A walk though vertebrate and invertebrate protamines

Lewis, John D.; Song, Yue; Jong, Miriam E. de; Bagha, Sabira M; Ausió, Juan

doi:10.1007/s00412-002-0226-0

Cited by 175 publications

(149 citation statements)

References 59 publications

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“…10). Consistent with SRPK1 being the major protamine 1 kinase, Ser 8 and Ser 10 ( 7 RSQSRSR 13 ) were previously identified as the phosphorylation sites of monophosphorylated and diphosphorylated human P1 protamine (6).…”

Section: Srpk1 Phosphorylates Lbr and P1 Protamine In Testes-supporting

confidence: 58%

Temporal Association of Protamine 1 with the Inner Nuclear Membrane Protein Lamin B Receptor during Spermiogenesis

Mylonis

Drosou

Brancorsini

et al. 2004

Journal of Biological Chemistry

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During mammalian spermiogenesis, histones are replaced by transition proteins, which are in turn replaced by protamines P1 and P2. P1 protamine contains a short arginine/serine-rich (RS) domain that is highly phosphorylated before being deposited into sperm chromatin and almost completely dephosphorylated during sperm maturation. We now demonstrate that, in elongating spermatids, this phosphorylation is required for the temporal association of P1 protamine with lamin B receptor (LBR), an inner nuclear membrane protein that also possesses a stretch of RS dipeptides at its nucleoplasmic NH 2 -terminal domain. Previous studies have shown that the cellular protein p32 also binds tightly to the unmodified RS domain of LBR. Extending those findings, we now present evidence that p32 prevents phosphorylation of LBR and furthermore that dissociation of this protein precedes P1 protamine association. Our data suggest that docking of protamine 1 to the nuclear envelope is an important intermediate step in spermiogenesis and reveal a novel role for SR protein kinases and p32.The development of spermatids into spermatozoa, termed spermiogenesis, is characterized by the replacement of histones by the highly basic, arginine-rich, protamines (1). As a result of this exchange, the nucleosomal-type chromatin is transformed into a smooth fiber and compacted in a volume of about 5% of that of a somatic cell nucleus (2, 3). Although the exchange of chromatin proteins during spermiogenesis has long been known, the molecular mechanisms and the signaling pathways governing the histone to protamine transition have remained obscure.The deposition of protamines on sperm chromatin and the subsequent chromatin condensation appear to be controlled by phosphorylation-dephosphorylation events. Protamines are highly phosphorylated, shortly after their synthesis and before binding to DNA, whereas they become largely dephosphorylated during sperm maturation (4 -8). Phosphorylation of P2 protamine has been shown to be essential, because deletion of the calmodulin-dependent protein kinase Camk4, which phosphorylates P2 protamine, impairs the replacement of transition protein-2 with P2 protamine, resulting in defective spermiogenesis and male sterility (9). On the other hand, all P1 protamines contain short arginine/serine-rich (RS) 1 domains that are efficiently phosphorylated by SRPK1 (SR protein kinase 1) (10), but the physiological significance of this modification is mostly unknown.In this respect, Biggiogera et al. (11) reported that protamines initially appear at the nuclear periphery, implying that the nuclear envelope might play a role in the replacement of transition proteins by protamines during spermiogenesis. Given that RS domains mediate protein-protein interactions (12), we sought to investigate the potential interaction of P1 protamine with the inner nuclear membrane protein lamin B receptor (LBR), which also possesses a repeat of RS dipeptides at its nucleoplasmic NH 2 -terminal domain. In the present study we demonstrate a direct a...

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Section: Srpk1 Phosphorylates Lbr and P1 Protamine In Testes-supporting

confidence: 58%

Temporal Association of Protamine 1 with the Inner Nuclear Membrane Protein Lamin B Receptor during Spermiogenesis

Mylonis

Drosou

Brancorsini

et al. 2004

Journal of Biological Chemistry

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“…Protamines size ranging between 4000-12 000 Da, are composed of more than 50% arginine (13). There are 2 types of protamines, namely protamine 1 (P1) and protamine 2 (P2).…”

Section: Mortalities and Morbiditiesmentioning

confidence: 99%

The Impact of Bacterial Infections on Human Spermatozoa

Zeyad¹,

Amor²,

Hammadeh³

2017

International Journal of Women’s Health and Reproduction Scienc

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“…8 It is characterized by an exceptionally high content of basic amino acids (i.e., arginine, lysine, and histidine), which may reach 80%. 9,10 In addition to neutralizing the anticoagulant action of heparin, it is also used for titrating heparin in vitro. 11 Poly-L-lysine is another polymer used for heparin removal, [12][13][14] and it also amplifies the action of protamine.…”

Section: Introductionmentioning

confidence: 99%

pH-Sensitive Genipin-Cross-Linked Chitosan Microspheres For Heparin Removal

et al. 2008

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Chitosan hydrogel microspheres were obtained by cross-linking chitosan in its inverse emulsion using genipin as cross-linker. The genipin-cross-linked chitosan microspheres (ChGp) swell significantly in water at pH values below 6.5 and shrink to a smaller extent at pH values above 6.5. ChGp microspheres bind heparin in water. The kinetics of heparin binding was found to be pH dependent and was faster and more efficient at a lower pH. That can be also controlled by the weight of ChGp microspheres used. Rate and efficiency of heparin adsorption at pH 7.4, which is typical of blood, could be increased by quaternization of ChGp microspheres using glycidyltrimethylammonium chloride (GTMAC). The polymeric material obtained thus can be potentially useful for heparin removal in biomedical applications.

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A walk though vertebrate and invertebrate protamines

Cited by 175 publications

References 59 publications

Temporal Association of Protamine 1 with the Inner Nuclear Membrane Protein Lamin B Receptor during Spermiogenesis

Temporal Association of Protamine 1 with the Inner Nuclear Membrane Protein Lamin B Receptor during Spermiogenesis

The Impact of Bacterial Infections on Human Spermatozoa

pH-Sensitive Genipin-Cross-Linked Chitosan Microspheres For Heparin Removal

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