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Abstract
LH, FSH, and CG are comprised of a common
-subunit
and a hormone-specific
-subunit. Using Madin-Darby
canine kidney (MDCK) epithelial cells to examine the
polarized secretion of human CG/LH, we previously reported
that CG and LH were detected in the apical and basolateral
compartments, respectively, and the carboxyl terminal end
of the CG
-subunit contains a strong apical signal.
Here we show that the carboxyl seven amino acids in the
LH
-subunit contribute to the basolateral secretion
of LH, and an LH chimera bearing the CG
apical
signal is redirected from the basolateral to the apical
compartments. Because LH and FSH are synthesized in the
same cell, we also compared the secretion polarity of LH
with FSH. MDCK cells expressing the FSH dimer displayed an
almost equal distribution of protein into the apical and
basolateral compartments. Given that the LH
and CG
carboxy terminal sequences, which differ from that
in the FSH
-subunit, occupy a pivotal role in their
polarized behavior, the results support the hypothesis
that pituitary exit of LH and FSH occur via different
secretion pathways, and are released spatially from the
pituitary via different circulatory routes.
Key words:
Pituitary
Follicle-stimulating hormone
Human chorionic gonadotropin
Luteinizing hormone
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S. Nakav, A. Jablonka-Shariff, S. Kaner, P. Chadna-Mohanty, H. E. Grotjan, and D. Ben-Menahem The LH{beta} Gene of Several Mammals Embeds a Carboxyl-terminal Peptide-like Sequence Revealing a Critical Role for Mucin Oligosaccharides in the Evolution of Lutropin to Chorionic Gonadotropin in the Animal Phyla J. Biol. Chem., April 29, 2005; 280(17): 16676 - 16684. [Abstract] [Full Text] [PDF] |
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