title: Subcellular and regional location of "brain" proteins BASP1 and MARCKS in kidney and testis.
abstract: Proteins BASP1 and MARCKS are abundant in axonal endings of neurons. Similarly to brain-specific protein GAP-43, BASP1 and MARCKS are reversibly bound to the plasma membrane. These proteins control both actin polymerization and actin cytoskeleton binding to the membrane. Performing these functions, BASP1 and MARCKS take part in growth cone guidance during development and in neurotransmitter secretion in adults. These activities predetermine the pivotal role of BASP1 and MARCKS in learning and memory. BASP1 and MARCKS were also found in non-nerve tissues, in particular, in the kidney and testis. Evidently, the physiological roles of these proteins differ in different tissues. Correspondingly, their intracellular location and activities may not be similar to those in neurons. In this paper, we analyze subcellular fractions (cytoplasm and nuclei) of rat kidney and testis with the purpose of determining the intracellular location of BASP1 and MARCKS. Western blots demonstrated that in these tissues, as in the brain, both proteins are present in the cytoplasm of the cell. According to our immunohistochemical study, BASP1 and MARCKS are specifically distributed in the tissues studied. In kidney, both proteins are present in cells located in glomeruli. In the testicular tubules, BASP1 is mainly expressed at the late stage of spermatogenesis (in spermatids) and is preserved in mature spermatozoa, while MARCKS appears equally during all stages of spermatogenesis. MARCKS is not found in mature spermatozoa. The results indicate that study of functions of BASP1 and MARCKS in the kidney and in the reproduction system holds much promise.
authors.affiliation: Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, Leningrad District, Russian Federation. m_mosev@mail.ru
authors.forename: Mark
authors.initials: M
authors.lastname: Mosevitsky
authors.forename: Inga
authors.initials: I
authors.lastname: Silicheva
mesh_terms: D000818:Animals; D015153:Blotting, Western; D001921:Brain / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000378:metabolism; D002458:Cell Fractionation; D002462:Cell Membrane / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D007150:Immunohistochemistry; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism; D007668:Kidney / Q000378:metabolism* / Q000648:ultrastructure*; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009928:Organ Specificity; D051381:Rats; D013091:Spermatogenesis; D013347:Subcellular Fractions / Q000378:metabolism*; D013737:Testis / Q000378:metabolism* / Q000648:ultrastructure*
chemical_list: D002148:Calmodulin-Binding Proteins; D003598:Cytoskeletal Proteins; D047908:Intracellular Signaling Peptides and Proteins; C000619712:Marcks protein, rat; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; C066853:Basp1 protein, rat