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PubMed1989

Protamine enhances epidermal growth factor (EGF)-stimulated mitogenesis by increasing cell surface EGF receptor number. Implications for existence of cryptic EGF receptors.

Treatment of Swiss mouse 3T3 cells and human epidermoid carcinoma A431 cells with protamine at 37 degrees C increased the 125I-epidermal growth factor (EGF) binding activity at 4 degrees C. The effect of protamine on the increase of 125I-EGF binding activity appeared to be time, temperature, and dose dependent. This up-modulation of 125I-EGF binding by protamine correlated with protamine enhancement of EGF-stimulated mitogenesis, with respect to the magnitude of the effect and the dose response curves. Scatchard plot analyses indicated that protamine induced an increase in numbers of both high and low affinity EGF receptors without affecting their affinities. Protamine also increased functionally active EGF receptors in plasma membranes and solubilized membranes. This was evidenced by Scatchard plot analyses and by a protamine-induced increase of 125I-EGF-EGF receptor complex and an increase in EGF-stimulated phosphorylation of the EGF receptor. Combined with column chromatography of the solubilized EGF receptor on protamine-agarose gel, these results suggest that protamine may increase the EGF receptor number by directly activating cryptic EGF receptors in the plasma membrane.

Animals↗
PubMedDate not supplied

A pulmonary mock circulation model for a better understanding of protamine reversal of heparin.

Neutralization of heparin by protamine is a common procedure following extracorporeal circulation (cardiopulmonary bypass) of blood. Protamine administration has been shown to cause serious hemodynamic derangement in some patients. Obstruction of the pulmonary vascular bed following protamine administration has been suggested to be the primary cause of hemodynamic changes. The present study was undertaken to test the hypothesis that macromolecular complexes formed between cationic protamine with anionic heparin or other plasma components cause the obstruction of the vascular bed. An in vitro mock circulation model was designed to examine the formation of such complexes. In this model, blood or plasma was passed through a glass bead column at a constant flow rate while the pressure between the syringe pump and the column was closely monitored. No increase in pressure was noted when blood, plasma or saline alone or with added heparin were passed through the column. Addition of protamine to either blood or plasma resulted in a significant increase in the pressure; this increase was even greater when heparin was also present in the test medium. That the increase in pressure was due to the obstruction of the column was confirmed by using 1251-protamine and documenting that complexes formed between protamine and plasma proteins/heparin were retained in the column. These observations suggested that protamine formed large insoluble complexes with plasma proteins. Heparin appeared to help consolidate these complexes thus causing a rapid increase in the pressure. This may explain why the hemodynamic changes following protamine administration are more pronounced in patients with circulating heparin.

Blood↗
PubMed1986

Protamine: does it alter right ventricular function?

Protamine administration has been associated with cardiac decompensation secondary to acute pulmonary vasoconstriction and subsequent right ventricular failure. To determine whether protamine infusion produced alterations in right ventricular performance, we evaluated both right and left ventricular function in patients receiving protamine infusion. The dose of protamine administered was calculated as adequate to reverse heparin as measured by the activated clotting time (ACT). Indices of right and left ventricular function obtained included right atrial pressure, right ventricular pressure, right ventricular ejection fraction, pulmonary artery pressure, pulmonary capillary wedge pressure, cardiac output, blood pressure, and heart rate. These measurements were obtained prior to protamine administration, at 1/2 total protamine dose, at completion of protamine infusion, and prior to sternal closure. No significant changes in right ventricular ejection fraction, right ventricular end-diastolic pressure, mean pulmonary artery pressure, or pulmonary vascular resistance were seen at any point during the study. Left ventricular function remained unchanged. Even in patients who are possibly at an increased risk (pulmonary artery hypertension, PAP greater than 25 mm Hg), no deterioration in right or left ventricular function could be demonstrated following protamine administration. These data suggest that protamine does not consistently exert a significant detrimental effect on right ventricular performance.

Blood Pressure↗
PubMed1980

[Mode of action of protamine sulfate on histamine secretion in the rat mast cells].

Protamine sulfate, known for a long time as a histamine releaser, was labeled with a fluorescent dye (FITC). This conjugate was shown to stain selectively the mast cell fraction of rat peritoneal cells. Within a few seconds, the protamine was found inside the cells. Although the cells had lost their histamine completely, no granules were found outside the cells. In the electron microscope, the protamine treated mast cells showed a loss of the electron density of their granules, a vacuolization, and other signs of histamine release. Evidence for a direct connection between the vacuoles and the extracellular fluid was gained by incubating mast cells in FITC-labeled human serum albumin followed by the addition of unlabeled protamine. After washing, the fluorescence was found to be located inside the cells, demonstrating an influx of the FITC-HSA under the influence of protamine. The protamine-induced release reaction is increased after addition of Ca2+, reduced by lowering the temperature, addition of 2-deoxyglucose, or cytochalasin B. Disodium cromoglycate also diminished the histamine release in a dose dependent manner. Protamine did not induce a loss of lactate dehydrogenase from the mast cells. The release reaction is mediated by the cell membrane, as shown by the releasing activity of insolubilized protamine. We conclude that the protamine-induced release is a non-cytotoxic reaction, fulfilling some criteria of the anaphylactic histamine release.

Animals↗
PubMed1983

The hemodynamic effects of intra-aortic versus intravenous administration of protamine for reversal of heparin in pigs.

The hemodynamic effects of intra-aortic (IA) versus intravenous (IV) administration of protamine for reversal of heparin were studied in pigs. The animals were anesthetized with sodium thiopental, nitrous oxide, oxygen, and halothane. Twenty minutes after heparinization (3 mg/kg) the following hemodynamic parameters were measured: heart rate, arterial pressure, pulmonary artery pressure (PAP), left ventricular end-diastolic pressure, and cardiac output. Protamine sulfate (3 mg/kg) was injected over 30 seconds IV in Group I (five pigs) and into the ascending aorta (IA) in Group II (five pigs). After injection, the above measurements were repeated at 1.0, 2.5, 5, and 15 minutes. The hemodynamic effects of intravenous protamine (3 mg/kg) without prior heparinization were studied in Group III (four pigs). Groups I and II experienced a decrease in cardiac output (Group I, 14%; Group II, 29%) and a marked increase in PAP (Group I, 78%; Group II, 79%) and pulmonary vascular resistance (PVR) (Group I, 174%; Group II, 559%) which peaked at 1 minute after protamine injection (p less than 0.05). Cardiac output, PAP, and PVR returned to baseline within 15 minutes. Heart rate, arterial pressure, left ventricular end-diastolic pressure, and systemic vascular resistance (SVR) were unchanged. No hemodynamic abnormalities occurred in animals injected with protamine alone (Group III). It is concluded that IV or IA administration of protamine causes marked hemodynamic changes in heparinized pigs. This does not confirm a recent clinical study reporting stable hemodynamics after IA administration of protamine. The lack of circulatory effects of protamine in unheparinized pigs suggests that a protamine-heparin interaction may be involved.

Animals↗
PubMed1997

Comparison of the hemodynamic and hematologic toxicity of a protamine variant after reversal of low-molecular-weight heparin anticoagulation in a canine model.

Using the dog as an animal model, we developed an experimental preparation to compare hemodynamic and hematologic toxicity of anticoagulation reversal. Currently, protamine sulfate reversal of standard unfractionated heparin and low-molecular-weight heparin (LMWH) anticoagulation causes adverse side effects, including decreased systemic mean arterial pressure (MAP), decreased cardiac output (CO), decreased oxygen consumption (VO2), and thrombocytopenia. In addition, standard protamine is only marginally effective at reversing the factor Xa inhibition induced by LMWHs. We have produced protamine-like variant peptides to decrease the adverse responses attributed to standard protamine. The hemodynamic, hematologic, and coagulation effects of standard protamine and the protamine variant (+18RGD) were assessed after reversal of LMWH anticoagulation in anesthetized dogs. Flow probes and vascular catheters were surgically implanted for measurement of hemodynamic parameters including MAP, CO, VO2, and heart rate (HR). Hematologic studies (platelet and white blood cell counts) and coagulation studies (activated clotting time [ACT], activated partial thromboplastin time [aPTT], thrombin clotting time [TCT], antifactor Xa and antifactor IIa values) also were performed. The protamine variant +18RGD was less toxic, induced less thrombocytopenia, and was more effective in anticoagulation reversal than was standard protamine sulfate. Results of this study indicate that the dog may be a useful model for investigating important hemodynamic, hematologic, and coagulation parameters during reversal of LMWH anticoagulation by use of synthetic protamine variants.

Animals↗
PubMed1999

Protamine Reversal of Heparin After Cardiopulmonary Bypass Increases Lung Resistance, Not Elastance.

BACKGROUND: Protamine, an immunologically active, cationic amine, has been suspected of impairing lung mechanics when administered after cardiopulmonary bypass (CPB) to reverse heparin. Whether such adverse changes are an effect of protamine itself, the formation of heparin-protamine complexes, the extent of heparin anticoagulation, or its chemical reversal is not known. METHODS AND RESULTS: Using a computer-controlled, forced-ventilation method over a variety of physiological tidal volume (V(T)) and frequency (f) combinations, we prospectively studied 18 adult, elective patients before systemic heparinization and after protamine reversal to confirm and, possibly, elucidate an etiology for any adverse pulmonary effects. Protamine and heparin doses, their sum (Sigma-dose) and differential (Delta-dose) doses, and activated clotting times were tabulated. In all patients, lung resistance (R(L)) and, to a lesser extent, elastance (E(L)) increased after CPB, compared with pre-CPB values (P <.05). However, R(L) particularly increased after CPB with increases correlated to the Delta-dose, where R(LPRE-->POST) = -0.037 [Delta-dose] - 0.56f \_ 0.019V(T) + 36.1 (r =.652, P <.05). No other significant correlations were found among the remaining clinical parameters and changes in either R(L) or E(L), or any chest wall component (all P >.05). CONCLUSIONS: The changes seen in R(L) after CPB were greatest in those patients receiving the most nearly balanced doses of heparin and protamine, and were not related significantly to the total heparin or protamine doses, or their sum. These suggests that the extent of anticoagulation reversal or formation of heparin-protamine complexes, and not protamine itself, are more responsible for changes seen in lung mechanics. The changes seen were limited solely to R(L), and not in either E(L) nor the chest wall mechanical properties.

Journal Article↗
PubMed2005

Toll-like receptor-dependent activation of several human blood cell types by protamine-condensed mRNA.

We reported that RNA condensed on protamine is protected from RNase-mediated degradation and can be used for vaccination. Here, we show that such complexes are also danger signals that activate mouse cells through a MyD88-dependent pathway. Moreover, mRNA-protamine complexes stimulate human blood cells. They strongly activate DC and monocytes, leading to TNF-alpha and IFN-alpha secretion. In addition, protamine-RNA complexes directly activate B cells, NK cells and granulocytes. The detailed analysis of the activated cell types, the study of the cytokines released from PBMC cultured with protamine-RNA complexes and recently published results suggest that TLR-7 and TLR-8 may be involved in the recognition of protamine-stabilized RNA. Our data indicate that protamine-stabilized RNA, which may be similar to RNA condensed in the nucleocapsids of RNA viruses, is a strong danger signal. Thus, similarly to plasmid DNA, protamine-RNA combines antigen production and non-specific immunostimulation. The studies presented here explain the capacity of protamine-RNA to act as a vaccine, and pave the way towards the development of safe and efficient mRNA-based immunotherapies.

Adaptor Proteins, Signal Transducing↗
PubMed1995

Protamine-sensitive polymer membrane electrode: characterization and bioanalytical applications.

A polymeric membrane electrode that exhibits significant and analytically useful potentiometric response to submicromolar levels of the heparin antagonist, protamine, is reported. The sensor is prepared by incorporating a lipophilic cation exchanger, potassium tetrakis(4-chlorophenyl)borate (KTpClPB) (at 1 wt%), within a specially formulated polymer membrane composed of 33 wt% 2-nitrophenyl octyl ether (2-NPOE), and 66 wt% poly(vinyl chloride) (PVC). When the polymer film is mounted in an appropriate electrode body, the resulting membrane electrode responds reproducibly to protamine via a nonequilibrium quasi-steady-state change in the phase boundary potential at the membrane/sample interface. Such response can be used to directly monitor, via classical potentiometric titrations, the binding between protamine and a variety of native (porcine and beef) as well as low-molecular-weight heparins. Scatchard analysis of the EMF titration data provides binding constants and stoichiometries for protamine-heparin interactions. The electrode can be further used to follow the enzymatic digestion of protamine by trypsin. In the presence of a given level of protamine, initial rates of potential decrease (-dE/dt) are shown to be linearly related to trypsin activity in solution over the range of 0-130 units/ml. The speed and simplicity of the protamine sensor make it an attractive alternative to classical methods for studying the interaction of protamine with other biologically important macromolecules as well as the proteolytic activity and reaction kinetics of trypsin.

Electrodes↗
PubMed1994

Interaction of human P1 and P2 protamines with DNA.

The interaction of two classes of human sperm protamines, P1 (HP1) and P2 (HP2, HP3, HP4), with DNA was investigated. Gel mobility shift assays with a range of DNA fragments of defined sizes show that, whatever its length, all the DNA is complexed with protamines at arginine to phosphate ratio of 0.1. Further addition of protamine molecules leads to a precipitation of the protamine-DNA complexes for arginine-phosphate ratio > or = 1.2. Fluorescence studies using the dye Hoescht 33258 as a fluorophore and DNAase I footprinting experiments suggest that P1 and P2 protamines bind at the DNA surface without apparent location in the minor or major groove of DNA. No differences in protamine-DNA interaction were observed between the two classes of human protamines P1 and P2. Moreover the binding to DNA was not influenced by the presence of zinc which induces the formation of a zinc-finger structure in protamine P2.

Binding, Competitive↗
PubMed1997

Involvement of fibrinogen in protamine-induced pulmonary hypertension.

Protamine reversal of heparin anticoagulation occasionally results in pulmonary hypertension as well as systemic hypotension. To examine the contribution of blood components to this induction of pulmonary hypertension, we developed an isolated rat lung perfusion model and perfused heparinized plasma, heparinized serum, and Hepes (4% bovine serum albumin, 20 mM N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid, 5 mM glucose, in warm physiological saline) buffer solution with or without fibrinogen. Perfusion with heparinized plasma and Hepes buffer solution with fibrinogen caused pulmonary hypertension; perfusion with heparinized serum or Hepes buffer solution without fibrinogen did not, suggesting that fibrinogen is involved in the induction of pulmonary hypertension. We also labeled protamine with 125I and compared the amounts of protamine accumulating in the lung with different concentrations of fibrinogen. The amount of protamine trapped in the lung increased according to the concentration of fibrinogen. Fibrinogen may accelerate the reaction between pulmonary endothelial cells and protamine or protamine-heparin complexes. In the mechanism of protamine-induced pulmonary hypertension, fibrinogen, as well as heparin and protamine, may be an essential component.

Animals↗
PubMed1986

Evidence of sequences resembling avian retrovirus long terminal repeats flanking the trout protamine gene.

Additional TATA boxes are present in the flanking regions of trout protamine genes. Their activity as promoters was assayed using an in vitro transcription system. These additional TATA boxes, together with polyadenylation signals that include the consensus AATAAA and CACTG sequences very close to the promoters, suggest that these sequences may be closely related to retroviral long terminal repeat (LTR) sequences. Other features of retroviral LTRs that are also present are short inverted repeats. The LTR-like sequences flanking the trout protamine gene show significant homology to the avian sarcoma virus LTR over a 40-bp region. The trout protamine gene falls into the relatively rare intronless class of eukaryotic genes. This suggests that the gene could have been derived from a processed gene introduced into the genome by reverse transcription of a mature mRNA. The protamine-mRNA-coding region is flanked by AACA... TGTT sequences, which might represent vestigial traces of past recombination events and whose presence supports the notion that the protamine gene sequence was of foreign origin. Recent attempts in this laboratory to transfer the protamine gene into mouse cells have resulted in a high frequency of deletions similar to those observed with constructs in which a retrovirus was used as a vector to transfect foreign DNA with promoters. The distribution of protamine genes in the animal kingdom is very sporadic, which suggests that protamine genes appeared relatively late in evolution. The nonuniform occurrence of the gene among lower vertebrates may have been the result of its horizontal transmission only to certain species, possibly by infection with retroviruses that acquired it from a different species.

Animals↗
PubMed1985

Protamine induced arterial hypoxaemia: the relationship to hypoxic pulmonary vasoconstriction.

Protamine administration may induce arterial hypoxaemia in dogs and humans. However, the responsible mechanism has not been established. Protamine, as it is a pulmonary vasoactive substance, may interfere with normal hypoxic pulmonary vasoconstriction (HPV) and cause arterial hypoxaemia. This possibility was tested in dogs utilizing a one lung hypoxic model. One lung hypoxic ventilation decreased pulmonary blood flow in the hypoxic lung from 1022 +/- 96 ml X min-1 (mean +/- SEM) to 846 +/- 39 ml X min-1 (p less than 0.05) while increasing blood flow from 833 +/- 85 ml X min-1 to 1109 +/- 101 ml X min-1 (p less than 0.05) in the normoxic lung, resulting in 24 per cent effective diversion of blood flow. Protamine infusion, after heparinization, markedly elevated pulmonary vascular resistance in both lungs but preferentially in the normoxic lung (102 +/- 27 per cent increase in normoxic lung, 60 +/- 6.4 per cent increase in hypoxic lung) and significantly reversed the pulmonary blood flow shift induced by one lung hypoxic ventilation (effective diversion of blood flow was reduced to four per cent). Concurrently, arterial PO2 further decreased. Our results demonstrate that protamine interferes with effectiveness of pre-existing HPV and suggest that this mechanism, at least in part, may be responsible for arterial hypoxaemia observed after protamine infusion. The marked generalized pulmonary vasoconstriction with protamine appears to be the direct force that interferes with pre-existing auto-regulatory HPV. In addition to the well known haemodynamic effects of protamine, protamine infusion may also cause arterial hypoxaemia in those patients in whom HPV plays a significant role in maintaining arterial oxygenation.

Animals↗
PubMed1997

Influence of protamine on adhesion, chemotaxis and proliferation of human vascular smooth muscle cells.

It has been shown that, in streptozotocin diabetic rats, protamine-retarded insulin administered in vivo stimulates intimal hyperplasia in balloon-injured carotid artery. The aim of this study was to evaluate the influence of protamine on cultured human vascular smooth muscle cells (h VSMC), by observing its effects on adhesion, chemotaxis and proliferation. hVSMC were isolated during abdominal surgery, cultured and utilized at passages 6-10. We observed that protamine stimulates: 1) cell adhesion in the concentration range 0.04-20 micrograms/ml (analysis of variance, ANOVA, p < 0.0001); 2) cell chemotaxis in the absence of fetal calf serum (FCS) in the concentration range 1-200 micrograms/ml (ANOVA, p < 0.0001) and in the presence of 1% FCS in the concentration range 5-200 micrograms/ml (ANOVA, p < 0.0001), further enhancing the chemotaxis induced by 10% FCS in the concentration range 20-200 micrograms/ml (ANOVA, p < 0.0001); 3) cell proliferation and 3H-thymidine incorporation from 1 to 5 micrograms/ml (ANOVA, p < 0.0001); 4) cell c-fos oncoprotein nuclear expression. We also observed that protamine effects on chemotaxis, proliferation and c-fos expression are inhibited by heparin that human insulin stimulates cell proliferation and 3H-thymidine incorporation (ANOVA, p < 0.0001) at concentrations equal to or greater than 480 pmol/l and that these effects of insulin persist in the presence of protamine. In conclusion, protamine influences hVSMC behaviour by interfering with biological functions involved in atherogenesis. The concentrations used in this short-term in vitro study were higher than those probably occurring in vivo in patients chronically treated by protamine-retarded insulin preparations: further studies, therefore, are needed to evaluate the safety of protamine as a retardant of insulin action in vivo.

Cell Adhesion↗
PubMed2004

All roads lead to arginine: the squid protamine gene.

The protamine of squid is one of the most arginine-rich protamines (77%, mol/mol). It possesses a leading sequence that is posttranslationally removed during spermatogenesis in a manner that is analogous to that observed in some of its vertebrate protamine counterparts. In this paper we describe the gene sequence of the protamine of the squid Loligo opalescens. This represents the first complete gene sequence ever reported for an invertebrate protamine. Like those of vertebrate protamines, the messenger RNA is polyadenylated but the gene does not contain an intron. The promoter region contains the major transcriptional regulatory elements (CRE, TATA box, and CAP) that are also characteristic of the vertebrate protamine genes. It is unclear whether the similarities of protamines in species from both the deuterostome and the protostome branches represent the result of phylogenetic conservation or evolutionary convergence.

Amino Acid Sequence↗
PubMed1992

Purification and properties of a protamine kinase from bovine kidney microsomes.

About an eightfold increase in protamine kinase activity was detected following extraction of highly purified microsomes from bovine kidney with 1% Triton X-100. Relative to the soluble fraction, the microsomes contained about 30% protamine kinase activity. The microsomal protamine kinase was purified to apparent homogeneity. The purified enzyme exhibited an apparent M(r) approximately 45,000 as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by gel permeation chromatography on Sephacryl S-200. Relative to protamine, the purified kinase exhibited about 100% activity with the synthetic peptide RRLSSLRA and about 5, 8, and less than 0.1% activity with casein, histone H2B, and histone H1, respectively. The purified kinase phosphorylated several 40 S ribosome polypeptides. One of these polypeptides was identified as ribosomal protein S6 by N-terminal sequencing. About 2.5 mol of phosphoryl groups was incorporated per mole of ribosomal protein S6 following incubation of the 40 S ribosomes with the purified kinase. Following incubation with protein phosphatase 2A2, purified preparations of the protamine kinase were inactivated. These properties were identical to those of purified preparations of a protamine kinase from extracts of bovine kidney cytosol (Z. Damuni, G.D. Amick, and T.R. Sneed, 1989, J. Biol. Chem. 264, 6412-6418). Near identical peptide patterns were obtained following incubation of purified preparations of the microsomal and cytosolic protamine kinases with Staphylococcus aureus V8 proteinase. The results indicate that a form of the cytosolic protamine kinase is present in microsomes.

Animals↗
PubMed1990

pH dependence of protamine action on apical membrane permeability in Necturus gallbladder epithelium.

Protamine reversibly decreases cation permeability and alters the structure of Necturus gallbladder tight junctions. Conflicting results, however, have been published whether or not it also affects apical cell membrane permeability. We investigated this issue more systematically by measuring voltage (psi mc) and fractional resistance (fRa) of the apical membrane at varying concentrations of protamine, K+, and H+ in the bathing solution. At pH 7.6 and [K+] 2.5 mM, (Poler, M.S. and Reuss, L. (1987) Am. J. Physiol. 253, C662) 6 microM protamine caused psi mc to depolarize from -58 to -51 mV and fRa to decrease from 0.74 to 0.67. If we increased pH to 8.1 these effects were even more pronounced. At [K+] 2.5 mM, but not 4.5 mM, psi mc transiently hyperpolarized for about 5 min after adding protamine. Most importantly, if [K+] was 4.5 mM and pH was adjusted to 7.1 (Bentzel et al. (1987) J. Membr. Biol. 95, 9) no significant changes of psi mc and fRa occurred. In any case, at a supramaximal concentration of 200 microM, protamine did not further increase the paracellular response but produced decreasing psi mc and fRa. We conclude that 6 microM protamine decreases K+ conductance of the apical membrane, if it is already tuned high by high pH. At low control K+ conductance as observed at lower pH, protamine action is restricted to the paracellular pathway. Thus, conflicting results were due to different experimental conditions. At a solution pH of 7.1, 6 microM protamine fulfills criteria of a selective tool for reversibly altering structure and function of the tight junction in Necturus gallbladder.

Animals↗
PubMed1979

Translation of partially purified poly(A)+ protamine messenger RNA components in wheat germ and rabbit reticulocyte cell-free systems. Evidence for translational control mechanisms.

The coding properties of individual poly(A)+ protamine mRNA subcomponents have been explored by analysis of their translation products in two different cell-free protein synthesis systems, the rabbit reticulocyte lysate and the wheat germ S-30, both of which can translate total protamine mRNA. The products synthesized in the reticulocyte lysate in the presence of total poly(A)+ PmRNA consisted mainly of protamine components CII and CIII with component CI only a minor product. However, in the wheat germ S-30, the same mRNA preparation supported the synthesis of all three protamine components, in approximately equal amounts. In addition a new polypeptide, a putative fourth protamine component, labelled CO, was also synthesized. The translation products of subcomponents of poly(A)+ PmRNA separated as individual bands on polyacrylamide gels were similarly analyzed and it was shown that each of the isolated poly(A)+ PmRNA species could stimulate the incorporation of [3H]arginine into protamines in both translational systems. Although each mRNA band stimulated the synthesis of one particular protamine polypeptide predominantly in a given cell-free system, the same RNA preparation was found to direct preferentially the synthesis of a different protamine component in the second cell-free system. The products synthesized in the rabbit reticulocyte lysate in the presence of the individual mRNA species still showed component CI present as a minor product.

Animals↗