Micro two‐dimensional gel electrophoresis of serum and testis esterases from different strains of mice

Abou-Haïla, A

doi:10.1002/elps.1150110213

Cited by 7 publications

(3 citation statements)

References 34 publications

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“…The co-migrating molecular forms of esterases common to serum, testicular (cf. Abou-Haila & Fain-Maurel, 1990) and epididymal fluids exhibited a comparable response to inhibitors and neuraminidase treatment.…”

Section: Androgen Selective Action On Esterase Varients 215mentioning

confidence: 90%

“…Comparative analysis of the molecular forms of esterases in the inbred line C57BL/ 6J and the natural population Swiss OF1 showed only that the two more acidic spots (pH 3.9), which co-migrated with serum and testicular components, moved farther in the epididymis and vas deferens in C57BL/6J than in Swiss OF, mice (Abou-Haila & Fain-Maurel, 1990).…”

Section: Androgen Regulation Of Esterases In the Epididymis And Vas Dmentioning

confidence: 93%

“…Two-dimensional gel electrophoresis was performed with the PhastSystem under non-denaturing conditions as detailed previously (Abou-Haila & Fain-Maurel, 1990). Isoelectric focusing (IEF) in the first dimension was carried out on PhastGel (50 x 43 x 0.35 mm) in an IEF media (5% T, 3% C) of pH range 3-9 (Pharmacia).…”

Section: Two-dimensional Gel Electrophoresismentioning

confidence: 99%

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Selective action of androgens on the molecular forms of esterases characterized by two‐dimensional gel electrophoresis in the epididymis and vas deferens of the mouse

Abou-Haïla¹

1991

Int J of Andrology

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Molecular forms of esterases were resolved in non-denaturing conditions by using two-dimensional gel electrophoresis with isoelectric focusing in the first dimension and a time-dependent polyacrylamide gradient gel electrophoresis (PAGGE) in the second dimension. This procedure was used to analyse sequential changes in esterase composition along the excurrent genital duct of the mouse and to initiate a specific identification of the androgen-regulated molecular forms. Almost all the 68 variants (pH 3.9-6.4 and 50-300 kDa) revealed by alpha-naphtyl acetate from the fluids of the three parts of the epididymis (caput, corpus, cauda) and vas deferens, could be assigned to the carboxylesterase group as shown by their action on various substrates and sensitivity to inhibitors. Some of these variants co-migrated with those in the serum and testis, whereas other enzyme forms made their first appearance in the caput (13), in the corpus (26) and in the vas deferens (3). The major changes occurred between the caput and the corpus of the epididymis. Only a few acidic spots were not revealed after neuraminidase digestion. Castration of mice (4 weeks) resulted in inhibition of the activity of 34 esterase forms, and thus abolished most of the regional differences in the excurrent duct system. By re-initiating or repressing the synthesis of regional esterase variants, testosterone supplementation (2 and/or 4 weeks) of castrated animals restored the normal esterase pattern in the three epididymal parts, but not in the vas deferens. The major effect of efferent duct ligation (4 weeks) was the emergence in the corpus and cauda of the epididymis of two variants found in the caput of uncastrated mice.

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Section: Androgen Selective Action On Esterase Varients 215mentioning

confidence: 90%

Section: Androgen Regulation Of Esterases In the Epididymis And Vas Dmentioning

confidence: 93%

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Selective action of androgens on the molecular forms of esterases characterized by two‐dimensional gel electrophoresis in the epididymis and vas deferens of the mouse

Abou-Haïla¹

1991

Int J of Andrology

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Androgen Regulation of Molecular Forms of β‐D‐Glucuronidase in the Mouse Epididymis: Comparison With Liver and Kidney

ABOU‐HAILA,

TULSIANI,

SKUDLAREK

et al. 1996

Journal of Andrology

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The expression and androgen regulation of β‐glucuronidase molecular forms were examined in mouse epididymis, liver, and kidney. Two‐dimensional polyacrylamide gel electrophoresis performed under nondenaturing conditions showed that, compared to liver and kidney, which contain four microsomal (M1‐M4) and a major lysosomal (L) form of β‐glucuronidase, the epididymis revealed regional differences and tissue specificity in the expression of the various molecular forms of the enzyme. Only the lysosomal form (pl 5.4–6.1) is present in the caput epididymidis while the corpus/cauda contains the lysosomal form, the free X form (pl 5.9‐6.3) and the four microsomal forms (X form complexed with egasyn). Mutant mice that lack egasyn have no microsomal forms in the distal epididymis. In epididymal fluid, the lysosomal form is found throughout the epididymis, whereas the X form appears only in the corpus/cauda epididymidis. Sodium dodecyl Sulfate (SDS)‐gel electrophoresis and western blot analysis of immunoprecipitated β‐glucuronidase revealed only one band corresponding to the L form (apparent molecular weight 74 kDa) in the caput epididymidis and two bands in the corpus/cauda (apparent molecular weights 73 and 75 kDa), corresponding to L and X forms, respectively. Castration of mice led to the suppression of the regional differences in the appearance of X and M forms in the epididymis. Testosterone supplementation to castrated mice restored the characteristic electrophoretic pattern of β‐glucuronidase in the caput epididymidis. In the liver and kidney, castration has no effect on the expression of the molecular forms, whereas androgen treatment induced the X form in the kidney. Histochemical localization of β‐glucuronidase confirmed the region specificity seen in the epididymis and in addition revealed cell specificity in the expression of β‐glucuronidase. These results indicate that β‐glucuronidase shows tissue specificity and, in the case of the epididymis, region and cell specificity. In addition, the enzyme in the different tissues responds differentially to androgens.

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Mannopeptimycins, a novel class of glycopeptide antibiotics active against gram-positive bacteria

2005

Appl Microbiol Biotechnol

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Mannopeptimycins alpha-epsilon, novel glycopeptides with activity against methicillin-resistant staphylococci and vancomycin-resistant enterococci, are purified from the fermentation broth of a strain of Streptomyces hygroscopicus, LL-AC98, and their structures characterized using spectroscopic analyses and chemical methods. The SAR data of the natural and synthetic esters demonstrate that the presence of hydrophobic groups near the terminal mannosyl moiety is critical for antibacterial potency. Scalable syntheses of 4,6-cyclic acetals and ketals on this moiety are used to produce significant quantities of the respective mannopeptimycin derivatives. These acetal and ketal derivatives exhibit potent activities against susceptible and resistant Gram-positive bacteria in both in vitro and in vivo experiments, comparable with or exceeding the activity of vancomycin. Studies on the mechanism of action suggest that the mannopeptimycins interfere with the late stages of bacterial cell wall biosynthesis. It is believed that these antibiotics inhibit the transglycosylation by binding to the transglycosylase substrate, lipid II.

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Micro two‐dimensional gel electrophoresis of serum and testis esterases from different strains of mice

Cited by 7 publications

References 34 publications

Selective action of androgens on the molecular forms of esterases characterized by two‐dimensional gel electrophoresis in the epididymis and vas deferens of the mouse

Selective action of androgens on the molecular forms of esterases characterized by two‐dimensional gel electrophoresis in the epididymis and vas deferens of the mouse

Androgen Regulation of Molecular Forms of β‐D‐Glucuronidase in the Mouse Epididymis: Comparison With Liver and Kidney

Mannopeptimycins, a novel class of glycopeptide antibiotics active against gram-positive bacteria

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