Helping foster parents cope with separation, loss, and grief.

Major changes in planning for children in foster care have resulted in significant changes in the roles of and expectations for foster parents, accompanied by even less attention to the issues of foster families' grief and loss. This article focuses on (1) the many ways foster parents encounter loss and grief on a continuous basis; (2) factors that affect the intensity of the loss and the healthy expression and resolution of grief; (3) problems that can result when the grief of foster parents is not adequately addressed; and (4) ways in which professionals can be helpful to these caregivers around loss and grief.

Experiences, concerns, and service needs of families adopting children with prenatal substance exposure: summary and recommendations.

Parents who adopted children from out-of-home care with prenatal substance exposure were interviewed four months after the child's placement in the home, and again after the first year regarding their experience with adoption and their concerns about their child's development, attachment, and behavior; aspects of parenting and the adoption process; effects of prenatal substance exposure; and availability and helpfulness of resources. Adoptive parents found parenting children with prenatal substance exposure to be both more rewarding and more difficult than they had imagined.

Monoamine oxidases A and B are differentially regulated by glucocorticoids and "aging" in human skin fibroblasts.

Two forms of monoamine oxidase (MAO A and MAO B) exist which, although similar in a number of properties, can be distinguished on the basis of their substrate specificity, inhibitor sensitivity, kinetic parameters, and protein structure. These properties were used to study the molecular mechanism(s) by which glucocorticoid hormones and "aging," known to alter MAO activity in vivo, regulated the expression of MAO A and MAO B in cultured human skin fibroblasts. The addition of dexamethasone or hydrocortisone to cultures resulted in a dose- and time-dependent increase in total MAO activity, whereas the removal of hormone from cultures resulted in a time-dependent decrease in activity toward control levels. The response to dexamethasone was affected by culture conditions such as serum concentration, feeding frequency, and cellular "age." Cellular aging, in the absence of hormone, also resulted in increased levels of total MAO activity. The effects of hormones and aging on total MAO activity appeared to be selective for MAO A. The 6- to 14-fold increases in total activity were paralleled by similar increases in the activity and amount of active MAO A but less than 2- to 3-fold increases in the activity and amount of MAO B. Altered synthesis or degradation of the active enzyme appeared to account for the effects of hormones, aging, and various culture conditions on MAO activity. Inhibitor sensitivity, substrate affinity, electrophoretic mobility, and molecular turnover number of either form of the enzyme were not altered during dexamethasone treatment or during cellular aging. However, rates of active MAO synthesis were affected by hormone treatment and feeding frequency, rates of active MAO degradation by serum concentration, and rates of active MAO synthesis or degradation by aging. In summary, we have shown that glucocorticoids and cellular aging selectively affect the amount of MAO A at the level of active enzyme synthesis or degradation. Further, our finding that the expression of the two forms of MAO in human fibroblasts can be independently regulated supports the growing evidence that MAO A and MAO B are separate molecular entities.

Properties of monoamine oxidase in control and Lesch-Nyhan fibroblasts.

Monoamine oxidase activity of the A type was measured in homogenates of cultured human skin fibroblasts. Twenty-four control lines had activities ranging over fifty-fold with an apparent bimodal distribution. Activity in fibroblasts from 20 patients with the Lesch-Nyhan syndrome fell in the low portion of the normal distribution with a mean activity about 50% that of the control mean (p < 0.05). In a subgroup of control and Lesch-Nyhan lines with levels of enzyme activity from 0.9 to 179 pmol/min/mg protein, monoamine oxidase was similar with respect to apparent Km for tryptamine, thermal stability at 56 C, and sensitivity to clorgyline. Thus the lower mean levels of activity observed in the Lesch-Nyhan as compared to control fibroblasts were not associated with other altered properties of the enzyme. The bimodal distribution of enzyme activity suggests that a genetic polymorphism for monoamine oxidase may control levels of activity expressed in fibroblasts.

Inherited levels of A and B types of monoamine oxidase activity.

In establishing the role of inherited variations in levels of monoamine oxidase (MAO) activity in neuropsychiatric diseases, it is important to measure levels of both A and B types of activity as they appear to be under separate genetic control. Levels of A and B types of activity can be evaluated in fibroblasts and platelets, respectively. A number of genes could be involved in determining levels of activity, including those coding for the catalytic and noncatalytic subunits of the enzyme, as well as those coding for enzymes involved in covalent attachment of the flavin cofactor, other processing steps, degradation of MAO, and lipid metabolism. Different genes may be critical in controlling activity levels in various cell types depending on differential expression of the genome. In order to establish the molecular basis of variation in activity, techniques should be employed to assess the structure and conformation of the enzyme, as well as the number of enzyme molecules and their interaction with other cellular components. Only by understanding the genetic and environmental factors controlling levels of A and B types of MAO activity can we hope to evaluate and manipulate the role of MAO in human neurophysiology.

Monoamine oxidase activity decreased in cells lacking hypoxanthine phosphoribosyltransferase activity.

The Lesch-Nyhan syndrome in humans is characterized by lack of hypoxanthine phosphoribosyltransferase activity and neurologic abnormalities that suggest changes in catecholamine metabolism. Monoamine oxidase, which degrades biogenic amines, has decreased activity in noradrenergic murine neuroblastoma cell lines lacking hypoxanthine phosphoribosyltransferase activity and in skin fibroblasts from patients with the Lesch-Nyhan syndrome.