Sf1 steroidogenic factor 1

Despite the importance of family history and HH as potential indicators of X-linked AHC, the prevalence of DAX1 mutations was still 45% (20 of 44) in boys with no family history who were preadolescent (<14 yr) at the time of referral. Furthermore, milder or transient forms of adrenal insufficiency or associated features such as skeletal abnormalities were more likely to be found in the group in whom no DAX1 mutations were identified ( Table 2 ). If these individuals with transient adrenal insufficiency or additional features were excluded from analysis, the percentage of preadolescent boys with no family history who were found to harbor DAX1 mutations rose from 45% (20 of 44) to 68% (19 of 28).

Transient gene expression assays were performed in 96-well plates (Techno Plastic Products, Trasadingen, Switzerland) using tsa201 human embryonic kidney cells or Chinese hamster ovary (CHO) cells, lipofectamine 2000 (Invitrogen, Paisley, UK), and a dual-luciferase reporter assay system (Promega, Southampton, UK) with cotransfection of pRLSV40 Renilla luciferase (Promega) as a marker of transfection efficiency. For analysis of target gene transcriptional activation, pCMXWT or mutant SF1 expression vectors (2 ng/well) were cotransfected into tsa201 cells with reporters containing SF1-responsive minimal promoters (murine Cyp11a , rat Cyp19 , murine Insl3 /relaxin-like factor, and human MIS ) (100 ng/well), as reported previously ( 10 , 17 ). Synergistic activation of the rat LH β promoter was studied using 2 ng pCMXWT or mutant SF together with 2 ng/well of pCMXEgr1 (early growth response 1) ( 18 ). In all studies, cells were lysed 24 h after transfection and luciferase assays performed (dual luciferase reporter assay system; Promega) using a FLUOstar Optima fluorescence microplate reader (BMG Labtech, Aylesbury, UK). All data were standardized for Renilla coexpression. Results are shown as the mean ± sem of at least three independent experiments, each performed in triplicate.

Carey et al. (1993) described families in which the polycystic ovarian syndrome (PCO; 184700 ) and premature male pattern baldness (MPB; 109200 ) segregated as an autosomal dominant phenotype. Carey et al. (1994) studied 14 Caucasian families with 81 affected individuals and identified a -34T-C transition (A1 and A2 alleles, respectively) in the 5-prime promoter region of the CYP17 by heteroduplex analysis. The change created an additional SP1-type (CCACC box) promoter site that was thought to cause increased expression of the gene. The base change also created a recognition site for the restriction enzyme MspA1, allowing a simple screening procedure. There was a significant association between the A2 allele and the affected state for consecutively identified Caucasian women with PCO as compared either to consecutively matched controls or to a random population. Within the 14 families, members with polycystic ovaries or male pattern baldness had a significant association with the occurrence of at least 1 A2 allele compared to their normal relatives. The A2 allele did not cosegregate, however, with the affected phenotype in families showing association, demonstrating that the mutation in CYP17 is not the cause of PCO/MPB. Although variation represented by the A2 allele (-34C) of the CYP17 gene appeared to be a significant factor modifying the expression of PCO/MPB in families in which the phenotype was demonstrated to segregate as a single gene disorder, it was excluded as the primary genetic defect. Nedelcheva Kristensen et al. (1999) showed that the -34T-C polymorphism did not bind to SP1 ( 189906 ).

The regulatory domains of cPKC isoforms (cPKCα: cPKC-alpha; cPKCβI: cPKC-beta I, cPKCβII: cPKC-beta II; and cPKCγ: cPKC-gamma) contain a C1 domain consisting of tandem ~50 amino acid long sequences termed C1A and C1B. The C1A and C1B subdomains each have six cysteines and two histidines that coordinate two Zn 2+ ions. The cPKCβII enzyme is an alternatively spliced version of cPKCβI. The C1A/C1B motifs function as a DAG-/PMA-binding motif (PMA: phorbol myristic acid). The regulatory domains of the cPKC isoforms also contain a C2 domain that binds anionic phospholipids in a calcium-dependent manner. All the cPKC isoforms require DAG, Ca 2+ , and phospholipids for activation.

Sf1 steroidogenic factor 1

sf1 steroidogenic factor 1

The regulatory domains of cPKC isoforms (cPKCα: cPKC-alpha; cPKCβI: cPKC-beta I, cPKCβII: cPKC-beta II; and cPKCγ: cPKC-gamma) contain a C1 domain consisting of tandem ~50 amino acid long sequences termed C1A and C1B. The C1A and C1B subdomains each have six cysteines and two histidines that coordinate two Zn 2+ ions. The cPKCβII enzyme is an alternatively spliced version of cPKCβI. The C1A/C1B motifs function as a DAG-/PMA-binding motif (PMA: phorbol myristic acid). The regulatory domains of the cPKC isoforms also contain a C2 domain that binds anionic phospholipids in a calcium-dependent manner. All the cPKC isoforms require DAG, Ca 2+ , and phospholipids for activation.

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