W. Schulze et Ib. Buchwalow, ADENYLYL-CYCLASE IN THE HEART - AN ENZYMOCYTOCHEMICAL AND IMMUNOCYTOCHEMICAL APPROACH, Microscopy research and technique, 40(6), 1998, pp. 473-478
This review provides a discussion of the localization of adenylyl cycl
ase (AC) in normal mammalian heart tissue employing enzymocytochemistr
y (detection of the catalytic activity of AC by a metal precipitation
technique) and immunocytochemistry (immunolabeling of the enzyme prote
in with antibodies against AC subtypes). By the metal precipitation te
chnique, AC activity was localized in adult guinea pig cardiomyocytes
along the sarcolemma and the T-tubule membranes. This reaction can be
enhanced by hormones and guanylyl imidodiphosphate, fluoride, and fors
kolin. With this technique, no precipitates were detected at the sarco
plasmic reticulum. However, under ischemic conditions, AC activity was
also found in the junctional sarcoplasmic reticulum of rat cardiomyoc
ytes. Immunocytochemistry revealed AC in the plasma membrane of rat ca
rdiomyocytes. Detection of AC in the perinuclear space of cardiomyocyt
es might reflect initiation of synthesis and processing of the enzyme
protein. Colocalization of AC with cytoskeleton fibers of non-cardiomy
ocytes emerging in the cell culture of neonatal rat cardiocytes imply
a direct cytoskeletal-AC interaction. Finally, it can be stated that t
he immunolabeling pattern of AC in cryosections of adult and new-born
rat hearts reveals a good correspondence with the localization of AC a
ctivity in cardiomyocytes demonstrated by enzymocytochemistry. (C) 199
8 Wiley-Liss, Inc.