Scolexin is one of the bacterial induced hemolymph proteins of tobacco hornworm (Manduca sexta) larvae, that has hemocyte coagulation-provoking activity. The 72 kDa scolexin complex is composed of two 36 kDa subunits. To examine the protein secretory pathways in insect epithelia a polyclonal antibody was raised against the 36 kDa hemolymph protein. This MsH36 antibody recognised a 36 and a 72 kDa protein in tissue homogenates. On the basis of the characteristic labelling pattern observed on immunoblots and immunocytochemical sections we concluded that the 36 kDa protein in the hemolymph, in the midgut and in the epidermis was identical with the scolexin subunit. In present paper we report a labelling shift in the midgut epithelium between goblet and columnar cells that may be controlled by the hormonal system. A 72 kDa protein showed similar epitops and molecular weight to the scolexin complex and was detected in epidermis and in cuticle under both reducing and non-reducing conditions. Tissue localization of 36 kDa and 72 kDa MsH36 antibody labelling proteins indicated the possibility that the epidermal cells produce two kinds of scolexin-like proteins. The complex composed of 36 kDa subunits are transported basolaterally into the circulation and display hemocyte coagulation inducing activity while the 72 kDa form contains two subunits linked covalently secreted apically into the cuticle.
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Dedicated to Professor János Kovács on the occasion of his 70th birthday.
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Molnár, K., Borhegyi, N.H., Csikós, G. et al. The Immunoprotein Scolexin and Its Synthesizing Sites — The Midgut Epithelium and the Epidermis. BIOLOGIA FUTURA 52, 473–484 (2001). https://doi.org/10.1556/ABiol.52.2001.4.11
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