Seminalplasmin

Sitaram, N.; Nagaraj, Ramakrishnan

doi:10.1002/bies.950170509

Cited by 18 publications

(9 citation statements)

References 57 publications

(46 reference statements)

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“…The identified peptide sequences were included in both sequences indicated (bold type), and the sequence coverage is expressed as a percentage. environment suitable for the protection of spermatozoa production and integrity [2,3,28,29]. In the last 4 yr, a major reawakening of interest in this area has resulted in the publication of a number of papers suggesting that the male genital tract is a potential source of original and specific microbicidal molecules involved in host defense [30].…”

Section: Discussionmentioning

confidence: 99%

Involvement of Semenogelin-Derived Peptides in the Antibacterial Activity of Human Seminal Plasma1

Bourgeon

Evrard

Brillard-Bourdet

et al. 2004

Biology of Reproduction

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Mechanisms for protecting spermatozoa, and the testes that produce them, from infection are essential, given the importance of these cells and organs for the fertility of the individual and perpetuation of the species. This is borne out by the publication of numerous papers on this subject over the last 50 years. We extended our work and that of others on the anti-infectious defense system of the male genital tract, using a new strategy for the direct identification of antibacterial molecules in human seminal plasma. We subjected a liquefied seminal plasma cationic fraction to reversed-phase HPLC, monitored microbicidal activity by gel overlay and radial diffusion assays, and identified the proteins and/or peptides present in each active fraction by mass spectrometry. In addition to proteins with known potent microbicidal activity--phospholipase A2, lactoferrin, and lysozyme--we also found that peptides produced by cleavage of semenogelin I, the predominant human semen coagulum protein, had high levels of antibacterial activity.

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Section: Discussionmentioning

confidence: 99%

Involvement of Semenogelin-Derived Peptides in the Antibacterial Activity of Human Seminal Plasma1

Bourgeon

Evrard

Brillard-Bourdet

et al. 2004

Biology of Reproduction

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“…This structure, attained either by the formation of K-helix or L-pleated conformation, enables them to form ion channels or aqueous pores in the membrane. These groups of peptides, such as cecropins [16], magainins [17], seminalplasmin [14,18] and defensins [19], have been extensively studied and the killing mechanism for majority of these peptides shown to be an attack on the outer and cytoplasmic membranes leading to lysis of the target cells. PRrich peptides represent a variation in this general theme and these peptides do not kill bacteria by lysis.…”

Section: Discussionmentioning

confidence: 99%

Mechanism of antimicrobial action of indolicidin

Subbalakshmi¹

1998

FEMS Microbiology Letters

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Indolicidin, a 13-residue antimicrobial peptide isolated from cytoplasmic granules of bovine neutrophils, exhibits activity against Gram-positive and Gram-negative bacteria as well as fungi. Although indolicidin is bactericidal and permeabilizes the bacterial membranes, it does not lyse the bacterial cells. We examined the effect of bactericidal concentrations of indolicidin on the morphology of Escherichia coli cells and found that it induces filamentation. Further investigations showed that indolicidin inhibits DNA synthesis in E. coli cells at concentrations at which RNA and protein synthesis are either partially affected or not affected at all. Since inhibition of DNA synthesis is also known to induce filamentation in E. coli, it appears to contribute to the antimicrobial activity of indolicidin. z 1998 Published by Elsevier Science B.V.

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“…The unequivocal demonstration of the presence of a small molecular weight, non-enzymatic protein in bovine seminal fluid came from the isolation and characterization of seminal plasmin (SPLN), a 47-residue peptide [3][4][5]. Antibacterial peptides have been shown to play an important role in the innate immunity of many animal species [6].…”

Section: Introductionmentioning

confidence: 99%

Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin

et al. 1997

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Seminalplasmin (SPLN) is a 47-residue protein isolated from bovine seminal plasma having potent antimicrobial activity against a broad spectrum of microorganisms. SPLN, also known as caltrin, acts as a calcium transport regulator in bovine sperms. Analysis of the sequence of SPLN reveals a 27-residue stretch with the sequence SLSRYAKLANRLANPKL-LETFLSKWIG more hydrophobic than the rest of the protein. It is demonstrated that a synthetic peptide corresponding to this 27-residue segment has antimicrobial activity comparable to that of SPLN. It does not exhibit hemolytic activity at concentrations where antibacterial activity is observed. Since P27 can be conveniently obtained in large amounts by chemical synthesis, it could serve not only as a starting compound to obtain peptides with improved antibacterial activity but also to understand the role of SPLN in reproductive physiology.

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Seminalplasmin

Cited by 18 publications

References 57 publications

Involvement of Semenogelin-Derived Peptides in the Antibacterial Activity of Human Seminal Plasma1

Involvement of Semenogelin-Derived Peptides in the Antibacterial Activity of Human Seminal Plasma1

Mechanism of antimicrobial action of indolicidin

Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin

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