https://www.hal.inserm.fr/inserm-00353462/document

Progress in developing cationic vectors for non-viral systemic gene therapy against cancer.

Protamines are the major nuclear sperm proteins. The human sperm nucleus contains two types of protamine: protamine 1 (P1) encoded by a single-copy gene and the family of protamine 2 (P2) proteins (P2, P3 and P4), all also encoded by a single gene that is transcribed and translated into a precursor protein. The protamines were discovered more than a century ago, but their function is not yet fully understood. In fact, different hypotheses have been proposed: condensation of the sperm nucleus into a compact hydrodynamic shape, protection of the genetic message delivered by the spermatozoa, involvement in the processes maintaining the integrity and repair of DNA during or after the nucleohistone-nucleoprotamine transition and involvement in the epigenetic imprinting of the spermatozoa. Protamines are also one of the most variable proteins found in nature, with data supporting a positive Darwinian selection. Changes in the expression of P1 and P2 protamines have been found to be associated with infertility in man. Mutations in the protamine genes have also been found in some infertile patients. Transgenic mice defective in the expression of protamines also present several structural defects in the sperm nucleus and have variable degrees of infertility. There is also evidence that altered levels of protamines may result in an increased susceptibility to injury in the spermatozoan DNA causing infertility or poor outcomes in assisted reproduction. The present work reviews the articles published to date on the relationship between protamines and infertility.

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Protamines and male infertility.

The Amino Acid Sequence of Egg White Lysozyme

Saponins occur widely in plant species and exhibit a range of biological properties, both beneficial and deleterious. This review, which covers the literature to mid 1986, is concerned with their occurrence in plants and their effects when consumed by animals and man. After a short discussion on the nature, occurrence, and biosynthesis of saponins, during which the distinction between steroidal and triterpenoid saponins is made, the structures of saponins which have been identified in a variety of plants used as human foods, animal feedingstuffs, herbs, and flavorings are described. Many of these compounds have been characterized only during the last 2 decades, and modern techniques of isolation, purification, and structural elucidation are discussed. Particular consideration is given to mild chemical and enzymatic methods of hydrolysis and to recent developments in the application of NMR and soft ionization MS techniques to structural elucidation. Methods currently used for the quantitative analysis of saponins, sapogenols, and glycoalkaloids are critically considered; advances in the use of newer methods being emphasized. The levels of saponins in a variety of foods and food plants are discussed in the context of the methods used and factors affecting these levels, including genetic origin, agronomic, and processing variables, are indicated. Critical consideration is given to the biological effects of saponins in food which are very varied and dependent upon both the amount and chemical structure of the individual compounds. The properties considered include membranolytic effects, toxic and fungitoxic effects, adverse effects on animal growth and performance, and the important hypocholesterolemic effect. A final section deals briefly with the pharmacological effects of saponins from ginseng, since use of this plant is increasing in certain sections of western society as well as being traditional in the Orient.

The chemistry and biological significance of saponins in foods and feedingstuffs.

The protamines are a diverse family of small arginine-rich proteins that are synthesized in the late-stage spermatids of many animals and plants and bind to DNA, condensing the spermatid genome into a genetically inactive state. Vertebrates have from one to 15 protamine genes per haploid genome, which are clustered together on the same chromosome. Comparison of protamine gene and amino-acid sequences suggests that the family evolved from specialized histones through protamine-like proteins to the true protamines. Structural elements present in all true protamines are a series of arginine-rich DNA-anchoring domains (often containing a mixture of arginine and lysine residues in non-mammalian protamines) and multiple phosphorylation sites. The two protamines found in mammals, P1 and P2, are the most widely studied. P1 packages sperm DNA in all mammals, whereas protamine P2 is present only in the sperm of primates, many rodents and a subset of other placental mammals. P2, but not P1, is synthesized as a precursor that undergoes proteolytic processing after binding to DNA and also binds a zinc atom, the function of which is not known. P1 and P2 are phosphorylated soon after their synthesis, but after binding to DNA most of the phosphate groups are removed and cysteine residues are oxidized, forming disulfide bridges that link the protamines together. Both P1 and P2 have been shown to be required for normal sperm function in primates and many rodents.

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The protamine family of sperm nuclear proteins

It was proved that the genuine sapogenin of ginsenosides-Rb1, -Rb2, and -Rc, saponins of Ginseng roots, was represented by protopanaxadiol (IVa), and panaxadiol (I) was an artifact formed during the process of the acid hydrolysis of these saponins.

Chemical Studies on Oriental Plant Drugs. XIV. Protopanaxadiol, a Genuine Sapogenin of Ginseng Saponins

A new method for fractionation of protamines and the amino acid sequences of salmine and three components of iridine.

I Introduction.- (Accompanied by a Select Bibliography on Protamines, Histones, and Nucleoproteins).- II Distribution of Nucleoprotamines and Protamines.- III Preparation of Nucleoprotamines and Protamines.- A. Isolation of Sperm Heads.- 1. Outline of the "Classical" Procedure of Kossel.- 2. Isolation of Sperm Heads by Fractional Centrifugation in Isotonic Salt Solution.- 3. "Plasmolysis" Procedure of Felix.- 4. Isolation of Sperm Heads and/or Cell Nucleus Fraction or Chromatin from Fish Testes during Spermatogenesis.- B. Isolation and Purification of Nucleoprotamine.- C. Separation and Purification of Protamines from Sperm Heads or Nucleoprotamine.- 1. Classical Procedures.- a) Extraction with Dilute Mineral Acid.- b) Extraction with Aqueous Cupric Salt.- c) Further Purification of Protamine Preparations.- 2. Modern Improvements to Classical Procedures.- 3. Some Remarks on the Methods of Preparation of Whole Protamines.- IV Composition.- A. Composition of Nucleoprotamines.- 1. Composition of Sperm Head or Sperm Nucleus.- 2. Composition of Reconstituted Nucleoprotamine.- 3. Composition of Artificial Nucleoprotamines.- 4. Base Composition of Deoxyribonucleic Acid Associated with Protamine.- B. Composition of Unfractionated (or Whole) Protamines.- 1. Classification of Protamines.- 2. Ratio of Carbon to Nitrogen in Protamine.- 3. Amino-Acid Composition.- V Molecular Weight.- A. Nucleoprotamines.- B. Protamines (Whole or Unfractionated).- VI Chemical Structure of Nucleoprotamines and Protamines.- A. Nucleoprotamines.- B. Protamines (Whole or Unfractionated).- 1. Amino-Terminal Residue and Sequence.- 2. Carboxyl-Terminal Residue and Sequence.- 3. Amino-Acid Sequences of Peptides Obtained by Partial Hydrolysis - Hypothetical Structures of Whole Protamines.- VII Heterogeneity of Protamines and Homogeneous Molecular Species of Protamines.- A. Heterogeneity in Protamines.- B. Preparative Fractionation of Protamines into Their Components.- 1. Fractionation of Whole Clupeine into Y and Z Fractions by Column Chromatography on Buffered Alumina (Homogeneous Clupeine Z).- 2. Fractionation of Whole Clupeine into Y and Z Fractions by Column Chromatography on CM-Cellulose (Homogeneous Clupeine Z).- 3. Fractionation of Trinitrophenylated (TNP-) Whole Clupeine into TNP-YI, TNP-Z and Free YII Components by Column Chromatography on CM-Cellulose (Homogeneous TNP-Clupeine YI, TNP-Clupeine Z and Free Clupeine YII).- 4. Fractionation of Whole Clupeine into Its Three Components, YI, YII and Z, and of Whole Salmine and Iridine into Some of Their Components by One-Step Elution Chromatography on a Column of CM-Sephadex or Bio-Gel CM (Homogeneous Clupeine YI, YII and Z Homogeneous Salmine AI, Iridine I and II).- 5. Fractionation of Whole Thynnine into Four Fractions, Y1, Y2, Zl and Z2, by Chromatography on a Column of CM-Sephadex (Homogeneous Thynnine Y1, Y2, Zl and Z2).- 6. Fractionation of Whole Galline into Several Components by Column Chromatography on Bio-Gel CM-30.- 7. Isolation and Partial Characterization of a Basic Protein from Bull Sperm Heads.- VIII Chemical Structure of Homogeneous Molecular Species of Protamines.- A. Determination of the Complete Amino-Acid Sequence of Clupeine Z.- 1. Amino-Acid Composition, Amino Terminus, and Molecular Weight.- 2. Analysis of Tryptic Peptides of Clupeine Z, Leading to a Partial Chemical Structure.- 3. Application of N?O Acyl Rearrangement Reaction to Clupeine Z, Followed by Selective Chemical Cleavage of the Chain, Leading to the Final Primary Structure.- B. The Amino-Acid Sequence of Clupeine YII.- C. The Amino-Acid Sequence of Clupeine YI.- D. Comments on the Structure of Clupeine.- E. The Amino-Acid Sequences of the Three Components (Y'I, Y?II and Z?) of Clupeine from North Sea Herring.- F. The Amino-Acid Sequences of One Component of Salmine and Three Components of Iridine.- IX Physical Structure of Nucleoprotamines and Protamines.- A. Nucleoprotamines.- B. Protamines.- X Properties and Functions.- A. Physical Properties.- B. Chemical Properties.- C. Biological and Physiological Properties.- 1. Biological Functions.- 2. Physiological Properties.- Acknowledgement.- References.

Protamines: isolation, characterization, structure and function

Studies on saponins and sapogenins of ginseng. the structure of panaxatriol.

The sapogenin of Ginseng saponins, ginsenosides-Rb1, -Rb2 and -Rc, was once reported to be protopanaxadiol (III). But it was found recently that dammarane type triperpenes with hydroxyl or methoxyl group at C(12) and C(20) give an equilibrated mixture of epimeric compounds at C(20). On mild hydrolysis of the saponins 20-epi-protopanaxadiol has been obtained as the genuine sapogenin for which the name of 20 (S)-protopanaxadiol (V) is proposed. The prosapogenin (XI), which was obtained by the partial hydrolysis of the above mentioned three saponins is found to be 3-O-(2β-D-glucopyranosyl-β-D-glucopyranosyl)-20 (R)-protopanaxadiol. The remaining glycosidic linkage in ginsenosides-Rb1, -Rb2 and -Rc should be located at C(20)-OH.

Chemical Studies on the Oriental Plant Drugs. XXVIII. Saponins and Sapogenins of Ginseng : Stereochemistry of the Sapogenin of Ginsenosides-Rb1, -Rb2 and -Rc

Toshio Ando

Papers

Chemical Studies on Oriental Plant Drugs. XIV. Protopanaxadiol, a Genuine Sapogenin of Ginseng Saponins

A new method for fractionation of protamines and the amino acid sequences of salmine and three components of iridine.

Protamines: isolation, characterization, structure and function

Studies on saponins and sapogenins of ginseng. the structure of panaxatriol.

Chemical Studies on the Oriental Plant Drugs. XXVIII. Saponins and Sapogenins of Ginseng : Stereochemistry of the Sapogenin of Ginsenosides-Rb1, -Rb2 and -Rc