Amino acid sequence of an egg-lysin protein from abalone spermatozoa that solubilizes the vitelline layer.

Fridberger, Anita; Sundelin, Johan; Vacquier, V D; Peterson, Per A.

doi:10.1016/s0021-9258(17)39334-1

Cited by 18 publications

(4 citation statements)

References 21 publications

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“…To characterize interactions of lysin with the phospholipid bilayer, understanding the structure of the protein is essential. The complete amino acid sequence of 16K lysin has been resolved recently (Fridberger et al, 1985). Lysin, a cationic protein, contains a segment (residues 29-72) which has 10 positively charged but no negatively charged residues.…”

Section: Discussionmentioning

confidence: 99%

“…Surface electrostatics of liposomes containing acidic phospholipid are modified by the presence of multivalent cations, both by specific binding and by electrostatic screening of the double layer (Nir et al, 1983). Lysin, a natural polycation with some distinctive positively charge domains (Fridberger et al, 1985), is expected to decrease the surface charge density and surface potential. The consequent reduction of the electrostatic repulsion by lysin seems to induce liposomes to aggregate, as seen in PS-containing liposomes (Table II).…”

Section: Discussionmentioning

confidence: 99%

“…There is a tendency that lysin self-associated at higher protein concentrations in salt solution. In view of lysin's predicted secondary structure (Fridberger et al, 1985), in ionic media lysin may form a molecular complex with most charged residues located on the surface via hydrophobic protein-protein bonding. Thus, the site for hydrophobic bilayer penetration is not available.…”

Section: Discussionmentioning

confidence: 99%

“…The amino acid sequence of this protein has been determined by automated Edman degradation. The molecule is composed of 134 amino acids, has a calculated molecular weight of 16070, and hereafter will be termed 16K lysin (Fridberger et al, 1985). The 16K lysin has a p7 of about 9, is soluble in aqueous low-salt solutions, and must have exposed hydrophobic domains, since it binds to paraffin-coated glass (Lewis et al, 1982).…”

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confidence: 99%

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Fusion of liposomes induced by a cationic protein from the acrosome granule of abalone spermatozoa

Hong¹,

Vacquier²

1986

Biochemistry

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Lysin, a protein of Mr 16 000 from the acrosome granule of the abalone, is responsible for the dissolution of the egg vitelline layer. The primary structure of this cationic protein projects some hydrophobic domains in the secondary structure. Lysin was found to associate nonselectively with phospholipid bilayers and cause a spontaneous release of encapsulated carboxyfluorescein in liposomes. The association of lysin with phosphatidylcholine liposomes suggests that there is a hydrophobic interaction between lysin and lipid bilayers. Binding of lysin to phospholipid resulted in the aggregation of phosphatidylserine-containing liposomes, but aggregation was not observed in neutral phosphatidylcholine liposomes. Resonance energy transfer and dequenching of fluorescent 1-palmitoyl-2-cis-parinaroylphosphatidylcholine were both used to determine the fusogenic activity of lysin in aggregated liposomes. Results from both assays are consistent. Lysin-induced fusion was observed in all the phosphatidylserine-containing liposomes, and the general trend of fusion susceptibility was phosphatidylserine/phosphatidylcholine (1:2) approximately equal to phosphatidylserine/phosphatidylcholine/phosphatidylethanolamine (1:1:1) greater than phosphatidylserine/phosphatidylethanolamine (1:2). Cholesterol up to 30% did not affect the intrinsic fusion susceptibility. A hydrophobic penetration by protein molecules and the packing of phospholipid bilayers are used to interpret the fusion susceptibility. Lysin-induced liposome aggregation was highly independent of the state of self-association of lysin in ionic medium. However, the fusogenic activity of self-associated lysin was found to be much less than the monodispersed one. Liposomes preincubated with Ca2+ did not fuse initially as readily as those without Ca2+ treatment.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Fusion of liposomes induced by a cationic protein from the acrosome granule of abalone spermatozoa

Hong¹,

Vacquier²

1986

Biochemistry

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Membrane Fusion

Blumenthal

Dimitrov

1997

Comprehensive Physiology

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The sections in this article are: Observation of Fusion Requires Physical Techniques for Monitoring Mixing of Membranes and the Compartments they Enclose Morphological Changes Following Fusion Are Observed by Light Microscopy but Membrane Fusion May Occur without such Changes Fluorescence Microscopy and Spectrofluorometry Allow Quantitation of Membrane Fusion Events in Living Cells Electron Microscopy Provides Direct Observation of Structural Rearrangements Due to Fusion Patch‐Clamp Techniques Allow the Monitoring of Very Fast Openings of Fusion Pores What Do We Learn from “Nonbiological” Fusion Processes? Ca 2+ Induces Aggregation Destabilization, and Fusion of Liposomes Containing Phospholipids with Negatively Charged Head‐groups Fusion of Lipid Membranes by Amphipathic and Nonpolar Molecules Correlates with Their Lytic and Aggregational Activity Dehydration, Aggregation, and Destabilization of Membranes by Polyethelene Glycol Are Essential for Fusion of Lipid Membranes Destabilization by High‐Voltage Electric Pulses Leads to Fusion of Adjoining Membranes Molecular Rearrangements in the Lipid Bilayers during the Very Act of Fusion May Involve Intermediate Structures Specialized Proteins Mediate Fusion in Life Processes Viral Envelope Proteins Contain Hydrophobic “Fusion Peptide” Sequences To Enter a Cell a Virus Must Find the Receptor That Invites It In Some Viruses Require More Than One Type of Envelope Protein for Entry Influenza Hemagglutinin Was the Only Fusion Protein with Known Three‐Dimensional Structure The Process of HA ‐mediated Membrane Fusion Can Be Dissected into a Number of Elementary Steps Human Immunodeficiency Virus Type 1 ( HIV ‐1), the Primary Etiological Agent of the Acquired Immunodeficiency Syndrome ( AIDS ), Enters Cells by Membrane Fusion at Neutral pH The Receptor CD 4 Plays Both a Passive and an Active Role in Allowing Entry of the Virus into the Cell Stable Envelope Glycoprotein‐Receptor Complex Formation Is Rate‐limiting in the Overall Fusion Process Multiple Copies of the HIV ‐1 Envelope Glycoprotein May Be Required for Fusion Pore Formation Sperm Membrane Proteins Involved in Sperm‐Egg Fusion May Resemble Viral Fusion Proteins Toward A Resolution of Fusion Proteins in Exocytosis Multiple Proteins May Be Required for Intracellular Fusion Toward A Physicochemical Analysis of Fusion Kinetics Delays in Fusion Are Proportional to the Fusion Barriers and Decrease with an Increase in the Strength of the Fusogen Rates of Fusion Can Provide Information for the Time Course of Membrane Merging and Fusion Pore Expansion Fusion Yields and Delays Are Related but May Reflect Different Properties of the Fusing Membranes Does Understanding Membrane Fusion Need New Breakthroughs in Methodology? Note Added in Proof

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Two major acrosomal proteins act on different parts of the oocyte vitelline coat in the abalone, Haliotis discus

Usui

Haino-Fukushima

1991

Molecular Reproduction Devel

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Two proteins of molecular weights 20,000 (20K) and 15,500 (15.5K) are the major soluble substances released from the acrosomal vesicle of the abalone, Haliotis discus, spermatozoon. A crude preparation of them has been shown to possess lytic activity on the oocyte vitelline coat (VC). To elucidate the role(s) of each acrosomal protein (AP) in VC lysis, oocytes were examined after treatment with various AP preparations. The VC, which is about 1 micron thick, is composed of thin outer and inner electron-dense layers and a thick main layer of a fine filamentous feltwork. When oocytes were treated with a crude preparation containing both APs, the outer layer disappeared and the feltwork of the main layer loosened extensively. A preparation containing predominantly the 20K AP dissolved the outer layer completely and the main layer to some extent, whereas another preparation containing predominantly the 15.5K AP caused loosening of the main layer without alteration of the outer layer, suggesting that the 20K AP acts on the outer layer, whereas the 15.5K AP acts on the main layer. However, when purified, each AP by itself failed to dissolve the VC, although lysis occurred in a 1:1 mixture of these preparations. Moreover, when the oocytes were pretreated with the 20K AP and thoroughly washed, the 15.5K AP alone could induce lysis. These results suggest that the lysis of the outer layer requires both APs but not simultaneously. The 15.5K AP, which is located posteriorly in the acrosomal vesicle, must be released to act on the VC following the action of the 20K AP.

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Amino acid sequence of an egg-lysin protein from abalone spermatozoa that solubilizes the vitelline layer.

Cited by 18 publications

References 21 publications

Fusion of liposomes induced by a cationic protein from the acrosome granule of abalone spermatozoa

Fusion of liposomes induced by a cationic protein from the acrosome granule of abalone spermatozoa

Membrane Fusion

Two major acrosomal proteins act on different parts of the oocyte vitelline coat in the abalone, Haliotis discus

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