Many Faces of Openness in Adoption: Perspectives of Adopted Adolescents and Their Parents.

Parents and adolescents (mean age, 15.7 years) from 177 adoptive families participating in the second wave of the Minnesota/Texas Adoption Research Project were interviewed about their post-adoption contact arrangements. The sample included families with no contact, stopped contact, contact without meetings, and contact with face-to-face meetings between the adolescent and birth mother. Openness arrangements were dynamic, and different openness arrangements were associated with different experiences and feelings. Adoptive families with contact reported having higher levels of satisfaction about their openness arrangements, experiencing more positive feelings about the birth mother, and possessing more factual and personal knowledge about the birth mother than did families without contact. Adolescents and adoptive mothers in the contact with meetings group reported the greatest satisfaction with their openness arrangements; those with no contact or stopped contact reported the least satisfaction with their arrangements. Participants having no contact were more likely to want the intensity of contact to increase in the future rather than stay the same. Many participants already having contact wanted it to increase in the future. Fewer than 1 percent of all participants wanted to see the intensity of contact decrease.

Identification of the molecular chaperone, heat shock protein 1 (chaperonin 10), in the reproductive tract and in capacitating spermatozoa in the male mouse.

Mammalian spermatozoa must undergo epididymal maturation in the male reproductive tract and capacitation in the female tract before acquiring the ability to fertilize an oocyte. Previous studies from our laboratory have demonstrated a causal relationship between capacitation-associated surface phosphotyrosine expression and the ability of mouse spermatozoa to recognize the oocyte and engage in sperm-zona pellucida interaction. Our previous analyses of the surface phosphoproteome of capacitated murine spermatozoa identified two molecular chaperones, heat shock protein (HSP) D1 and HSP90B1, with well-characterized roles in protein folding and the assemblage of multimeric protein complexes. The expression of these chaperones was restricted to the rostral aspect of the sperm head, in an ideal position to mediate sperm-zona pellucida interaction. Herein, we report the characterization of an additional chaperone in this location, HSPE1 (chaperonin 10; HSP10). This chaperone was identified using a coimmunoprecipitation strategy employing HSPD1 as bait. The putative interaction between HSPE1 and HSPD1 was supported by reciprocal immunoprecipitation and colocalization studies, which demonstrated the coordinated appearance of both proteins on the surface of the sperm head during capacitation. However, the surface exposure of the protein was lost upon induction of acrosomal exocytosis, as would be expected of a protein potentially involved in sperm-zona pellucida interaction. Collectively, these data invite speculation that a number of molecular chaperones are involved in modification of the sperm surface during capacitation to render these cells functionally competent to engage the process of fertilization.