Zinc and carbonic anhydrase in human semen

Mawson, C. A.; Fischer, Michael

doi:10.1042/bj0550696

Cited by 119 publications

(51 citation statements)

References 14 publications

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“…The predominance ofprostatic secretory components in their ejaculates was verified by the very high concentration ofzinc (24) and PSA (25). The lack ofsecretory components originating from the seminal vesicles and the ampullae was evidenced by subnormal ejaculate volumes, extremely low fructose levels (26), absence of the normal basic fragments of semenogelin on agarose gel electrophoresis (2), and only traces ofimmunoreactive lactoferrin (1 1).…”

Section: Discussionmentioning

confidence: 99%

Seminal vesicle-secreted proteins and their reactions during gelation and liquefaction of human semen.

Lilja¹,

Oldbring²,

Rannevik³

et al. 1987

J. Clin. Invest.

328

105

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The comparison of measurements of fibronectin and lactofem in ejaculates from vasectomized men, subjects with functional deficiency or aplasia of the seminal vesicies, and reference subjects provided evidence that both the fibronectin and the lactoferrin in human seminal fluid originate from the seminal vesicles and the ampullae.The fibronectin is incorporated in the framework of the seminal gel formed during the immediate postejaculatory phase, whereas the lactoferrin remains in solution. In the seminal gel fibronectin is linked to its predominant structural protein, a high molecular weight seminal vesicle protein (semenogelin). Both the gel-bound fibronectin and semenogelin are progressively fragmented and solubilized by the abundant prostatic kallikreinlike protease (prostate-specific antigen) during and after seminal gel liquefaction. Lactoferrin remains essentially unaffected by the seminal proteases.

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Section: Discussionmentioning

confidence: 99%

Seminal vesicle-secreted proteins and their reactions during gelation and liquefaction of human semen.

Lilja¹,

Oldbring²,

Rannevik³

et al. 1987

J. Clin. Invest.

328

105

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“…Nothing is known about the mechanism of zinc uptake and homeostasis in N. gonorrhoeae. During the transmission of gonorrhea from men to women, gonococci are exposed to the high zinc concentrations that are present in semen [2,14]. The zinc concentration in seminal £uid has been reported to be greater than 53 Wg ml 31 [15], which is potentially toxic to the gonococcus, and 37 times greater than that found in serum (0.9^1.4 Wg ml 31 ) [14].…”

Section: Introductionmentioning

confidence: 99%

“…During the transmission of gonorrhea from men to women, gonococci are exposed to the high zinc concentrations that are present in semen [2,14]. The zinc concentration in seminal £uid has been reported to be greater than 53 Wg ml 31 [15], which is potentially toxic to the gonococcus, and 37 times greater than that found in serum (0.9^1.4 Wg ml 31 ) [14]. Most of the zinc in serum is bound to proteins such as albumin and K 2 -macroglobulin [2,15,16].…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of a high-affinity zinc uptake system in Neisseria gonorrhoeae

Chen

2001

FEMS Microbiology Letters

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A search of the gonococcal genome database using the known zinc-binding protein (znuA) sequences from Escherichia coli and Haemophilus influenzae identified an open reading frame encoding a putative gonococcal ZnuA. The consensus amino acid sequence of this open reading frame possessed a characteristic 30-amino acid histidine-rich metal-binding motif (repetitive HDH sequence) containing 43% histidine and 37% aspartic acid and glutamic acid. Subsequently, two adjacent open reading frames with homology to E. coli and H. influenzae znuB and znuC were located upstream of znuA. When partially purified from sonicated cell-free supernatants by CMSepharose chromatography, the mature gonococcal ZnuA had an estimated molecular mass of 38 kDa by SDS^PAGE. The presence of a DNA sequence encoding a 19-amino acid signal peptide and the solubility of the mature ZnuA suggested that this protein was located in the periplasm. Inactivation of the Neisseria gonorrhoeae F62 znuA by insertional mutagenesis resulted in a mutant that had a growth rate lower than that of the wild-type parent strain and that required high concentrations of ZnCl 2 (v200 WM) for optimal growth. Using a chemically defined agar medium, the gonococcal ZnuA mutant grew only in the presence of Zn 2 , whereas Mg

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“…Omission of EDTA from the reaction m ixture decreased the activity of seminal glutathione reductase by 50% or more. This metal chelating agent was added to complex with zinc, since the concentration of this m etal in hum an semen is large (34), and glutathione reductase is extremely sensitive to the inhibitory action of Z n++ ions (35). Variations in the zinc content of the seminal plasm a m ay be partially responsible for the very wide range of values observed for glutathione reductase activity.…”

Section: Patients From Fertility Clinicmentioning

confidence: 99%