Vascular permeability to proteins and peptides in the mouse pineal gland.
The permeability of fenestrated capillaries in the mouse pineal gland to proteins and peptides was demonstrated by means of ultrastructural tracers. Horseradish peroxidase (HRP) and microperoxidase (MP) were injected intravenously and allowed to circulate for approximately 30 s, 1 min, 5 min, 1 or 2 h. The tissue was then fixed by vascular perfusion or by immersion with aldehydes. In all experiments a pronounced extravasation of HRP and MP occurred. Transendothelial vesicular transport seemed to have occurred across the fenestrated capillaries. The most pronounced tracer labeling of vesicles was found after 1 min of MP- or HRP-circulation. The vesicles were uncoated and more than 70% of the HRP- and MP-containing vesicles exhibited diameters between 50 and 110 nm. Furthermore, three other transcapillary pathways taken by the tracers are suggested: 1) via intercellular junctions, 2) through fenestrae and 3) via channels formed by fusion of vesicles with the luminal and abluminal cell membranes. Based on these results, it is assumed that the capillaries in the mouse pineal gland also permeable to peptides synthesized and secreted by the pineal gland.
D000818:Animals; D002196:Capillaries / Q000648:ultrastructure; D002199:Capillary Permeability; D004727:Endothelium / Q000378:metabolism; D006420:Hemeproteins / Q000378:metabolism; D006735:Horseradish Peroxidase / Q000378:metabolism; D008297:Male; D051379:Mice; D010455:Peptides / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism; D010870:Pineal Gland / Q000098:blood supply / Q000378:metabolism* / Q000648:ultrastructure; D011506:Proteins / Q000378:metabolism*
D006420:Hemeproteins; D010455:Peptides; D011506:Proteins; D006735:Horseradish Peroxidase; D010544:Peroxidases; C021799:microperoxidase