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1

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Identification of heparin-binding proteins in bovine seminal plasma (1990)

Chandonnet, L. ; Roberts, K. D. ; Chapdelaine, A. ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Molecular Reproduction and Development 26 (1990), S. 313-318

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ISSN: 1040-452X

Keywords: Affinity chromatography ; Glycosaminoglycans ; Proteins ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology

Notes: A group of four similar proteins, BSP-A1, BSP-A2, BSP-A3, and BSP-30-kDa, represent the major acidic proteins found in bovine seminal plasma (BSP). These proteins are secretory products of the seminal vesicles; they bind to spermatozoa upon ejaculation and could represent decapacitation factors. It has been shown that the glycosaminoglycans present in the female reproductive tract are involved in the capacitation of spermatozoa. Therefore, it was of interest to investigate whether BSP-A1, -A2, -A3, and -30-kDa proteins of bovine seminal fluid interact with heparin. Chromatography of alcohol precipitates of bovine seminal fluid on a heparin-Sepharose column resolved these proteins into three peaks. Peaks 1 and 2 (retarded proteins) were eluted upon extensive washing of the column with 0.05 M phosphate buffer, pH 7.4 (equilibrating buffer), and accounted for approximately 25% of the applied proteins. Proteins in peak 3 represented adsorbed proteins and were eluted with phosphate buffer containing 1 M NaCl. Proteins in each peak were characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. Peak 1 contained proteins with molecular weights ranging from 8 to 350 kDa, peak 2 contained a single protein with a molecular weight of 14 kDa, and peak 3 contained proteins with molecular weights of 15.5, 16, 25, and 30 kDa. The proteins in peak 3 were further resolved into unadsorbed (peak 4) and adsorbed (peak 5) proteins on a gelatin-Agarose column. Separation of the proteins of peak 3 and peak 5 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and reducing agents followed by transfer to nitrocellulose and probing with antibodies against the previously well-characterized BSP proteins indicated the presence of BSP-A1, BSP-A2, BSP-A3, and BSP-30-kDa proteins. These results demonstrate that BSP-A1, -A2, -A3, and -30-kDa proteins bind to heparin or glycosaminoglycans and we postulate interaction of these spermatozoa-bound proteins with glycosaminoglycans in the female reproductive tract.

Additional Material: 4 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/mrd.1080260404

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Prostatic epithelial cells in culture: Phosphorylation of protein tyrosyl residues and tyrosine protein kinase activity (1991)

Bourassa, C. ; Nguyen, L. T. ; Durocher, Y. ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 46 (1991), S. 291-301

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ISSN: 0730-2312

Keywords: protein phosphorylation ; phosphotyrosine ; phosphotyrosyl protein phosphatase ; orthovanadate ; cell proliferation ; canine prostate ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: The ability of dividing canine prostatic epithelial cells in primary monolayers to phosphorylate protein tyrosyl residues was evaluated by metabolic studies performed through incorporation of [32P]-phosphate into alkali-resistant phosphoproteins and by the assay of their tyrosine protein kinase activity. The presence of sodium orthovanadate during cell incubation with [32P]-phosphate greatly enhanced the relative labelling intensity of a 44 kDa alkali-resistant phosphoprotein and the total cellular content of phosphotyrosine in proteins; in this respect, growth factors such as epidermal growth factor, insulin, and insulin-like growth factor I, and the steroids dihydrotestosterone and estradiol were inactive. When the cells were solubilized, sodium orthovanadate stimulated their tyrosine protein kinase activity and inhibited their phosphotyrosine phosphatase activity. To characterize the tyrosine protein kinase of these cultured cells, conditions for optimal activity were established using the substrate poly [Glu80Na, Tyr20]. The subcellular localization of the enzyme was determined upon cell fractionation: 88% of the kinase activity was associated with the particulate fraction and 30% of this activity was partially solubilized with 0.5% Triton X-100; this solubilization was improved to 83% in the presence of 0.25 M KCl. The enzyme directly solubilized from prostatic cells with Triton X-100 (38% of activity) mainly catalyzed the alkali-resistant phosphorylation of pp63, pp59, and pp44, which contained phosphotyrosine. These proteins were also phosphorylated by the major peak of kinase activity which was eluted at an apparent molecular weight of 300-350 kDa upon gel filtration. On a cell basis, the kinase activity was four- to eleven-fold higher in the dividing epithelial cells in culture compared to quiescent secretory and non-secretory epithelial cells, freshly isolated from dog prostates. It is proposed that this tyrosine protein kinase is implicated in the regulation of the proliferation of prostatic epithelial cells.

Additional Material: 6 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/jcb.240460404

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Die Cardenolide der Samen von Mallotus paniculatus MÜLL.-ARG. (Euphorbiaceae). 2. Mitt.: Strukturbeweise. Glykoside und Aglykone, 295. Mitteilung294. Mitteilung vgl. Reichstein et al. [1]. (1967)

Roberts, K. D. ; Weiss, Ek. ; Reichstein, T.

New York, NY : Wiley-Blackwell

Helvetica Chimica Acta 50 (1967), S. 1645-1664

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ISSN: 0018-019X

Keywords: Chemistry ; Organic Chemistry

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: The structures of the following cardenolides, isolated from Mallotus paniculatus have been reported: Genin D = 11-oxo-uzarigenin (1), genin F = mallogenin = 11β-hydroxy-uzarigenin (3). Glycoside K = mallosid (5) is an L-rhamnoside of mallogenin, and glycoside L (21) is an L-rhamnoside of a new genine which we have called panogenin. Panogenin was isolated in crystalline form by the hydrolysis of panoside, and its structure was found to be that of 11β-hydroxy-coroglaucigenin (23). Glycoside N = glucopanoside (22), the predominant glycoside of the unfermented seeds, was found to contain one molecule of D-glucose bound in glycosidic form; its position was not investigated.

Additional Material: 18 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/hlca.19670500624

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Die Cardenolide der Samen von Mallotus philippinensis (LAM.) MÜLL.-ARG. (= Rottlera tinctoria ROXB.)Herrn. Prof. K. BERNHARD zu seinem 60. Geburtstag gewidmet.. Glykoside und Aglykone, 252. Mitteilung (1963)

Roberts, K. D. ; Weiss, Ek. ; Reichstein, T.

New York, NY : Wiley-Blackwell

Helvetica Chimica Acta 46 (1963), S. 2886-2893

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ISSN: 0018-019X

Keywords: Chemistry ; Organic Chemistry

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: The seeds of Mallotus philippinensis (Lam.) Muell.-Arg. were found to contain 4 cardenolides (A, B, C and D) after fermentation. Two new glycosides, C and D, were obtained in crystalline form and were shwon to be corotoxigenin-rhamnoside and coroglaucigenin-rhamnoside respectively. The minor constituents A and B were identified as corotoxigenin and coroglaucigenin after paper chromatography.

Additional Material: 3 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/hlca.19630460745

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Evidence for two forms of phospholipase A2 in human semen (1988)

Antaki, P. ; Langlais, J. ; Ross, P. ; [et al.]

New York, NY : Wiley-Blackwell

Gamete Research 19 (1988), S. 305-314

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ISSN: 0148-7280

Keywords: radiation inactivation ; spermatozoa ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology

Notes: The molecular weight of the active unit of phospholipase A2 (PA2) in human seminal plasma and spermatozoa was determined using the radiation inactivation technique. Fresh spermatozoa possess more than one form of PA2 activity as judged by the biphasic nature of the curve obtained during enzyme inactivation. However, when stored frozen for several months followed by a period of heating for 60 min at 60 °C prior to irradiation, the sperm exhibited PA2 activity, which corresponded to a single low molecular mass form of 12,000 d when radioactive phosphatidylcholine (PC) was used as substrate and 8,000 d when radioactive phosphatidylethanolamine (PE) was used as substrate. In fresh seminal fluid, only one active form of PA2 was detected as judged by the linear nature of the curve obtained during enzyme inactivation by irradiation. Using PC as substrate, the active unit was again estimated to be 12,000 d, whereas it corresponded to 18,000 d when PE was used. The PA2 activity associated with normal spermatozoa exhibited a 60% decrease in activity after storage at -20 °C for 48 hr followed by a heating period of 10 min at 60 °C. Long-term storage of spermatozoa at -20 °C also resulted in a similar decrease in the deacylation of PC. No further loss of activity was observed during subsequent heat treatment at 60 °C. Seminal plasma, however, showed no loss of activity following short (48 hr at 4 °C or -20 °C) or long-term storage and subsequent heat treatment. Thus, the behavior of PA2 when the effect of temperature was studied and in radiation inactivation experiments indicates that the low molecular weight component in the seminal plasma as well as in spermatozoa is temperature resistant. However, in fresh spermatozoa, a second form of PA2 was found and was sensitive to changes in temperature.

Additional Material: 5 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/mrd.1120190309

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Identification of sterol acceptors that stimulate cholesterol efflux from human spermatozoa during in vitro capacitation (1988)

Langlais, J. ; Kan, F. W. K. ; Granger, L. ; [et al.]

New York, NY : Wiley-Blackwell

Gamete Research 20 (1988), S. 185-201

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ISSN: 0148-7280

Keywords: acrosome reaction ; fertilization ; lipoproteins ; lipids ; albumin ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology

Notes: The nature of cholesterol-binding proteins acting upon human spermatozoa during in vitro capacitation was determined by measuring the efflux of [3H]cholesterol and of [3H]cholesteryl sulfate from labeled spermatozoa. Efflux of [3H]sterols was stimulated when the labeled gametes were incubated in Ham's F-10 medium supplemented with female serum or follicular fluid. Upon centrifugation of capacitated spermatozoa and application of the supernatant to density-gradient ultracentrifugation for lipoprotein analysis, both [3H]cholesterol and [3H]cholesteryl sulfate were found to be carried by very-low-density lipoproteins (VLDL), low-density lipoproteins (VLDL), high-density lipoproteins (HDL), as well as the albumin fraction (d 〉 1.21) in serum. When the capacitation medium was supplemented with follicular fluid, the [3H]sterols were bound to HDL's and to the albumin fraction; when the latter fraction was analysed by molecular sieve chromatography, 60-70% of the radioactivity eluted in fractions with a mean molecular weight corresponding to that of human serum albumin. Sperm cholesterol efflux was also stimulated when serum or follicular fluid was added to a simplified medium (50 mM Tris-HCl, 0.56% NaCl, pH 7.8); efflux of [3H]cholesterol from labeled gametes progressed in a time-dependent manner, but was low in the absence of serum components. The [3H]cholesterol/cholesterol ratios were higher in the albumin and HDL fractions, indicating some degree of specificity of these sterol acceptors. It was observed that follicular fluid albumin has a [3H]sterol binding capacity that is 2 - 3-fold higher than that of serum albumin. Commercial human serum albumin also promoted sperm cholesterol efflux. These results provide new information concerning those components of follicular fluid which may play a role in human sperm capacitation and provide further support for the concept that loss of cholesterol from the sperm plasma membrane is an important component of the capacitation process.

Additional Material: 6 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/mrd.1120200209

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