PKC plays a central role for the regulation of renal function. PKC con
sists of a family of isoenzymes. By employing Northern blot techniques
we have demonstrated that mRNA transcripts for the classical Ca2+-dep
endent, diacylglycerol-activated isoform alpha, the novel, Ca2+-indepe
ndent isoform delta and the atypical isoform zeta are abundantly expre
ssed in the rat kidney. The novel PKC-epsilon was weakly expressed. Th
e classical PKCs >beta I, beta II and gamma could not be detected. The
mRNA expression of PKC-delta and -zeta increased with age. The intrar
enal localization of PKC-alpha, -delta and -zeta isoforms were studied
in the adult kidney using in situ hybridization. In the cortex, the P
KC-alpha isofom showed the strongest hybridization signal. PKC alpha,
delta and zeta were all distributed in the outer medulla. The PKC-alph
a probe detected particularly strong signal in the outer stripe of the
outer medulla. Western blot confirmed the presence of the PKC-alpha,
-delta and -zeta enzymes in renal tissue. The results show cell-specif
ic and developmentally-dependent expression of three types of PKC isof
orms with different responses to diacylglycerol and calcium. The devel
opmental increase of both PKC-delta and PKC-zeta suggests a specific r
ole for these isoforms for the functional regulation of the mature kid
ney.