Evaluation of the Purity of Boar Sperm Plasma Membranes Prepared by Nitrogen Cavitation

Peterson, R. N.; Russell, Lonnie D.; Bundman, Donna; Freund, M.

doi:10.1095/biolreprod23.3.637

Cited by 72 publications

(52 citation statements)

References 5 publications

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“…Such a local variation of the plasma membrane was demonstrated in salmon sperm surface (Haruo and Yamamoto 1984): the membrane covering the tail differs in its physiological properties from that of the head. Several bands were also obtained when boar sperm plasma membrane was centrifuged onto linear sucrose gradients (Peterson et al, 1980) and a similar interpretation was proposed. …”

Section: Discussionmentioning

confidence: 65%

Plasma membrane of trout spermatozoa: I. Isolation and partial characterization

Labbé

Loir

1991

Fish Physiol Biochem

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AbslractThe plasma membrane from spermatozoa of rainbow trout was isolated by four techniques: sonication, hypotonic shock, mechanical homogenization after freeze-thawing, and nitrogen cavitation, in combination with continuous sucrose gradient centrifugation. Nitrogen cavitation (900 PSI, 20 min equilibration at 4°C) was the most effective technique.Following nitrogen cavitation, four bands were recovered in the sucrose gradient at densities = 1.03, 1.05, 1.09 and 1.15 g/ml. Elect ron microscopy revealed membrane vesicles of various sizes in bands 1 to 3, while enzyme analysis revealed a 3.9 to 5.5-fold enrichment in 5'-nucleotidase and little contamination by lactate dehydrogenase (cytosol) and succinic dehydrogenase (mitochondria). Lipid analysis of bands 1 and 2 indicated a 6 to 7-fold enrichment in cholesterol and a cholesterol: phospholipid ratio of 0.59-0.70. Seven classes of phospholipids were present in bands 1-3 with no significant differences observed among bands. These data indicate that the vesicles (in bands 1 and 2) obtained after nitrogen cavitation are primarily plasma membranes. Membranes in band 3 appear to be slightly contaminated with nuclear membranes.Most of the plasma membrane proteins were acidic to neutral. The 2 main membrane proteins were 42 and 30 Kilodaltons.

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Section: Discussionmentioning

confidence: 65%

Plasma membrane of trout spermatozoa: I. Isolation and partial characterization

Labbé

Loir

1991

Fish Physiol Biochem

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“…Once capacitation has been completed, the acrosome reaction can proceed, involving progressive fusion, vesiculation and/or exocytosis of the acrosomal membrane to the overlying plasma membrane; this vesiculation/exocytosis allows for the concomitant release of the acrosomal enzymes which are subsequently involved in the sperm's penetration of the mucoproteinaeous investments surrounding the oocyte. Both capacitation and the acrosome reaction have been linked to cellular modifications in membrane structure of the lipid bilayer to produce protein-free zones via protein alteration and/or migration which may also include polar/neutral lipid efflux (Ahuji et al, 1975;Yanagimachi, 1981;Austin, 1985;Hammerstedt and Parks, 1987;Phelps et al, 1990;Ravinik et al, 1990 (Hathaway and Hartree, 1963;Bernstein and Teichman, 1973;Schill, 1973), extraction with detergents (Srivastava et al, 1970;Multamaki et al, 1975), physical removal using glass beads (Hathaway and Hartree, 1963;Morton and Lardy, 1967;Multamaki and Niemi, 1972), freeze-thawing (Pedersen, 1972;Brown and Hartree, 1974), sonication (Lunstra et al, 1974;Esbenshade and Clegg, 1976;Clegg et al, 1975;Hinkovska et al, 1986), homogenization (Moore and Hibbit, 1976;Soucek and Vary, 1984;Holt and North, 1985;Casali et al, 1985;Holt and North, 1986), hypotonic shock (Ivanov and Profirov, 1981;Rana and Majumder, 1989) and nitrogen cavitation (Gillis et al, 1978;Peterson et al, 1980;Noland et al, 1983;Nikolopoulou et al, 1985;Parks and Hammerstedt, 1985;…”

Section: The Spermatozoanmentioning

confidence: 99%

“…When examining initial purification techniques, a good percentage of this past work has been performed in the boar (Lunstra et al, 1974;Gillis et al, 1978;Peterson et al, 1980;Soucek and Vary, 1984;Nikolopoulou et al, 1985;Canvin and Buhr, 1989;Parks and Lynch, 1992) with less done in the ram and goat (Hathaway and Hartree, 1963;Srivastava et al, 1970;Srivatava et al,, 1970;Brown and Hartree, 1974;Ivanov and Propfirov, 1981;Holt and North, 1985;Parks and Hammestedt, 1985;Hinkovska et al, 1989;Rana and Majumder, 1989), bull (Hathaway and Hartree, 1963;Multamaki and Niemi, 1972;Berstein and Teichman, 1973;Multamaki et al, 1975;Noland et al, 1983;Casaii et al, 1985;Parks et al, 1987;Parks and Lynch, 1992), stallion (Parks and Lynch, 1992) and rat (Jones, 1986;Agrawal et al, 1988 (i.e., exposure to pure, pressurized for 10 minutes followed by rapid decompression to atmospheric conditions which allows Nj to form gas vesicles which disrupt the membrane when Nj escapes into the surrounding atmosphere).…”

Section: The Spermatozoanmentioning

confidence: 99%

“…Two years later, Peterson et al (1980) Several years later, others examining the effects of temperature on the fluidity of boar spermatozoal plasma membranes described another modification of the Gillis procedure . After collecting semen from boars using the gloved-hand technique, the semen was filtered, diluted with a TRIS-buffered sucrose solution and then washed through two different types of an industrial grade silicon oil.…”

Section: The Spermatozoanmentioning

confidence: 99%

“…The major proteins were of an approximate molecular weight of 14, 16, 16.5, 17.5, 18, 18+, 18.5, 20, 43, 44, 47, 50, 64, 67, 72, 82, 110, 115, 120 and 300 kDa; of these, eight were considered to be glycopeptides (20,43,44,64,72,110,120 and 300 kDa). Using fluorescent monoclonal antibodies to these major 39 glycoproteins, it was found that these major glycoproteins were localized primarily in the head region of the sperm cell -this is entirely understandable given the fact that the authors' previous work showed that their plasma membrane isolation technique routinely isolated only those plasma membranes surrounding the sperm head above the equatorial segment (Peterson et al, 1980). Later, Hunt et al (1985) quantitated that the 44 and 47 kDa major proteins made up approximately 20% of the total plasma membrane protein component that Coomassie- was added by the remaining accessory sex glands (prostate or bulbourethral gland).…”

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confidence: 99%

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Biochemical composition of the spermatozoal plasma membrane in normal and heat-stressed boars

Althouse

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This manuscript has been reproduced from the microfilm master, UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer.The quality of this reproduction is dependent upon the qualify of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction.In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion.Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overlaps. Each original is also photographed in one exposure and is included in reduced form at the back of the book.

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Isolation and characterization of a protein with homology to angiotensin converting enzyme from the periacrosomal plasma membrane of equine spermatozoa

Dobrinski¹,

Ignotz²,

Fagnan³

et al. 1997

Mol. Reprod. Dev.

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The periacrosomal plasma membrane of spermatozoa is involved in sperm binding to oviductal epithelial cells and to the zona pellucida. A protein of 68–70 kD molecular mass was purified biochemically from the isolated periacrosomal plasma membrane of equine spermatozoa as a possible receptor for adhesion of spermatozoa to oviductal epithelial cells. A polyclonal antibody raised in rabbits against the purified equine sperm membrane protein recognized the 70 kD and an antigenically related 32 kD protein in preparations of isolated periacrosomal sperm plasma membrane and in detergent extracted ejaculated and epididymal spermatozoa. A larger protein (∼110 kD) was detected in equine testis. Two antigenically related proteins (64 and 45 kD) were recognized on the plasma membrane of cynomolgus macaque spermatozoa. In vitro sperm‐binding assays were performed in the presence of antigen‐binding fragments or IgG purified from the polyclonal antiserum to investigate a possible function of the isolated protein in binding of equine spermatozoa to homologous oviductal epithelial cells or zona pellucida. Incubation with antigen‐binding fragments or IgG purified from the antiserum did not inhibit binding of equine spermatozoa either to oviductal epithelial cells or to the zona pellucida. On ultrastructural examination, the antibody bound exclusively to the cytoplasmic side of the periacrosomal plasma membrane of equine and macaque spermatozoa. Microsequence analysis of 13 residues of sequence showed strong homology with a number of angiotensin converting enzymes: An 84% identity was identified with testis specific and somatic forms of human and mouse angiotensin‐converting enzyme. Immunocytochemistry and immunoblot analysis established that the protein is specific for the periacrosomal membrane of ejaculated, epididymal, and testicular stallion spermatozoa. Mol. Reprod. Dev. 48:251–260, 1997. © 1997 Wiley‐Liss, Inc.

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Evaluation of the Purity of Boar Sperm Plasma Membranes Prepared by Nitrogen Cavitation

Cited by 72 publications

References 5 publications

Plasma membrane of trout spermatozoa: I. Isolation and partial characterization

Plasma membrane of trout spermatozoa: I. Isolation and partial characterization

Biochemical composition of the spermatozoal plasma membrane in normal and heat-stressed boars

Isolation and characterization of a protein with homology to angiotensin converting enzyme from the periacrosomal plasma membrane of equine spermatozoa

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