Immunolocalization of secretory protein-I or chromogranin A in amphibian urinary bladder granular cell granules.
The presence of secretory protein-I (SP-I) or chromogranin A (CGA) in granules isolated from the granular cells of the amphibian urinary bladder epithelium was investigated using ultraimmunohistochemistry. Granules were isolated by cell fractionation using Percoll density gradients. SP-I was isolated and purified from bovine parathyroid glands. Antibodies were raised in rabbits and purified by affinity chromatography. Ultraimmunocytochemistry, employing the avidin-biotin-peroxidase (ABC-complex) procedure, was used to localize SP-I on thin sections of isolated granules. About 27% of the granules from control (-ADH) cells were SP-I+, while 51% of the granules fractionated from hormone treated (+ADH) cells were positive for this protein (p less than 0.0001). Accordingly, granules from ADH-treated cells also showed a significant (p less than 0.0001) increase in total protein.
Davis
W L
WL
Department of Anatomy, Baylor College of Dentistry, Dallas, TX 75246.
Schmid
K O
KO
Huettner
J W
JW
Farmer
G R
GR
Jacoby
B H
BH
Goodman
D B
DB
D000818:Animals; D002024:Bufo marinus / Q000378:metabolism*; D053379:Chromogranin A; D002864:Chromogranins / Q000378:metabolism*; D003594:Cytoplasmic Granules / Q000378:metabolism / Q000648:ultrastructure; D005260:Female; D007150:Immunohistochemistry; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D001743:Urinary Bladder / Q000166:cytology* / Q000378:metabolism / Q000648:ultrastructure
D053379:Chromogranin A; D002864:Chromogranins; D009419:Nerve Tissue Proteins