alan E, Liman N (June 1, 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 and N. Liman, “Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein ve Alt Ünitelerinin Lokalizasyonları”, iuvfd, vol. 42, no. 2, pp. 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 (June 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 and Narin Liman. “Sıçanların Lakrimal Bezlerinde α-SMA, S-100 Protein Ve Alt Ünitelerinin Lokalizasyonları”. İstanbul Üniversitesi Veteriner Fakültesi Dergisi, vol. 42, no. 2, 2016, pp. 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.