Studies on the spermatogenic sulfogalactolipid binding protein SLIP 1.
We have purified the testicular sulfogalactolipid binding protein SLIP 1 and shown by photoaffinity labeling that it contains an ATP binding site. Purified SLIP 1 was fluorescently labeled and shown to retain specific sulfogalactolipid binding function. This probe was used to investigate the topology of SLIP 1 binding sites on testicular germ cells. The binding pattern precisely coincided with the previously demonstrated asymmetric surface domains of sulfogalactoglycerolipid (SGG). Occasionally these SGG-containing, SLIP 1-binding cell surface domains exactly coincided with structural features on the cell surface as detected by differential interference contrast microscopy. These results demonstrate that SLIP 1/SGG interactions could provide an effective intercellular communication network between testicular germ cells within the seminiferous tubule.
Lingwood
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Department of Biochemistry, Hospital for Sick Children, Toronto, Canada.
Nutikka
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D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism; D000345:Affinity Labels; D000818:Animals; D001386:Azides / Q000378:metabolism; D002352:Carrier Proteins / Q000096:biosynthesis / Q000302:isolation & purification*; D018797:Cell Cycle Proteins; D002846:Chromatography, Affinity; D006017:Glycolipids / Q000378:metabolism; D008297:Male; D008565:Membrane Proteins / Q000096:biosynthesis / Q000302:isolation & purification*; D010761:Phosphorus Radioisotopes; D051381:Rats; D011919:Rats, Inbred Strains; D013091:Spermatogenesis / Q000502:physiology*; D013737:Testis / Q000737:chemistry
D000345:Affinity Labels; D001386:Azides; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D006017:Glycolipids; D008565:Membrane Proteins; D010761:Phosphorus Radioisotopes; C051337:Slip1 protein, rat; C017040:8-azidoadenosine 5'-triphosphate; D000255:Adenosine Triphosphate