Site of synthesis, intracellular transport and secretion of glycoprotein in exocrine cells.

The site of attachment of the first sugar, N-acetylgalactosamine, to the seryl and threonyl residues of the protein chain is unknown in exocrine cells. The subsequent sugars of the carbohydrate side chains, galactose and N-acetylglucosamine alternately, and the end-group sugars, galactose, N-acetylgalactosamine and fucose, are attached in the Golgi complex. Sulphate too is attached in that structure. In the stomach, sulphate is probably transferred in the most mature cisterna of the Golgi stacks, galactose and fucose in other cisternae, suggesting a gradient in transferase activities along the stack. The possibilities of regulating the amount and relative sugar composition of the glycoproteins are discussed. The secretory product is stored in granules. Their polygonal, large and swollen appearance and complex formation by loss of bordering membranes, as observed in many kinds of glycoprotein-secreting cells ('mucous cells') might be caused by ineffective fixation techniques. Direct vascular perfusion results in a picture no different from what is found in non-mucous cells. Whether secretion is merely exocytotic, as in non-mucous cells, or whether it is accompanied by a loss of membrane and even cytoplasm needs thorough investigation, with the effects of various fixation techniques being compared.