Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Structure and control of a cell-cell adhesion complex associated with spermiation in rat seminiferous epithelium
Autore:
Chapin, RE; Wine, RN; Harris, MW; Borchers, CH; Haseman, JK;
Indirizzi:
NIEHS, Reprod Toxicol Grp, Res Triangle Pk, NC 27709 USA NIEHS Res Triangle Pk NC USA 27709 col Grp, Res Triangle Pk, NC 27709 USA NIEHS, Struct Biol Lab, Res Triangle Pk, NC 27709 USA NIEHS Res Triangle Pk NC USA 27709 iol Lab, Res Triangle Pk, NC 27709 USA NIEHS, Biostat Branch, Natl Toxicol Program, Res Triangle Pk, NC 27709 USANIEHS Res Triangle Pk NC USA 27709 Program, Res Triangle Pk, NC 27709 USA
Titolo Testata:
JOURNAL OF ANDROLOGY
fascicolo: 6, volume: 22, anno: 2001,
pagine: 1030 - 1052
SICI:
0196-3635(200111/12)22:6<1030:SACOAC>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTEGRIN-LINKED KINASE; PROTEIN-KINASE; ECTOPLASMIC SPECIALIZATIONS; TYROSINE PHOSPHORYLATION; SERTOLI CELLS; CYTOPLASMIC DOMAIN; MAP KINASE; SIGNALING PROTEINS; ADHERENS JUNCTION; DOWN-REGULATION;
Keywords:
cadherins; cell adhesions; control; integrins; spermiation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
82
Recensione:
Indirizzi per estratti:
Indirizzo: Chapin, RE Dupont Pharmaceut Co, POB 30,1090 Elkton Rd, Newark, DE 19714 USA Dupont Pharmaceut Co POB 30,1090 Elkton Rd Newark DE USA 19714
Citazione:
R.E. Chapin et al., "Structure and control of a cell-cell adhesion complex associated with spermiation in rat seminiferous epithelium", J ANDROLOGY, 22(6), 2001, pp. 1030-1052

Abstract

Spermiation, the release of late spermatids from the Sertoli cell, is disrupted by a number of toxicants. Control of the spermiation process, and theproteins that interact to adhere mature spermatids to Sertoli cells, is poorly understood. In these studies we used immunohistochemistry, coimmunoprecipitation/Western blotting, and mass spectrometry to refine an earlier model of sperm adhesion proposed by our laboratory. We have identified specific proteins linked together as part of a multiprotein complex, as well as several additional proteins (cortactin, ERK1/2, and 14-3-3 zeta) that may be functioning in both structural and signal transduction roles. The current and prior data suggest that protein phosphorylation is central to the control of spermiation. We also present and characterize an in vitro tubule culture system that allowed functional testing of the spermiation model by pharmacologic manipulation, and yielded data consistent with the importance of protein phosphorylation in spermiation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 18:13:29