Multidrug resistance-associated protein 9 (ABCC12) is present in mouse and boar sperm | Zendy

Nobuhito Ono | Zendy; Ingrid van der Heijden | Zendy; George L. Scheffer | Zendy; Koen van de Wetering | Zendy; Elizabeth Van Deemter | Zendy; Marcel de Haas | Zendy; Arjan Boerke | Zendy; Bart M. Gadella | Zendy; Dirk G. de Rooij | Zendy; Jacques Neefjes | Zendy; Tom A. Groothuis | Zendy; Lauran C. J. M. Oomen | Zendy; Lenny Brocks | Zendy; Toshihisa Ishikawa | Zendy; Piet Borst | Zendy

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Multidrug resistance-associated protein 9 (ABCC12) is present in mouse and boar sperm

Author(s) -

Nobuhito Ono,

Ingrid van der Heijden,

George L. Scheffer,

Koen van de Wetering,

Elizabeth Van Deemter,

Marcel de Haas,

Arjan Boerke,

Bart M. Gadella,

Dirk G. de Rooij,

Jacques Neefjes,

Tom A. Groothuis,

Lauran C. J. M. Oomen,

Lenny Brocks,

Toshihisa Ishikawa,

Piet Borst

Publication year - 2007

Publication title -

biochemical journal

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.706

H-Index - 265

eISSN - 1470-8728

pISSN - 0264-6021

DOI - 10.1042/bj20070292

Subject(s) - hek 293 cells , transfection , sperm , biology , microbiology and biotechnology , endoplasmic reticulum , embryonic stem cell , mitochondrion , germ cell , cell culture , biochemistry , gene , genetics

The human and murine genes for MRP9 (multidrug resistance-associated protein 9; ABCC12) yield many alternatively spliced RNAs. Using a panel of monoclonal antibodies, we detected full-length Mrp9 only in testicular germ cells and mouse sperm; we obtained no evidence for the existence of the truncated 100 kDa MRP9 protein reported previously. In contrast with other MRPs, neither murine Mrp9 nor the human MRP9 produced in MRP9-transfected HEK-293 cells (human embryonic kidney cells) appears to contain N-linked carbohydrates. In mouse and boar sperm, Mrp9 localizes to the midpiece, a structure containing all sperm mitochondria. However, immunolocalization microscopy and cell fractionation studies with transfected HEK-293 cells and mouse testis show that MRP9/Mrp9 does not localize to mitochondria. In HEK-293 cells, it is predominantly localized in the endoplasmic reticulum. We have been unable to demonstrate transport by MRP9 of substrates transported by other MRPs, such as drug conjugates and other organic anions.

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