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Titolo:
A fragment of prosaposin (SGP-1) from rooster sperm promotes sperm-egg binding and improves fertility in chickens
Autore:
Hammerstedt, RH; Cramer, PG; Barbato, GF; Amann, RP; OBrien, JS; Griswold, MD;
Indirizzi:
BioPore Inc, State Coll, PA 16805 USA BioPore Inc State Coll PA USA 16805BioPore Inc, State Coll, PA 16805 USA Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA PennState Univ University Pk PA USA 16802 l, University Pk, PA 16802 USA Penn State Univ, Dept Poultry Sci, University Pk, PA 16802 USA Penn State Univ University Pk PA USA 16802 i, University Pk, PA 16802 USA Univ Calif San Diego, Sch Med, Dept Neurosci, La Jolla, CA 92093 USA Univ Calif San Diego La Jolla CA USA 92093 urosci, La Jolla, CA 92093 USA Washington State Univ, Dept Biochem & Biophys, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 Biophys, Pullman, WA 99164 USA
Titolo Testata:
JOURNAL OF ANDROLOGY
fascicolo: 3, volume: 22, anno: 2001,
pagine: 361 - 375
SICI:
0196-3635(200105/06)22:3<361:AFOP(F>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
BULL SEMINAL PLASMA; INSEMINATION INCREASES FERTILITY; SULFATED GLYCOPROTEIN-1 SGP-1; MALE REPRODUCTIVE-SYSTEM; RAT SERTOLI CELLS; IN-VITRO BINDING; SYNTHETIC PEPTIDE; MOLECULAR-CLONING; NONCILIATED CELLS; EPIDIDYMAL SPERM;
Keywords:
profertility peptides; fertilization; seminal plasma; male reproductive tract;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
77
Recensione:
Indirizzi per estratti:
Indirizzo: Hammerstedt, RH BioPore Inc, POB 10074, State Coll, PA 16805 USA BioPore Inc POB 10074 State Coll PA USA 16805 PA 16805 USA
Citazione:
R.H. Hammerstedt et al., "A fragment of prosaposin (SGP-1) from rooster sperm promotes sperm-egg binding and improves fertility in chickens", J ANDROLOGY, 22(3), 2001, pp. 361-375

Abstract

A protein isolated from the supernatant of cryopreserved rooster sperm wasfound to increase the capability of cryopreserved rooster sperm to bind invitro to the perivitelline membrane of a chicken egg and substantially raise fertility after artificial insemination (Al). That activity was partially purified and termed universal primary sperm-egg binding protein (UPSEBP). Insufficient protein remained from 6 x 10(11) sperm, despite retention of bioactivity, to allow sequencing. We deduced that the protein may be related to prosaposin (also termed SGP-1, for sulfated glycoprotein-1), and we used published amino acid sequences of prosaposin as a guide for synthesis ofpeptides. Certain peptides were found to increase in vitro sperm-egg binding and increase fertility of frozen-thawed or fresh rooster sperm, in a manner similar to semipurified UPSEBP. Active epitopes were in a 60 amino acidsequence, reflecting the intervening sequence between saposins A and B, plus short extensions into saposins A and B. Highest activity was found when this synthetic peptide was oxidized to form a disulfide bond between terminal cysteines. Antibody against a synthetic peptide consisting of 58 of these 60 amino acids bound to a 7-9 kilodalton protein in UPSEBP. Collectively,the data support the conclusion that UPSEBP is a fragment of prosaposin. Because prosaposin is in semen in humans and animals, these observations have broad implications for possible cause and therapy of one type of subfertility.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 14:46:06