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

The correlations between the levels of various plasma proteins and lipids and platelet function on glass and platelet factor 3 (PF 3)-availability in children of different age-groups were investigated. Several statistically significant positive and some significant negative correlations were found. Although conclusions based solely on such correlations should be considered with reservation, in our opinion the following factors should stimulate platelet function: prealbumin (adhesion and PF 3-availability in all age-groups, aggregation--specifically for children in puberty); alpha 1-antitrypsin (PF 3-availability); alpha 2-macroglobulin (platelet spreading capacity, PF 3-availability); plasminogen (platelet adhesion and aggregation--specifically for boys in puberty); caeruloplasmin (number of "free adhering platelets" spreading capacity); lysolecithin and lecithin (time-dependent increase of spontaneous platelet adhesion and aggregation, PF 3-availability); and free fatty acids (FFA) (PF 3-availability). Plasminogen and complement component C'3 show a negative relationship to the time-dependent increase of spontaneous platelet adhesiveness and aggregability in platelet-rich plasma.
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PMID:Correlations between age-dependent protein and lipid concentrations in plasma and platelet functions in children. 9 14

The effect of clofibrate (1.5 g/day) on different plasma proteins and on components of the hemostatic system was studied in eight men with either mild diabetes mellitus or cardiosclerosis. Before treatment, the subjects were investigated weekly on five occasions. The means of these determinations were compared with the values observed after 2, 6 and 14 weeks of treatment. During the treatment albumin and transferrin increased significantly while orosomucoid, ceruloplasmin, beta1 E-globulin, IgA, IgM and fibrinogen decreased significantly. The decreases of the last proteins in per cent were found to be associated with each other in single subjects, i.e. a subject who reacted with a certain degree of change in one protein tended to react in a similar way with regard to the other proteins. A correlation was observed between the concentration before the treatment and the decrease in concentration during the treatment for ceruloplasmin, IgG, IgA, IgM and fibrinogen. The fibrinolytic activity increased significantly. Plasminogen decreased after 6 weeks and increased after 14 weeks of treatment. Platelet adhesiveness was not influenced.
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PMID:Effect of clofibrate on plasma proteins including components of the hemostatic mechanism. 13 Oct 8

Cryostat sections of normal human first-trimester placentae have been studied by indirect immunofluorescence to localize numerous protein antigens to well-defined anatomical regions. Transferrin was identified in the apical aspect of all trophoblasts. Fibrinogen/fibrin was also clearly demonstrated in speckled pattern in this location and similar reactions were also observed for alpha-2-macroglobulin, IgG and C3. Plasminogen was identifiable in trophoblasts, and beta-2-microglobulin was uniformly absent from these cells. Collagen and fibrinogen/fibrin were demonstrated on trophoblastic basement membrane, whereas IgG and C3 were only very rarely identified at this site. Few antisera gave strong staining of first-trimester villous stroma, although collagen was shown to contribute much of the stromal matrix. Fibrinogen/fibrin, plasminogen, alpha-2-macroglobulin, C4, C3, C1q, IgG and caeruloplasmin gave positive reactions in fibrin and fibrinoid areas, and phytohaemagglutinin was demonstrated to bind strongly to these areas as well as to trophoblastic basement membrane.
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PMID:Immunological studies of human placentae: identification and distribution of proteins in immature chorionic villi. 35 18

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