Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The influence of rat round spermatid protein(s) (RSP) on protein synthesis and secretory function of Sertoli cells was used in the bicameral chamber system. Round spermatids (RS) were purified from 90-day-old rats by centrifugal elutriation. RS were incubated in a supplement-enriched culture medium that lacked exogenous proteins. The RS-conditioned media were dialysed and lyophilized to obtain RSP. Most de novo protein synthesized under basal conditions by Sertoli cells (18-day-old) was secreted into the apical chamber (apical/basal ratio: 3.42). Follicle-stimulating hormone (FSH, 100 ng/ml) stimulated total protein secretion from Sertoli cells by a factor of 1.54. The RSP (100 micrograms/ml) stimulated total protein secretion from Sertoli cells by a factor of 2.33. The enhancement of total Sertoli cell protein secretion by FSH and RSP additively increased by a factor of 2.82. The combined effect of FSH and RSP on total protein secretion from Sertoli cells was dose dependent and saturated at approximately 200 micrograms/ml of RSP. Polarity of total protein secretion from Sertoli cells (apical/basal ratio: 3.42) was stimulated by RSP predominantly in the apical direction (apical/basal ratio: 8.48). The modulation of radiolabeled Sertoli cell secretory proteins (ceruloplasmin, CP; sulfated glycoprotein-2, SGP-2; testins and transferrin, Tf) by cold (non-labeled) RSP was investigated by immunoprecipitation followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The secretion of CP, SGP-2 and Tf was stimulated in a dose-dependent manner by the addition of RSP up to a saturating concentration of between 200 and 300 micrograms/ml, whereas the secretion of Sertoli cell testins did not reach saturation at 300 micrograms/ml RSP. These results indicate that FSH and RSP independently modulate Sertoli cell protein secretion, and that Sertoli cell secretory proteins may differentially respond to RSP stimulation.
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PMID:Modulation of Sertoli cell secretory function by rat round spermatid protein(s). 212 59

As was stated in the introduction, many of the functions of the Sertoli cells are apparently carried out by the protein secretions of these cells. The use of Sertoli cell cultures and appropriate biochemical and immunological techniques has allowed the characterization of some of these secretion products. It is likely that many of the functions of the Sertoli cells are necessary because of the presence of the blood-testis barrier. Many growth and nutritive factors which are necessary for cell viability are available to most cells via the serum. The germinal cells within the adluminal compartment do not have access to serum factors and one of the functions of the Sertoli cells is to synthesize serum-like components and secrete them into the adluminal compartment. The historical description of Sertoli cells as "nurse cells" thus appears to have been accurate. The nurse-cell function is most clearly demonstrated by the proposed mechanism by which germinal cells obtain ferric ions. The Sertoli cells have developed a system to move serum-derived iron through their own cytoplasm and to secrete it bound to newly synthesized testicular transferrin molecules which can deliver it to specific receptors on the germinal cell surface (Huggenvik et al., 1984). Functionally, all of the secreted proteins from Sertoli cells which have been characterized or proposed fall into one of five basic classes. First, Sertoli cells secrete a number of transport proteins including transferrin, ceruloplasmin, and ABP. The proposed function of these proteins is the transport of Fe3+, Cu2+, and androgens to the germinal cells or to the epididymis (ABP). Second, Sertoli cells synthesize and secrete a number of proteins which have a hormone-like or growth factor-like activity. AMH is a clear and well-documented example of this type of product while the evidence for inhibin, somatomedin C, EGF-like growth factor, and seminiferous growth factor will require further corroboration. Third, Sertoli cells secrete proteins which have enzymatic activities. Plasminogen activator is the best characterized example of this class of products and the alpha-lactalbumin-like activity is of potential interest. The fourth class of Sertoli cell secretion products includes those proteins which contribute to the basement membrane, namely, type IV collagen and laminin. Finally, there is a very important group of Sertoli cell secretion products for which there is, as yet, no evidence for a defined function. This group includes SGP-1 and SGP-2 which are the major sertoli cell products in rats and which have been well-characterized biochemically.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Protein secretions of Sertoli cells. 305 98