Non-gastric H+/K+ ATPase is present in the microvillous membrane of the human placental syncytiotrophoblast.
In humans, the non-gastric H(+)/K(+)ATPase (ATP1AL1) has previously been shown to be expressed in the epithelia of skin, kidney and colon. In this study we tested the hypothesis that the non-gastric H(+)/K(+)ATPase is localized to the syncytiotrophoblast, the transporting epithelium of the human placenta. Microvillous (MVM) and basal plasma membranes (BM) of the syncytiotrophoblast were isolated from term placenta and membrane proteins were separated using SDS-PAGE. The ATP1AL1 protein was identified as a 114 kD band in both MVM and BM by Western blot, however, the protein was more abundant in the MVM. Using immunocytochemistry H(+)/K(+)ATPase protein was localized in MVM but not BM. We constructed primers specific for ATP1AL1 and performed RT-PCR on RNA isolated from human placenta and human kidney. A product of the expected size could be detected in both tissues after 30 cycles of amplification. The sequence identity of this 517 nucleotide product was confirmed by sequencing and found to be identical to the human non-gastric H(+)/K(+)ATPase. The activity of this proton pump appears to be low in normal healthy placental at term, however, it is speculated that MVM non-gastric H(+)/K(+)ATPase may be important in pathological states. In conclusion, non-gastric H(+)/K(+)ATPase is present in the microvillous plasma membrane of the transporting epithelia of the human placenta.[1]References
- Non-gastric H+/K+ ATPase is present in the microvillous membrane of the human placental syncytiotrophoblast. Johansson, M., Jansson, T., Pestov, N.B., Powell, T.L. Placenta (2004) [Pubmed]
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